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LT and CT in parenteral immunization methods against helicobacter infection This invention provides methods of inducing a protective or therapeutic immune response to Helicobacter infection in a mammal by parenterally administering to the mammal one or more Helicobacter antigens and an adjuvant selected from one or more of LT, CT, LTB, and CTB.
Primary Examiner: Smith; Lynette R. F. Assistant Examiner: Portner; Ginny Allen Attorney, Agent or Firm: This is a continuation-in-part of U.S. Ser. No. 09/100,258, filed Jun. 19, 1998. What is claimed is: 1. A method of inducing an immune response to Helicobacter in a mammal, said method comprising administering to said mammal by injection (a) an immunogenic Helicobacter pylori polypeptide that is admixed with (b) an adjuvant comprising immunogenic Helicobacter pylori polypeptide that is admixed with (b) an adjuvant comprising one or more of (i) heat-labile toxin of Escherichia coli, (ii) the B subunit of the heat-labile toxin of Escherichia coli, (iii) cholera toxin, and (iv) the B subunit of cholera toxin. 2. The method of claim 1, wherein the polypeptide and the adjuvant are provided together in a solution. 3. The method of claim 1, wherein the polypeptide comprises Helicobacter pylori urease or a subunit or immunogenic fragment thereof. 4. The method of claim 1, wherein the heat-labile toxin of Escherichia coli and the B subunit of the heat-labile toxin of Escherichia coli are administered to said mammal. 5. The method of claim 1, wherein said injection is subcutaneous. 6. The method of claim 1, wherein said injection is intradermal. 7. The method of claim 1, wherein said Helicobacter pyloripolypeptide comprises catalase or an immunogenic fragment thereof. 8. The method of claim 1, wherein said Helicobacter pylori polypeptide comprises a polypeptide selected from the group consisting of HspA, HspB, lactoferrin receptor, p76 (SEQ ID NOs:1-22), p32 (SEQ ID NOs:23 and 24), BabA, BabB, AlpA, AlpB, and immunogenic fragments thereof. 9. The method of claim 1, further comprising administering to said mammal one or more additional immunogenic Helicobacter pylori polypeptides. 10. The method of claim 9, wherein said Helicobacter pylori polypeptide is urease and said one or more additional Helicobacter pylori polypeptides is selected from the group consisting of catalase, HspA, HspB, lactoferrin receptor, p76 (SEQ ID NOs:1-22), p32 (SEQ ID NOs:23 and 24), BabA, BabB, AlpA, AlpB, and immunogenic fragments thereof. 11. The method of claim 1, wherein said Helicobacter pylori polypeptide comprises a subunit of Helicobacter pylori urease. 12. The method of claim 1, wherein said Helicobacter pylori polypeptide comprises Helicobacter pylori catalase. 13. The method of claim 1, wherein said Helicobacter pylori polypeptide comprises a Helicobacter pylori polypeptide selected from the group consisting of catalase, HspA, HspB, lactoferrin receptor, p76 (SEQ ID NOs:1-22), p32 (SEQ ID NOs:23 and 24), BabA, BabB, AlpA, and AlpB. 14. A method of inducing a protective or therapeutic immune response to Helicobacter infection in a mammal, said method comprising administering to said mammal by injection (a) a polypeptide comprising a subunit of Helicobacter pylori urease that is admixed with (b) an adjuvant comprising one or more of (i) heat-labile toxin of Escherichia coli, (ii) the B subunit of the heat-labile toxin of Escherichia coli, (iii) cholera toxin, and (iv) the B subunit of cholera toxin. BACKGROUND OF THE INVENTION This invention relates to methods of immunizing against Helicobacter infection. Cholera toxin (CT) and the heat-labile-enterotoxin of E. coli (LT) are commonly used as immunological adjuvants for mucosal immunization. The non-toxic B subunit of LT (LTB) has also been shown to have mucosal immunomodulating activity. When delivered mucosally with urease or other Helicobacter antigens, LT and CT each induce immune responses that protect mice against infection with Helicobacter pylori. Xu-Amano et al. (J. Exp. Med. 178:1309-1320, 1993) showed that mice develop specific serum IgM and IgG (but not IgA) responses following intraperitoneal immunization with tetanus toxin (TT) plus CT. TT alone gave low responses. Hornquist, et al. (Eur. J. Immunol. 23:2136-2143, 1993) showed that CT promotes priming of CD4+ T cells when delivered intravenously with Keyhole Limpet Hemocyanin (KLH). Marinaro et al. (J. Immunol. 155:4621-4629, 1995) showed that CT stimulates production of serum IgE to TT when the antigen and adjuvant are delivered subcutaneously. SUMMARY OF THE INVENTION We have discovered that parenterally delivered LT and LTB are effective adjuvants that enhance the immunoprotective effect of Helicobacter antigens, such as urease. We have also discovered that LT+LTB gives better results that LT alone. Accordingly, the invention provides methods of inducing a protective or therapeutic immune response to Helicobacter infection in a mammal, in which (a) a Helicobacter antigen, and (b) an adjuvant including one or more of (i) LT, (ii) LTB, (iii) CT, and (iv) CTB (e.g., LT+LTB) is parenterally (e.g., subcutaneously, intradermally, intramuscularly, or intravenously) administered to a mammal. The antigen and the adjuvant can be provided together in a solution, or separately. The antigen can be urease or a subunit, enzymatically inactivate derivative, or fragment thereof. The antigen can also be catalase, HspA, HspB, lactoferrin receptor, p76 (SEQ ID NOs:1-22), p32 (SEQ ID NOs:23 and 24), BabA, BabB, AlpA, AlpB, or an immunogenic fragment or derivative thereof. The methods of the invention also include the administration of more than one Helicobacter antigen. The invention provides several advantages. For example, parenteral delivery of LT is advantageous in that the toxin does not contact the intestinal epithelial cells, and thus does not cause diarrhea. Also, the toxicity of parenterally administered LT we observed was limited to injection site swelling, and we observed no toxicity with LTB at high doses (see below), which matched the effectiveness of LT in augmenting protective immunity. Also, our observation of the heightened effect of parenterally administering LT (low dose)+LTB (high dose) minimizes the possibility of any potential side effects. Other features and advantages of the invention are apparent from the following detailed description, the drawings, and the claims. BRIEF DESCRIPTION OF THE DRAWINGS FIG. 1 is a graph showing gastric urease activity measured under treatment and control conditions. Urease activity in samples of mouse stomach tissue was determined by a calorimetric assay. Individual A.sub.550 values for each mouse (triangles) are shown along with the median value for each group (lines). (See below for further details.) FIG. 2 is a graph showing quantitative culture measurements made under treatment and control conditions. Samples of mouse stomach tissue were homogenized and cultured to determine the number of colony-forming units (CFU) per sample. Individual counts for each mouse (circles) are shown along with the median for each group (lines). (See below for further details.) FIG. 3 is a graph showing anti-urease serum IgG measurements made under treatment and control conditions. Post-immunization sera were tested for IgG antibody against urease by ELISA. IgG levels in ELISA units (EU) per ml for individual mice are shown. FIG. 4 is a graph showing anti-urease salivary IgA measurements made under treatment and control conditions. Post-immunization saliva samples were diluted 1:10 and tested for IgA antibody against urease by ELISA. A.sub.405 values for individual mice are shown. FIG. 5 is a graph showing gastric H. pylori colonization in mice following oral or subcutaneous immunization with urease alone or mixed with LT or LTB. Mice were either unimmunized (no treatment) or immunized 3 times with urease plus the adjuvants shown and challenged with H. pylori orally 2 weeks after the final immunization. For oral immunization, 25 .mu.g of urease was delivered with 1 .mu.g of LT. For subcutaneous immunization, 10 .mu.g urease was delivered with the dose of adjuvant shown. Symbols show the CFU per quarter antrum of individual mice. The horizontal lines show the median for each group. FIG. 6 is a graph showing titers of IgG to urease in sera of immunized mice. Mice were immunized 3 times orally or subcutaneously with urease plus the adjuvants shown. Serum was collected 1 week after the final immunization and. tested for urease-specific IgG by ELISA. Endpoint titers for individual mice are shown. Samples in which no specific antibody was detected were assigned a titer of 50. The horizontal lines show the median titer for each group. FIG. 7 is a graph showing IgE to urease in sera of immunized mice. Mice were immunized 3 times orally or subcutaneously with urease plus the adjuvants shown. Serum was collected 1 week after the final immunization and tested for urease-specific IgE at a 1/100 dilution by ELISA. Absorbance values for individual mice are shown. The horizontal lines show the median value for each group. FIG. 8 is a graph showing IgA to urease in saliva samples of immunized mice. Mice were immunized 3 times orally or subcutaneously with urease plus the adjuvants shown. Saliva was collected 1 week after the final immunization and tested for urease-specific IgA at a 1/10 dilution by ELISA. Absorbance values for individual mice are shown. The horizontal lines show the median value for each group. FIG. 9 is a graph showing urease-specific IgE in serum and IgA in saliva of mice immunized 3 times subcutaneously with urease adsorbed to alum adjuvant. Serum and saliva were collected 1 week after the final immunization and tested for urease-specific antibody by ELISA. Absorbance values for individual mice are shown. The horizontal lines show the median value for each group. FIG. 10 is a graph showing gastric urease activity measured under treatment and control conditions. Urease activity in samples of mouse stomach tissue was determined by a calorimetric assay. Individual A.sub.550 values for each mouse (circles) are shown along with the median value for each group (lines). (See below for further details.) FIG. 11 is a graph showing quantitative culture measurements made under treatment and control conditions. Samples of mouse stomach tissue were homogenized and cultured to determine the number of colony-forming units (CFU) per sample. Individual counts for each mouse (circles) are shown along with the median for each group (lines). (See below for further details.) DETAILED DESCRIPTION The methods and compositions of the invention employ several components and techniques, which are described in greater detail as follows. Antigens Preferred antigens for use in the invention are Helicobacter (e.g., H. pylori or H. felis) proteins or other components (e.g., lipopolysaccharides or carbohydrates) that either are purified from bacterial cultures or are produced using standard recombinant or chemical synthetic methods. Preferred antigens are proteins or portions of proteins (i.e., peptides or polypeptides). Methods for identifying immunogenic fragments of polypeptide antigens are known in the art, and can be employed in preparing antigens for use in the methods of the invention (Sturniolo et al., Nature Biotechnology, "Generation of Tissue-Specific and Promiscuous HLA Ligand Databases Using DNA Microarrays and Virtual HLA Class II Matrices," June 1999). Additional antigens that can be used in the invention are whole bacteria and non-purified protein preparations, such as Helicobacter lysates. The antigens used in the invention can be produced as fusion proteins, i.e., polypeptides containing amino acid sequences corresponding to two or more proteins (or fragments thereof), which are normally separate proteins, linked together by a peptide bond(s). Fusion proteins generally are synthesized by expression of a hybrid gene containing nucleotides encoding each of the individual polypeptides that make up the fusion protein. An example of an antigenic fusion protein included in the invention is one that contains a CT or an LT toxin adjuvant (e.g., toxin A or B subunit, or a fragment or derivative thereof having adjuvant activity) fused to an H. pylori antigen, e.g., urease. Another type of fusion protein included in the invention consists of an antigen fused to a polypeptide (e.g., glutathione S-transferase (GST)) that facilitates purification of the fusion protein. Proteins used as antigens in the invention can also be covalently coupled or chemically cross-linked to adjuvants using standard methods. The most preferred H. pylori antigens for use in the invention are urease and derivatives thereof. Most preferred are enzymatically inactive, recombinant multimeric urease complexes, produced as described in Lee et al., WO 96/33732, which is hereby incorporated by reference. A number of other immunogenic H. pylori antigens can also be administered according to the invention, e.g., catalase (WO 95/27506), HspA and HspB (WO 94/26901), lactoferrin receptor (WO 97/13784), p76 (SEQ ID NOs:1-22; WO 97/12908), p32 (SEQ ID NOs:23 and 24; WO 97/12909), BabA and BabB (WO 97/47646), AlpA (WO 96/41880), AlpB (WO 97/11182), as well as the antigens described in WO 96/38475, WO 96/40893, WO 97/19098, WO 97/37044, and WO 98/18323. The immunogenic antigens can be used alone (with the adjuvant) or in "cocktails" of two or more antigens. LT and CT Adjuvants Any of the known LT or CT adjuvants or variants thereof can be used in the invention. Although the native form can be used (see, e.g., Clements et al., Vaccine 6:269, 1988), and exhibits strong adjuvant activity, it is somewhat toxic, and therefore less toxic mutants are preferred. Several such mutants, having demonstrated adjuvant activity, are described in WO 93/13202, WO 95/17211, and WO 96/06627, which are hereby incorporated by reference. The low-toxicity B subunit (LTB), described in U.S. Pat. Nos. 5,308,835, 5,079,165, 4,808,700, and 5,182,109, which are hereby incorporated by reference, is also efficacious. The invention can also employ LT or CT toxoids as adjuvants. A toxoid is a toxin that has been treated so as to destroy or decrease its toxic properties, but to retain adjuvant activity. Toxoids included in the invention are made using standard methods including, but not limited to, chemical (e.g., formaldehyde or glutaraldehyde) treatment, protease cleavage, and recombinant methods (e.g., by making fragments or mutations (e.g., point mutations) of the toxin(s)). DNA encoding LT or CT toxin subunit or toxoid in an appropriate expression vector can also be used. CT and LT are further described, for example, by Spangler (Microbiological Reviews 56(4):622-647, 1992). Vaccine Formulation Generally, the H. pylori antigen(s) and adjuvant are admixed together in a pharmaceutically acceptable carrier, e.g., water, saline, or phosphate-buffered saline. The concentration of H. pylori antigen in the composition preferably is between 10 .mu.g and 1 mg, advantageously from 25 .mu.g to 500 .mu.g, preferably from 50 .mu.g to 200 .mu.g, and most preferably a single dose contains about 100 .mu.g antigen. The concentration of LT or CT adjuvant in the composition preferably is between 1 .mu.g and 100 .mu.g, and the concentration of LTB or CTB subunit or toxoid is preferably between 1 .mu.g and 1 .mu.g, for example, between 10 .mu.g and 50 .mu.g. Administration The compositions of the invention are administered parenterally; i.e., the composition is injected subcutaneously, intramuscularly, intravenously, intradermally, or by any other non-mucosal modality. The LT or CT adjuvant can be administered in an encapsulated form or in an unencapsulated form (i.e., in solution). The methods of the invention can be used both for treatment and prevention of H. pylori infection. For prevention, the composition is injected into the patient at intervals of one week to six months for a period of between one and six months, at a dosage of 0.05 to 5 mg/kg H. pylori antigen. Where the patient has an H. pylori infection that is to be treated, injections at intervals of one week to six months, for one to six months, are administered, for 0.05 to 5 mg/kg H. pyloriantigen. Antibiotics can be administered as an adjunct to the immunotherapy of the invention. The following experimental results support the methods of the present invention. Results Characterization of recombinant LT and LTB. LT and LTB were tested for toxicity using a Y-1 cell-rounding assay (Chapman et al., J. Med. Microbiol. 18:399-403, 1984). LT was tested before and after treatment with trypsin, which activates the toxin by cleavage of the A subunit. The dose of untreated LT required for 50% cell rounding (ED50) was 0.2 ng/ml. Following trypsin treatment, the ED50 fell to 0.1 ng/ml, indicating that approximately 50% of the LT was active prior to trypsin treatment. LTB had no activity in the assay when tested at concentrations up to 100 .mu.g/ml. Adjuvant effects of parenterally delivered LT and LTB for protection against H. pylori challenge. Mice were immunized subcutaneously or intradermally with 10 .mu.g of H. pylori urease mixed with 5 ng to 5 .mu.g of recombinant LT or 5 .mu.g to 50 .mu.g of recombinant LTB (see Table 1). As a positive control, mice were immunized orally or intragastrically with 25 .mu.g of urease plus 1 .mu.g LT, a regimen shown previously to protect against H. pylori challenge (Ermak et al., J. Exp. Med. 188:2277-2288, 1998). A schedule of 3 immunizations, with a two-week interval between doses was used. Mice injected subcutaneously with the two higher doses of LT (0.5 and 5 .mu.g) developed swelling at the injection site that was still present two weeks after the first immunization. As a result, the second dose was omitted in these 2 groups and a single boosting immunization was given 4 weeks after the first dose, at which point the swelling had subsided. Injection site swelling consisted of a raised area approximately 1 cm in diameter with no skin color change or necrosis apparent. No other signs of toxicity were observed. Mice injected intradermally with 0.5 or 5 .mu.g of LT also experienced injection site swelling. Because swelling did not subside as quickly in these mice, further immunization was not performed and the mice were removed from the study. Two weeks after the final immunization, mice were challenged intragastrically with mouse-adapted H. pylori strain X47-2AL. Gastric colonization was assessed two weeks after challenge by determining urease activity and bacterial CFU. Gastric urease activity results are shown in FIG. 1. A.sub.550 values for individual mice and the median for each group are shown. Some groups contain fewer than 10 data points, due to a technical problem with the assay. Mice in the unimmunized group were clearly infected (A.sub.550.gtoreq.0.20), with a median A.sub.550 of 0.67. Mice immunized intragastrically with urease plus LT (positive control) had a median A.sub.550 of 0.21, with substantial reductions in gastric H. pylori colonization in all mice. A similar effect was seen in mice immunized subcutaneously with urease plus LT at the two highest doses (5 and 0.5 .mu.g). The lower doses of LT (50 and 5 ng) were somewhat less effective. Intradermal immunization with urease and LT result in similar levels of protection. Subcutaneous immunization with urease plus 50 .mu.g LTB resulted in the lowest median A.sub.550 value of any of the groups. Results of quantitative culture of gastric tissue mirrored those of the urease assay (FIG. 2). The highest subcutaneous doses of LT and LTB resulted in a level of protection equal to that afforded by intragastric immunization. Lower doses had lesser effects. More specifically, the median level of gastric H. pylori colonization in unimmunized mice was 2.9.times.10.sup.5 CFU/stomach sample (FIG. 2). In mice immunized orally with urease plus LT, the median level was 9.1.times.10.sup.3 CFU/sample, a significant reduction in colonization (P=0.0004) that was consistent with previous experiments using the X47-2AL challenge strain (26, 38). Subcutaneous delivery of urease with the highest dose of LT (5 .mu.g) was as effective at reducing infection as oral immunization, resulting in a significantly reduced median H. pylori level of 8.3.times.10.sup.3 CFU/sample (FIG. 2). Subcutaneous delivery of urease with lower doses of LT reduced gastric colonization to a lesser, but significant (P<0.05) extent. Intradermal injection of urease with 5 ng or 50 ng of LT was similar in effectiveness to subcutaneous delivery of the same doses. Subcutaneous delivery of urease with 50 .mu.g of LTB reduced the median level of H. pylori to 3.2.times.10.sup.3 CFU/sample, the lowest level in any of the groups. A lesser but significant effect (P=0.0006) was seen when only 5 .mu.g of LTB was used. All mice developed IgG to urease in serum following immunization (FIG. 3). Responses in parenterally immunized mice were higher than those of intragastrically immunized mice. In groups receiving LT parenterally, there was a trend towards lower IgG responses with lower doses. Mice immunized with urease plus LTB had somewhat lower responses than mice immunized with urease plus LT. Salivary IgA to urease was highest in the intragastrically immunized group, although 3 of 10 mice did not respond (FIG. 4). Other immunized groups had a range of IgA responses. In mice immunized with urease plus LT subcutaneously, the highest responders were in the groups treated with the two lowest doses of LT (50 and 5 ng). Intradermal immunization with urease plus 50 or 5 ng LT stimulated salivary IgA in most mice. LTB immunization resulted in IgA responses primarily in the lower dose group. The results show that mucosally or parenterally delivered LT acts as an effective adjuvant for immunization of mice against H. pylori infection. Surprisingly, parenteral LT stimulated a secretory IgA response against urease. In previous experiments, we found that subcutaneous injection of urease, alone or adsorbed to alum adjuvant, elicited little or no salivary IgA response. Adjuvant effects of orally delivered LTB and parenterally delivered LT-LTB mixture. A second experiment, using the same immunization schedule and challenge procedure as described above, was designed to examine several questions regarding the adjuvant activities of LT and LTB with urease, including whether LTB was active orally, whether subcutaneously delivered urease was protective without LT or LTB, and whether a combination of LT and LTB was more effective than either molecule alone. As shown in FIG. 5, oral delivery of urease plus 1 .mu.g LT reduced gastric colonization to a median level of 1.5.times.10.sup.4 CFU/sample from a median of 7.9.times.10.sup.4 CFU/sample in untreated mice (P=0.02). Oral delivery of urease with 50 .mu.g of LTB, however, had no effect on colonization (P=0.82). Subcutaneous immunization with urease alone reduced the median H. pylori level slightly from that of unimmunized mice (P=0.02) and addition of LT or LTB enhanced the protective effect (P.ltoreq.0.01). As in the previous experiment, LTB was more effective at the higher dose (50 .mu.g) than at the lower dose (5 .mu.g). Administration of 50 .mu.g of LTB in the absence of urease had no effect on colonization. The greatest effect was seen when a mixture of 50 .mu.g LTB and 10 ng LT was used as adjuvant for subcutaneous immunization. In this group, colonization was reduced to 2.1.times.10.sup.3 CFU/sample (P=0.0002). Antibody responses to urease following parenteral delivery of urease with LT or LTB adjuvants. Serum and saliva collected after immunization, but before H. pylori challenge, were examined to determine the effects of different adjuvants and routes of immunization on the magnitude and type of antibodies elicited against urease. IgG to urease was not detected in the serum of unimmunized mice when tested at a 1/100 dilution. Oral immunization with urease plus LT elicited low to moderate titers of urease-specific IgG (FIG. 6). IgG titers were similar when mice were immunized orally using LTB as adjuvant. In serum from subcutaneously immunized mice, IgG levels in all groups were higher than those obtained with oral immunization and responses were more uniform within each group. Subcutaneous immunization with urease alone resulted in IgG titers of greater than 5 log.sub.10, while the addition of LT or LTB increased titers several fold (P=0.06 and P<0.005, respectively, comparing the LT and LTB groups against the no-adjuvant group). As with protection, co-administration of LT and LTB had an additive effect, resulting in a urease-specific IgG titer of 6.9 log.sub.10, a 20-fold increase over the median titer in mice immunized with urease in the absence of adjuvant (P=0.002). Analysis of serum IgG1 and IgG2a levels showed differences in the quality of the urease-specific IgG response among different groups (Table 2). In comparison to subcutaneous immunization, oral immunization tended to elicit lower levels of both IgG1 and IgG2a and a lower IgG1/IgG2a ratio, whether LT or LTB was delivered with urease. In contrast, subcutaneous LT and LTB elicited IgG responses to urease that were qualitatively different from each other. Subcutaneous delivery of urease alone elicited strong IgG1 and IgG2a responses, and the levels of both isotypes were enhanced by addition of LT or LTB. However, LT stimulated a greater increase in IgG1 than in IgG2a, while LTB stimulated a greater increase in IgG2a than in IgG1. When LT and LTB were delivered together, the effect of LTB appeared to be dominant, since the median IgG2a titer of 6.7 log.sub.10, was nearly 80-fold higher than that of mice receiving urease without adjuvant and the highest of any group. Serum IgE to urease was generated only by parenteral immunization (FIG. 7). Subcutaneous immunization with urease alone stimulated a low level IgE response in most mice. The addition of LT adjuvant increased IgE levels, although responses were highly variable. The median IgE response in mice receiving LTB adjuvant was only slightly higher than that of mice receiving no adjuvant. LT and LTB together led to levels that were somewhat higher than those seen with LTB alone. IgA to urease in saliva was greatest when mice were immunized orally and LT adjuvant was used, although not all mice had a detectable IgA response (FIG. 8). Delivery of urease orally with LTB or subcutaneously without adjuvant stimulated only low levels of specific IgA in saliva. LT stimulated low levels of specific IgA in the saliva of most mice when delivered subcutaneously with urease, while LTB had a similar effect but also induced moderate levels of salivary IgA in several mice. When LT and LTB were delivered together, specific salivary IgA was not increased over the level seen when mice were immunized with urease alone. Antibody responses to urease following parenteral delivery of urease with alum adjuvant. To compare the adjuvant activities of LT and LTB with a more conventional parenteral adjuvant, mice were immunized subcutaneously with urease adsorbed to alum (aluminum hydroxide) adjuvant. As in the experiments described above, mice were immunized 3 times and blood and saliva were collected 1 week after the final immunization. This regimen was shown previously to reduce colonization of the stomach following H. pylori challenge, but was less effective than oral immunization with urease plus LT (Ermak et al., J. Exp. Med. 188:2277-2288, 1998). The titer of specific IgG in serum following immunization with urease adsorbed to alum ranged from 5.7 to 7.1 log.sub.10, with a median of 6.3 log.sub.10. This was the same approximate level of serum IgG elicited by subcutaneous delivery of urease plus LT or LTB. The median titers of IgG1 and IgG2a in serum following urease plus alum immunization were 6.6 and 5.5, respectively (Table 2). IgG1/IgG2a ratios were relatively high, ranging from 3.9 to 53.2. This range was similar to that obtained with subcutaneous delivery of urease alone or with LT. IgE levels were higher with alum than with LT or LTB as adjuvant, with A.sub.405 values for urease-specific IgE exceeding 2.0 in over half of the mice that received alum (FIG. 9). Only slight salivary IgA responses were stimulated with alum as adjuvant (FIG. 9). Additional data supporting these findings is shown in FIGS. 10 and 11. In these experiments, groups of 10 mice each were immunized on days 0, 14, and 28, as follows: no antigen, no adjuvant (group 1); 25 .mu.g urease, 1 .mu.g LT, orally (group 2); 25 .mu.g urease, 50 .mu.g LTB, orally (group 3); 10 .mu.g urease, no adjuvant, s.c. (group 4); 10 .mu.g urease, 10 ng LT, s.c. (group 5); 10 .mu.g urease, 5 .mu.g LTB, s.c.(group 6); 10 .mu.g urease, 50 .mu.g LTB, s.c. (group 7); 10 .mu.g urease, 10 ng LT, 50 .mu.g LTB, s.c. (group 8); and no antigen, 50 .mu.g LTB, s.c. (group 9). The groups were challenged with 1.times.10.sup.7 H. pylori CFU at day 42. At day 56, mice were sacrificed and the gastric colonization was assessed by testing stomach samples for urease activity (Jatrow test) and H. pylori culture. As is shown in FIGS. 10 and 11, 10 ng LT and 50 .mu.g LTB given subcutaneously with urease (groups 5 and 7) similarly lead to a significant reduction of the infection rate, compared to controls (groups 1 and 9). These results are as good as those obtained with urease +1 .mu.g LT given orally (group 5); 10 ng LT +50 .mu.g LTB (group 7), give even better results. The results described above were obtained using the following materials and methods. Materials and Methods Antigens and adjuvants. Recombinant H. pylori urease was expressed in E. coli strain ORV214 and purified by anion-exchange and gel filtration chromatography as described previously (Lee et al., J. Infect. Dis. 172:161-172, 1995). Endotoxin concentration, as determined by the Limulus amoebocyte lysate assay, was reduced to 1.5 ng/mg urease using a Sartobind matrix (Sartorius Corporation, N.Y.). Recombinant LT was obtained from Berna Products Corp. (Coral Gables, Fla.). For trypsin cleavage, 100 .mu.g of LT was mixed with 1 .mu.g of bovine pancreas trypsin (Sigma Chemical Co., St. Louis, Mo.) in 200 .mu.l phosphate buffered saline (PBS) and incubated for 60 minutes at 37.degree. C. Enzymatic activity was stopped by addition of 100 .mu.g of soybean trypsin inhibitor (Sigma). Recombinant LTB was cloned and expressed in E. coli. B subunit was purified from lysates by galactose affinity chromatography which yielded a product consisting of greater than 90% pentameric LTB. Endotoxin was removed using a Sartobind matrix. Purified LTB was lyophilized and stored. Y-1 cell rounding assay. Toxicity of LT and LTB was assessed with a modified cell rounding assay (Chapman et al., J. Med. Microbiol. 18:399-403, 1984). In brief, 96-well flat bottom tissue culture plates were seeded with Y-1 mouse adrenal cells at 2.times.10.sup.4 cells/well in minimum essential medium supplemented with 10% fetal bovine serum. Following incubation at 37.degree. C. in 5% CO.sub.2 for .gtoreq.2 hours to allow spreading of cells on the substrate, medium was removed from wells and replaced with medium containing serial two-fold dilutions of LT or LTB and plates returned to the incubator. After overnight incubation at 37.degree. C., the cells were viewed with an inverted microscope. The toxin potency was defined as the lowest concentration at which .gtoreq.50% of cells were rounded (50% effective dose or ED50). Immunization and sampling. Procedures involving animals were approved by the Institutional Animal Care and Use Committee of OraVax, Inc. Specific pathogen-free, 6 to 8 week-old female Swiss-Webster mice were purchased from Taconic Laboratories (Germantown, N.Y.). Mice were immunized with urease via the oral, subcutaneous or intradermal routes. Three doses were given with a 2-week interval between doses. For oral immunization, 25 .mu.g of urease and 1 .mu.g of LT in a volume of 25 .mu.l was pipetted into the mouth. For subcutaneous immunization, 10 .mu.g of urease was injected in the lower back, with or without LT, LTB or aluminum hydroxide (alum) adjuvant, in a volume of 100 .mu.l. Equal volumes of alum (Rehydragel, Reheis, Inc., Berkeley Heights N.J.) at 2 mg/ml and urease at 100 .mu.g/ml were mixed 30-60 minutes prior to injection. For intradermal immunization, a patch of skin on the back was shaved, the mice were anesthetized by isoflurane inhalation, and 10 .mu.g urease with LT or LTB adjuvant was delivered via a 30 gauge needle in a volume of 50 .mu.l. Blood and saliva were sampled approximately 1 week after the third immunization. Blood was collected from the retro-orbital sinus while mice were under isoflurane inhalation anesthesia, and saliva was collected from the mouth with a micropipette after intraperitoneal injection of 70-100 .mu.g of pilocarpine. Challenge and analysis of colonization. Approximately 2 weeks after the final immunization, mice were challenged intragastrically with a single dose of 1.times.10.sup.7 live streptomycin-resistant H. pylori strain X47-2AL (Kleanthous et al., Infect. & Immun. 66:2879-2886, 1998). Challenge bacteria were grown first on Mueller-Hinton agar plates containing 10% sheep blood and transferred to Brucella broth as described previously (Kleanthous et al., Infect. & Immun. 66:2879-2886, 1998). The challenge dose was delivered intragastrically in a volume of 100 .mu.l using a blunt-tipped feeding needle. Mice were sacrificed 2 weeks after challenge to assess gastric colonization by H. pylori. The stomach was removed, rinsed with 0.9% NaCl solution, and cut open along the lesser and greater curvatures. One quarter of the antrum was placed into 1 ml of Brucella broth supplemented with 5% calf serum and disrupted using a Dounce homogenizer fitted with a loose pestle. Tenfold dilutions of homogenate were inoculated onto Mueller-Hinton agar containing 10% sheep blood, 5 .mu.g/ml amphotericin B, 5 .mu.g/ml trimethoprim, 10 .mu.g/ml vancomycin, 10 U/ml polymyxin B sulfate, and 50 .mu.g/ml streptomycin. Plates were incubated at 37.degree. C. in 7% CO.sub.2 and colonies counted 5-7 days later. Antibody analysis. Antibody responses in serum and saliva were measured by enzyme-linked immunosorbent assay (ELISA). Flat-bottom 96-well plates were coated overnight at 4.degree. C. with 0.5 .mu.g urease per well in 100 .mu.l of 0.1 M carbonate buffer, pH 9.6. Wells were washed with PBS containing 0.05% Tween 20 (PBS-Tween), and PBS-Tween containing 2.5% nonfat dry milk (blocking buffer) was added to block nonspecific binding. Blocking buffer was used as diluent for test samples and antibody conjugates. Samples and reagents were added to wells in 100 .mu.l volumes and wells were washed with PBS-Tween between steps. For IgG, IgG1, and IgG2a determination, serum was diluted 1/100 and then further diluted with a series of five-fold dilutions. After removing blocking buffer, 100 .mu.l of each dilution was added in duplicate and plates were incubated for 60 minutes at 28.degree. C. Biotin-conjugated goat anti-mouse IgG, IgG1, or IgG2a antibodies (Southern Biotechnology Associates, Birmingham Ala.), each diluted 1/1000, were added to wells next and plates were incubated for. 60 minutes at 28.degree. C. Streptavidin-alkaline phosphatase (Calbiochem, La Jolla Calif.) diluted 1/500 was added next and plates were incubated for 30 minutes at 28.degree. C. For the final step, 100 .mu.l of 1 mg/ml p-nitrophenyl phosphate substrate (Sigma) in 1 M diethanolamine buffer, pH 9.6 containing 5 mM MgCl.sub.2 was added. Plates were incubated for 20 minutes at room temperature and the A.sub.405 read with a Vmax microplate reader (Molecular Devices, Menlo Park, Calif.). The average absorbance value of duplicate wells was plotted and a curve was fit to the data points using the power function of Cricket Graph III software (Computer Associates International, Inc., Islandia N.Y.) running on an Apple Macintosh computer. The titer of each sample was defined as the reciprocal of the dilution corresponding to an A.sub.405 of 0.1, which was approximately 3 times the background absorbance for normal mouse serum at a 1/100 dilution. Samples with an A.sub.405 less than 0.1 at a 1/100 dilution were assigned a titer of 50. For determination of salivary IgA levels, saliva was tested at a single dilution of 1/10 and the results are reported as the average A.sub.405 for duplicate wells. The assay procedure for IgA determination was otherwise as described above except that goat anti-mouse IgA biotin conjugate (Southern Biotechnology) was used to detect bound salivary IgA antibodies. For quantitation of IgE to urease, a capture ELISA was used. Flat-bottom 96-well plates were coated overnight with 100 .mu.l of rat monoclonal antibody clone 23G3 against mouse IgE (Southern Biotech) at a concentration of 1 .mu./ml. Wells were washed and blocked with nonfat milk as described above and 100 .mu.l of mouse serum, diluted 1/100 was added to wells in duplicate. Following incubation for 1 hour at 28.degree. C., the plates were washed and urease, at 2.5 .mu.g/ml, was added to wells. Plates were again incubated for 1 hour at 28.degree. C. In subsequent steps, wells were treated with rabbit anti-urease diluted 1/4000 and goat anti-rabbit IgG conjugated to alkaline phosphatase at a 1/2000 dilution. Plates were incubated for 1 hour at 28.degree. C. at each step. Addition of substrate solution and measurement of absorbance was done as described above. TABLE 1 Immunization protocol Urease Adjuvant Delivery Delivery Group dose Adjuvant dose route schedule 1 none none -- -- -- 2 25 .mu.g LT 1 .mu.g i.g. days 0, 14, 28 3 10 .mu.g LT 5 .mu.g s.c. days 0, 28 4 10 .mu.g LT 0.5 .mu.g s.c. days 0, 28 5 10 .mu.g LT 50 ng s.c. days 0, 14, 28 6 10 .mu.g LT 5 ng s.c. days 0, 14, 28 7 10 .mu.g LT 50 ng i.d. days 0, 14, 28 8 10 .mu.g LT 5 ng i.d. days 0, 14, 28 9 10 .mu.g LTB 50 .mu.g s.c. days 0, 14, 28 10 10 .mu.g LTB 5 .mu.g s.c. days 0, 14, 28 TABLE 2 Serum IgG1 and IgG2a antibody responses following immunization with urease alone or urease with LT, LTB, or alum adjuvants. Median log.sub.10 titer (range).sup.a IgG1/IgG2a ratio Adjuvant Antigen Route.sup.b IgG1 IgG2a (range).sup.c 1 .mu.g LT 25 .mu.g urease oral 3.1 (1.7-4.5) 4.3 (1.7-5.2) 0.2 (0.01-1.6) 50 .mu.g LTB 25 .mu.g urease oral 2.2 (1.7-4.7) 3.5 (1.7-4.5) 0.03 (0.01-5.2) None 10 .mu.g urease s.c. 5.7 (5.5-6.3) 4.8 (3.9-5.4) 8.3 (3.9-56.7) 10 ng LT 10 .mu.g urease s.c. 6.7 (6.3-7.2) 5.3 (4.7-6.1) 30.1 (1.9-257.7) 5 .mu.g LTB 10 .mu.g urease s.c. 6.3 (5.8-6.8) 5.8 (5.2-6.4) 4.7 (0.2-8.0) 50 .mu.g LTB 10 .mu.g urease s.c. 6.5 (6.0-6.9) 6.2 (5.5-6.5) 2.1 (0.7-5.8) 10 ng LT + 10 .mu.g urease s.c. 6.8 (6.2-7.2) 6.7 (6.2-6.9) 1.0 (0.6-4.0) 50 .mu.g LTB Alum 10 .mu.g urease s.c. 6.6 (6.0-7.0) 5.5 (4.8-5.8) 11.8 (3.9-53.2) .sup.a Titers ofurease-specific IgG1 and IgG2a were determined by ELISA. Titers are defined as 1/dilution of serum giving an A.sub.405 of 0.1. Samples that were negative at the lowest dilution tested (1/100) were assigned a titer of 50 (1.7 log.sub.10). .sup.b Adjuvant and antigen were mixed and delivered by the oral or subcutaneous (s.c.) routes. All publications and patent applications mentioned herein are incorporated by reference. Other embodiments are within the following claims. SEQUENCE LISTING <100> GENERAL INFORMATION: <160> NUMBER OF SEQ ID NOS: 24 <200> SEQUENCE CHARACTERISTICS: <210> SEQ ID NO 1 <211> LENGTH: 2798 <212> TYPE: DNA <213> ORGANISM: Helicobacter pylori <220> FEATURE: <221> NAME/KEY: CDS <222> LOCATION: (328)...(2451) <220> FEATURE: <221> NAME/KEY: sig_peptide <222> LOCATION: (328)...(385) <400> SEQUENCE: 1 tggtcctggc attccgaggt tcgaatcctt gcaccccagc catttttcct tattttttgg 60 cgcggagtag agcagtccgg tagctcgttg ggctcataac ccaaaggtca gtggttcaaa 120 tccattctcc gcaaccaatc ctttaaacca caccaccacc aaacgaacca aacgaaacaa 180 aaagcatcaa aatcaaaaaa atgacaaaat ttttaagaaa atgacaaaaa aaaaaaaaac 240 gattttatgc tatattaacg aaatcttgtg ataagatctt attcttttaa aagacttatc 300 taaccatttt aatttcaagg agaaaac atg aaa aaa acc ctt tta ctc tct ctc 354 Met Lys Lys Thr Leu Leu Leu Ser Leu -15 tct ctc tct ctc tcg ttt ttg ctc cac gct gaa gac gac ggc ttt tac 402 Ser Leu Ser Leu Ser Phe Leu Leu His Ala Glu Asp Asp Gly Phe Tyr -10 -5 1 5 aca agc gtg ggc tat caa atc ggt gaa gcc gct caa atg gtg aaa aac 450 Thr Ser Val Gly Tyr Gln Ile Gly Glu Ala Ala Gln Met Val Lys Asn 10 15 20 acc aaa ggc att caa gag ctt tca gac aat tat gaa aag ctg aac aat 498 Thr Lys Gly Ile Gln Glu Leu Ser Asp Asn Tyr Glu Lys Leu Asn Asn 25 30 35 ctt ttg aat aat tac agc acc cta aac acc ctt atc aaa ttg tcc gct 546 Leu Leu Asn Asn Tyr Ser Thr Leu Asn Thr Leu Ile Lys Leu Ser Ala 40 45 50 gat ccg agc gcg att aac gac gca agg gat aat cta ggc tca agc tct 594 Asp Pro Ser Ala Ile Asn Asp Ala Arg Asp Asn Leu Gly Ser Ser Ser 55 60 65 70 agg aat ttg ctt gat gtc aaa acc aat tcc ccc gcg tat caa gcc gtg 642 Arg Asn Leu Leu Asp Val Lys Thr Asn Ser Pro Ala Tyr Gln Ala Val 75 80 85 ctt tta gca ctc aat gct gca gtg ggg ttg tgg caa gtt aca agc tac 690 Leu Leu Ala Leu Asn Ala Ala Val Gly Leu Trp Gln Val Thr Ser Tyr 90 95 100 gct ttt act gct tgt ggt cct ggc agt aac gag aat gcg aat gga ggg 738 Ala Phe Thr Ala Cys Gly Pro Gly Ser Asn Glu Asn Ala Asn Gly Gly 105 110 115 atc caa act ttt aat aat gtg cca gga caa gat acg acg acc atc act 786 Ile Gln Thr Phe Asn Asn Val Pro Gly Gln Asp Thr Thr Thr Ile Thr 120 125 130 tgc aat tcg tat tat gag cca gga cat ggt ggg cct ata tcc act gca 834 Cys Asn Ser Tyr Tyr Glu Pro Gly His Gly Gly Pro Ile Ser Thr Ala 135 140 145 150 aat tat gcg aaa atc aat caa gcc tat caa atc atc caa aag gct ttg 882 Asn Tyr Ala Lys Ile Asn Gln Ala Tyr Gln Ile Ile Gln Lys Ala Leu 155 160 165 aca gcc aat gga gct aat gga gat ggg gtc ccc gtt tta agc aac acc 930 Thr Ala Asn Gly Ala Asn Gly Asp Gly Val Pro Val Leu Ser Asn Thr 170 175 180 act aca aaa ctt gat ttc act atc aat gga gac aaa aga acg ggg ggc 978 Thr Thr Lys Leu Asp Phe Thr Ile Asn Gly Asp Lys Arg Thr Gly Gly 185 190 195 aaa cca aat aca cct gaa aag ttc cca tgg agt gat ggg aaa tat att 1026 Lys Pro Asn Thr Pro Glu Lys Phe Pro Trp Ser Asp Gly Lys Tyr Ile 200 205 210 cac acc caa tgg att aac aca ata gta aca cca aca gaa aca aat atc 1074 His Thr Gln Trp Ile Asn Thr Ile Val Thr Pro Thr Glu Thr Asn Ile 215 220 225 230 aac aca gaa aat aac gct caa gag ctt tta aaa caa gcg agc atc att 1122 Asn Thr Glu Asn Asn Ala Gln Glu Leu Leu Lys Gln Ala Ser Ile Ile 235 240 245 atc act acc cta aat gag gca tgc cca aac ttc caa aat ggt ggt aga 1170 Ile Thr Thr Leu Asn Glu Ala Cys Pro Asn Phe Gln Asn Gly Gly Arg 250 255 260 agt tat tgg caa ggg ata agc ggc aat ggg aca atg tgc ggg atg ttt 1218 Ser Tyr Trp Gln Gly Ile Ser Gly Asn Gly Thr Met Cys Gly Met Phe 265 270 275 aag aat gaa atc agc gcg atc caa ggc atg atc gct aac gct caa gaa 1266 Lys Asn Glu Ile Ser Ala Ile Gln Gly Met Ile Ala Asn Ala Gln Glu 280 285 290 gct gtc gcg caa agc aaa atc gtt agt gaa aac gcg caa aat caa aac 1314 Ala Val Ala Gln Ser Lys Ile Val Ser Glu Asn Ala Gln Asn Gln Asn 295 300 305 310 aac ttg gat act gga aaa cca ttc aac cct tac acg gac gcc agc ttt 1362 Asn Leu Asp Thr Gly Lys Pro Phe Asn Pro Tyr Thr Asp Ala Ser Phe 315 320 325 gcg caa agc atg ctc aaa aac gct caa gcg caa gca gag att tta aac 1410 Ala Gln Ser Met Leu Lys Asn Ala Gln Ala Gln Ala Glu Ile Leu Asn 330 335 340 caa gcc gaa caa gta gta aaa aac ttt gaa aaa atc cct aca gcc ttt 1458 Gln Ala Glu Gln Val Val Lys Asn Phe Glu Lys Ile Pro Thr Ala Phe 345 350 355 gta tca gac tct tta ggg gtg tgt tat gaa gtg caa ggg ggt gag cgt 1506 Val Ser Asp Ser Leu Gly Val Cys Tyr Glu Val Gln Gly Gly Glu Arg 360 365 370 agg ggc acc aat cca ggt cag gta act tct aac act tgg gga gcc ggt 1554 Arg Gly Thr Asn Pro Gly Gln Val Thr Ser Asn Thr Trp Gly Ala Gly 375 380 385 390 tgc gcg tat gtg aaa caa acc ata acg aat tta gac aac agc atc gct 1602 Cys Ala Tyr Val Lys Gln Thr Ile Thr Asn Leu Asp Asn Ser Ile Ala 395 400 405 cac ttt ggc act caa gag cag cag ata cag caa gcc gaa aac atc gct 1650 His Phe Gly Thr Gln Glu Gln Gln Ile Gln Gln Ala Glu Asn Ile Ala 410 415 420 gac act cta gtg aat ttc aaa tct aga tac agc gaa tta ggc aac acc 1698 Asp Thr Leu Val Asn Phe Lys Ser Arg Tyr Ser Glu Leu Gly Asn Thr 425 430 435 tat aac agc atc acc acc gcg ctc tcc aaa gtc cct aac gcg caa agc 1746 Tyr Asn Ser Ile Thr Thr Ala Leu Ser Lys Val Pro Asn Ala Gln Ser 440 445 450 ttg caa aac gtg gtg agc aaa aag aat aac ccc tat agc cct caa ggc 1794 Leu Gln Asn Val Val Ser Lys Lys Asn Asn Pro Tyr Ser Pro Gln Gly 455 460 465 470 ata gag acc aat tac tac ctc aat caa aat tct tac aac caa atc caa 1842 Ile Glu Thr Asn Tyr Tyr Leu Asn Gln Asn Ser Tyr Asn Gln Ile Gln 475 480 485 acc atc aac caa gaa cta ggg cgt aac ccc ttt agg aaa gtg ggc atc 1890 Thr Ile Asn Gln Glu Leu Gly Arg Asn Pro Phe Arg Lys Val Gly Ile 490 495 500 gtc aat tct caa acc aac aat ggt gcc atg aat ggg atc ggt att cag 1938 Val Asn Ser Gln Thr Asn Asn Gly Ala Met Asn Gly Ile Gly Ile Gln 505 510 515 gtg ggc tat aag caa ttc ttt ggc caa aaa aga aaa tgg ggc gct agg 1986 Val Gly Tyr Lys Gln Phe Phe Gly Gln Lys Arg Lys Trp Gly Ala Arg 520 525 530 tat tac ggc ttt ttt gac tac aac cat gcg ttc att aaa tcc agc ttc 2034 Tyr Tyr Gly Phe Phe Asp Tyr Asn His Ala Phe Ile Lys Ser Ser Phe 535 540 545 550 ttc aac tcg gct tct gat gtg tgg act tat ggt ttt gga gcg gac gct 2082 Phe Asn Ser Ala Ser Asp Val Trp Thr Tyr Gly Phe Gly Ala Asp Ala 555 560 565 ctt tat aac ttc atc aac gat aaa gcc acc aat ttc tta ggc aaa aac 2130 Leu Tyr Asn Phe Ile Asn Asp Lys Ala Thr Asn Phe Leu Gly Lys Asn 570 575 580 aac aag ctt tcc gtg ggg ctt ttt gga ggg att gcg tta gcg ggc act 2178 Asn Lys Leu Ser Val Gly Leu Phe Gly Gly Ile Ala Leu Ala Gly Thr 585 590 595 tca tgg ctt aat tct gag tat gtg aat tta gcc acc gtg aat aac gtc 2226 Ser Trp Leu Asn Ser Glu Tyr Val Asn Leu Ala Thr Val Asn Asn Val 600 605 610 tat aac gct aaa atg aat gtg gcg aat ttc caa ttc tta ttc aat atg 2274 Tyr Asn Ala Lys Met Asn Val Ala Asn Phe Gln Phe Leu Phe Asn Met 615 620 625 630 gga gtg agg atg aat tta gcc aga tcc aag aaa aaa ggc agc gat cat 2322 Gly Val Arg Met Asn Leu Ala Arg Ser Lys Lys Lys Gly Ser Asp His 635 640 645 gcg gct cag cat ggg att gaa cta ggg ctt aaa atc ccc acc atc aac 2370 Ala Ala Gln His Gly Ile Glu Leu Gly Leu Lys Ile Pro Thr Ile Asn 650 655 660 acg aac tat tat tct ttc atg ggg gct gaa ctc aaa tac aga agg ctt 2418 Thr Asn Tyr Tyr Ser Phe Met Gly Ala Glu Leu Lys Tyr Arg Arg Leu 665 670 675 tat agc gtg tat ttg aat tat gtg ttc gct tac taagcttttt gtgaaactcc 2471 Tyr Ser Val Tyr Leu Asn Tyr Val Phe Ala Tyr 680 685 ctttttaagg ggtttttttt tgaactctct ttttaaattc tctttttaaa gagatttctt 2531 ttttttaagc ttttttttga attctttttt ttgaattctt tgtttttaag ctttttttaa 2591 accctttcgt ttttaaactc ccttttttaa gggatttctt tttttaaact cttttttttt 2651 aaactctttt ttttaaaccc tcttttttta agggatttct ttttaaagct tttttgaagt 2711 ctttttttaa attctttttt tgggggtttg atctttcttt ttgccaatcc ccactacttt 2771 cgctttttaa tctttaggtt ttatttt 2798 <200> SEQUENCE CHARACTERISTICS: <210> SEQ ID NO 2 <211> LENGTH: 708 <212> TYPE: PRT <213> ORGANISM: Helicobacter pylori <220> FEATURE: <221> NAME/KEY: SIGNAL <222> LOCATION: (1)...(19) <400> SEQUENCE: 2 Met Lys Lys Thr Leu Leu Leu Ser Leu Ser Leu Ser Leu Ser Phe Leu -15 -10 -5 Leu His Ala Glu Asp Asp Gly Phe Tyr Thr Ser Val Gly Tyr Gln Ile 1 5 10 Gly Glu Ala Ala Gln Met Val Lys Asn Thr Lys Gly Ile Gln Glu Leu 15 20 25 Ser Asp Asn Tyr Glu Lys Leu Asn Asn Leu Leu Asn Asn Tyr Ser Thr 30 35 40 45 Leu Asn Thr Leu Ile Lys Leu Ser Ala Asp Pro Ser Ala Ile Asn Asp 50 55 60 Ala Arg Asp Asn Leu Gly Ser Ser Ser Arg Asn Leu Leu Asp Val Lys 65 70 75 Thr Asn Ser Pro Ala Tyr Gln Ala Val Leu Leu Ala Leu Asn Ala Ala 80 85 90 Val Gly Leu Trp Gln Val Thr Ser Tyr Ala Phe Thr Ala Cys Gly Pro 95 100 105 Gly Ser Asn Glu Asn Ala Asn Gly Gly Ile Gln Thr Phe Asn Asn Val 110 115 120 125 Pro Gly Gln Asp Thr Thr Thr Ile Thr Cys Asn Ser Tyr Tyr Glu Pro 130 135 140 Gly His Gly Gly Pro Ile Ser Thr Ala Asn Tyr Ala Lys Ile Asn Gln 145 150 155 Ala Tyr Gln Ile Ile Gln Lys Ala Leu Thr Ala Asn Gly Ala Asn Gly 160 165 170 Asp Gly Val Pro Val Leu Ser Asn Thr Thr Thr Lys Leu Asp Phe Thr 175 180 185 Ile Asn Gly Asp Lys Arg Thr Gly Gly Lys Pro Asn Thr Pro Glu Lys 190 195 200 205 Phe Pro Trp Ser Asp Gly Lys Tyr Ile His Thr Gln Trp Ile Asn Thr 210 215 220 Ile Val Thr Pro Thr Glu Thr Asn Ile Asn Thr Glu Asn Asn Ala Gln 225 230 235 Glu Leu Leu Lys Gln Ala Ser Ile Ile Ile Thr Thr Leu Asn Glu Ala 240 245 250 Cys Pro Asn Phe Gln Asn Gly Gly Arg Ser Tyr Trp Gln Gly Ile Ser 255 260 265 Gly Asn Gly Thr Met Cys Gly Met Phe Lys Asn Glu Ile Ser Ala Ile 270 275 280 285 Gln Gly Met Ile Ala Asn Ala Gln Glu Ala Val Ala Gln Ser Lys Ile 290 295 300 Val Ser Glu Asn Ala Gln Asn Gln Asn Asn Leu Asp Thr Gly Lys Pro 305 310 315 Phe Asn Pro Tyr Thr Asp Ala Ser Phe Ala Gln Ser Met Leu Lys Asn 320 325 330 Ala Gln Ala Gln Ala Glu Ile Leu Asn Gln Ala Glu Gln Val Val Lys 335 340 345 Asn Phe Glu Lys Ile Pro Thr Ala Phe Val Ser Asp Ser Leu Gly Val 350 355 360 365 Cys Tyr Glu Val Gln Gly Gly Glu Arg Arg Gly Thr Asn Pro Gly Gln 370 375 380 Val Thr Ser Asn Thr Trp Gly Ala Gly Cys Ala Tyr Val Lys Gln Thr 385 390 395 Ile Thr Asn Leu Asp Asn Ser Ile Ala His Phe Gly Thr Gln Glu Gln 400 405 410 Gln Ile Gln Gln Ala Glu Asn Ile Ala Asp Thr Leu Val Asn Phe Lys 415 420 425 Ser Arg Tyr Ser Glu Leu Gly Asn Thr Tyr Asn Ser Ile Thr Thr Ala 430 435 440 445 Leu Ser Lys Val Pro Asn Ala Gln Ser Leu Gln Asn Val Val Ser Lys 450 455 460 Lys Asn Asn Pro Tyr Ser Pro Gln Gly Ile Glu Thr Asn Tyr Tyr Leu 465 470 475 Asn Gln Asn Ser Tyr Asn Gln Ile Gln Thr Ile Asn Gln Glu Leu Gly 480 485 490 Arg Asn Pro Phe Arg Lys Val Gly Ile Val Asn Ser Gln Thr Asn Asn 495 500 505 Gly Ala Met Asn Gly Ile Gly Ile Gln Val Gly Tyr Lys Gln Phe Phe 510 515 520 525 Gly Gln Lys Arg Lys Trp Gly Ala Arg Tyr Tyr Gly Phe Phe Asp Tyr 530 535 540 Asn His Ala Phe Ile Lys Ser Ser Phe Phe Asn Ser Ala Ser Asp Val 545 550 555 Trp Thr Tyr Gly Phe Gly Ala Asp Ala Leu Tyr Asn Phe Ile Asn Asp 560 565 570 Lys Ala Thr Asn Phe Leu Gly Lys Asn Asn Lys Leu Ser Val Gly Leu 575 580 585 Phe Gly Gly Ile Ala Leu Ala Gly Thr Ser Trp Leu Asn Ser Glu Tyr 590 595 600 605 Val Asn Leu Ala Thr Val Asn Asn Val Tyr Asn Ala Lys Met Asn Val 610 615 620 Ala Asn Phe Gln Phe Leu Phe Asn Met Gly Val Arg Met Asn Leu Ala 625 630 635 Arg Ser Lys Lys Lys Gly Ser Asp His Ala Ala Gln His Gly Ile Glu 640 645 650 Leu Gly Leu Lys Ile Pro Thr Ile Asn Thr Asn Tyr Tyr Ser Phe Met 655 660 665 Gly Ala Glu Leu Lys Tyr Arg Arg Leu Tyr Ser Val Tyr Leu Asn Tyr 670 675 680 685 Val Phe Ala Tyr <200> SEQUENCE CHARACTERISTICS: <210> SEQ ID NO 3 <211> LENGTH: 2699 <212> TYPE: DNA <213> ORGANISM: Helicobacter pylori <220> FEATURE: <221> NAME/KEY: CDS <222> LOCATION: (199)...(2397) <220> FEATURE: <221> NAME/KEY: sig_peptide <222> LOCATION: (199)...(259) <400> SEQUENCE: 3 taaaatccaa ttaaaagcgt tcaaaggtaa cgcaaaaaaa caaaaaatga cgcaattttt 60 tcaaaatgac aaaaaaaaac gctttatgct ataatacccc aaatacattc taatagcaaa 120 tgcgttctaa tgcaaatgca ttccaatgta tgaaatccct aatactaaat ccaatttaat 180 ccaaaaagga gaaaaaac atg aaa aaa cac atc ctt tca tta gct tta ggc 231 Met Lys Lys His Ile Leu Ser Leu Ala Leu Gly -20 -15 -10 tcg ctt tta gtt tcc act ttg agc gct gaa gac gac ggc ttt tac aca 279 Ser Leu Leu Val Ser Thr Leu Ser Ala Glu Asp Asp Gly Phe Tyr Thr -5 1 5 agc gta ggc tat cag atc ggt gaa gcc gct caa atg gta aca aac acc 327 Ser Val Gly Tyr Gln Ile Gly Glu Ala Ala Gln Met Val Thr Asn Thr 10 15 20 aaa ggc atc caa cag ctt tca gac aat tat gaa aat ttg aac aac ctt 375 Lys Gly Ile Gln Gln Leu Ser Asp Asn Tyr Glu Asn Leu Asn Asn Leu 25 30 35 tta acg aga tac agc acc cta aac acc ctt atc aaa ttg tcc gct gat 423 Leu Thr Arg Tyr Ser Thr Leu Asn Thr Leu Ile Lys Leu Ser Ala Asp 40 45 50 55 ccg agc gca att aat gcg gtg cgg gaa aat ctg ggc gcg agc gcg aag 471 Pro Ser Ala Ile Asn Ala Val Arg Glu Asn Leu Gly Ala Ser Ala Lys 60 65 70 aat ttg atc ggc gat aaa gcc aac tcc ccc gcc tat caa gcc gtg ctt 519 Asn Leu Ile Gly Asp Lys Ala Asn Ser Pro Ala Tyr Gln Ala Val Leu 75 80 85 tta gcg atc aac gcg gcg gta ggg ttt tgg aat gtc gtg ggc tat gtg 567 Leu Ala Ile Asn Ala Ala Val Gly Phe Trp Asn Val Val Gly Tyr Val 90 95 100 acg caa tgt ggg ggt aac gcc aat ggt caa gaa agc acc tct tca acc 615 Thr Gln Cys Gly Gly Asn Ala Asn Gly Gln Glu Ser Thr Ser Ser Thr 105 110 115 acc atc ttc aac aac gag cca ggg tat cga tcc act tcc atc act tgt 663 Thr Ile Phe Asn Asn Glu Pro Gly Tyr Arg Ser Thr Ser Ile Thr Cys 120 125 130 135 tct ttg aac ggg cat aag cct gga tac tat ggc cct atg agc att gag 711 Ser Leu Asn Gly His Lys Pro Gly Tyr Tyr Gly Pro Met Ser Ile Glu 140 145 150 aat ttt aaa aag ctt aac gaa gcc tat cag atc ctc caa acg gct tta 759 Asn Phe Lys Lys Leu Asn Glu Ala Tyr Gln Ile Leu Gln Thr Ala Leu 155 160 165 aaa aac ggc tta ccc gcg ctc aaa gaa aac aac ggg aag gtc agt gta 807 Lys Asn Gly Leu Pro Ala Leu Lys Glu Asn Asn Gly Lys Val Ser Val 170 175 180 acc tat acc tac aca tgc tca ggg caa ggg aat aat aac tgc tcg cca 855 Thr Tyr Thr Tyr Thr Cys Ser Gly Gln Gly Asn Asn Asn Cys Ser Pro 185 190 195 agt gtc aac gga acc aaa acc aca acc caa acc ata gac ggc aaa agc 903 Ser Val Asn Gly Thr Lys Thr Thr Thr Gln Thr Ile Asp Gly Lys Ser 200 205 210 215 gta acc acc acg atc agt tca aaa gtg gtt ggt agc atc gct agt ggc 951 Val Thr Thr Thr Ile Ser Ser Lys Val Val Gly Ser Ile Ala Ser Gly 220 225 230 aac aca tca cat gtc atc acc aac aaa tta gac ggt gtg cct gat agc 999 Asn Thr Ser His Val Ile Thr Asn Lys Leu Asp Gly Val Pro Asp Ser 235 240 245 gct caa gcg ctc tta gcg caa gcg agc acg ctc atc aac acc atc aac 1047 Ala Gln Ala Leu Leu Ala Gln Ala Ser Thr Leu Ile Asn Thr Ile Asn 250 255 260 gaa gca tgc ccg tat ttc cat gct act aat agt agt gag gct aac gcc 1095 Glu Ala Cys Pro Tyr Phe His Ala Thr Asn Ser Ser Glu Ala Asn Ala 265 270 275 cca aaa ttc tct act act act ggg aaa ata tgc ggc gct ttt tca gaa 1143 Pro Lys Phe Ser Thr Thr Thr Gly Lys Ile Cys Gly Ala Phe Ser Glu 280 285 290 295 gaa atc agc gcg atc caa aag atg atc acg gac gcg caa gag cta gtt 1191 Glu Ile Ser Ala Ile Gln Lys Met Ile Thr Asp Ala Gln Glu Leu Val 300 305 310 aat caa acg agc gtc att aac agc aac gaa caa tca act ccg gta ggc 1239 Asn Gln Thr Ser Val Ile Asn Ser Asn Glu Gln Ser Thr Pro Val Gly 315 320 325 aat aat aat ggc aag cct ttc aac cct ttc acg gac gca agt ttt gcg 1287 Asn Asn Asn Gly Lys Pro Phe Asn Pro Phe Thr Asp Ala Ser Phe Ala 330 335 340 caa ggc atg ctc gct aac gct agc gcg caa gct aaa atg ctc aat tta 1335 Gln Gly Met Leu Ala Asn Ala Ser Ala Gln Ala Lys Met Leu Asn Leu 345 350 355 gcc cat cag gtg ggg caa gcc att aac cca gag aat ctt agc gag aat 1383 Ala His Gln Val Gly Gln Ala Ile Asn Pro Glu Asn Leu Ser Glu Asn 360 365 370 375 ttt aaa aat ttt gtt aca ggc ttt tta gcc aca tgc aat aac aaa tca 1431 Phe Lys Asn Phe Val Thr Gly Phe Leu Ala Thr Cys Asn Asn Lys Ser 380 385 390 aca gct ggc act ggt ggc aca caa ggt tca gct cca ggc aca gtg acc 1479 Thr Ala Gly Thr Gly Gly Thr Gln Gly Ser Ala Pro Gly Thr Val Thr 395 400 405 act caa act ttc gct tct ggt tgc gcg tat gtg gag caa acc cta acg 1527 Thr Gln Thr Phe Ala Ser Gly Cys Ala Tyr Val Glu Gln Thr Leu Thr 410 415 420 aac tta ggc aac agc atc gct cac ttt ggc act caa gag cag cag ata 1575 Asn Leu Gly Asn Ser Ile Ala His Phe Gly Thr Gln Glu Gln Gln Ile 425 430 435 cag caa gcc gaa aac atc gct gac act cta gtg aat ttc aaa tct aga 1623 Gln Gln Ala Glu Asn Ile Ala Asp Thr Leu Val Asn Phe Lys Ser Arg 440 445 450 455 tac agc gaa tta ggc aac acc tat aac agc atc acc acc gcg ctc tcc 1671 Tyr Ser Glu Leu Gly Asn Thr Tyr Asn Ser Ile Thr Thr Ala Leu Ser 460 465 470 aaa gtc cct aac gcg caa agc ttg caa aac gtg gtg agc aaa aag aat 1719 Lys Val Pro Asn Ala Gln Ser Leu Gln Asn Val Val Ser Lys Lys Asn 475 480 485 aac ccc tat agc cct caa ggc ata gag acc aat tac tac ctc aat caa 1767 Asn Pro Tyr Ser Pro Gln Gly Ile Glu Thr Asn Tyr Tyr Leu Asn Gln 490 495 500 aat tct tac aac caa atc caa acc atc aac caa gaa cta ggg cgt aac 1815 Asn Ser Tyr Asn Gln Ile Gln Thr Ile Asn Gln Glu Leu Gly Arg Asn 505 510 515 ccc ttt agg aaa gtg ggc atc gtc aat tct caa acc aac aat ggt gcc 1863 Pro Phe Arg Lys Val Gly Ile Val Asn Ser Gln Thr Asn Asn Gly Ala 520 525 530 535 atg aat ggg atc ggt att cag gtg ggc tat aag caa ttc ttt ggc caa 1911 Met Asn Gly Ile Gly Ile Gln Val Gly Tyr Lys Gln Phe Phe Gly Gln 540 545 550 aaa aga aaa tgg ggc gct agg tat tac ggc ttt ttt gat tac aac cat 1959 Lys Arg Lys Trp Gly Ala Arg Tyr Tyr Gly Phe Phe Asp Tyr Asn His 555 560 565 gcg ttc atc aaa tcc agc ttt ttc aac tcg gct tct gac gtg tgg act 2007 Ala Phe Ile Lys Ser Ser Phe Phe Asn Ser Ala Ser Asp Val Trp Thr 570 575 580 tat ggt ttt gga gcg gac gcg ctt tat aac ttc atc aac gat aaa gcc 2055 Tyr Gly Phe Gly Ala Asp Ala Leu Tyr Asn Phe Ile Asn Asp Lys Ala 585 590 595 acc aat ttc tta ggc aaa aac aac aag ctt tct ttg ggg ctt ttt ggc 2103 Thr Asn Phe Leu Gly Lys Asn Asn Lys Leu Ser Leu Gly Leu Phe Gly 600 605 610 615 ggg att gcg tta gcg ggc act tca tgg ctc aat tct gag tac gtg aat 2151 Gly Ile Ala Leu Ala Gly Thr Ser Trp Leu Asn Ser Glu Tyr Val Asn 620 625 630 tta gcc acc gtg aat aac gtc tat aac gct aaa atg aat gtg gcg aat 2199 Leu Ala Thr Val Asn Asn Val Tyr Asn Ala Lys Met Asn Val Ala Asn 635 640 645 ttc caa ttc tta ttc aat atg gga gtg agg atg aat tta gcc aga tcc 2247 Phe Gln Phe Leu Phe Asn Met Gly Val Arg Met Asn Leu Ala Arg Ser 650 655 660 aag aaa aaa ggc agc gat cat gca gct cag cat ggg att gag tta ggg 2295 Lys Lys Lys Gly Ser Asp His Ala Ala Gln His Gly Ile Glu Leu Gly 665 670 675 ctt aaa atc ccc acc atc aac acg aac tat tat tcc ttt atg ggg gct 2343 Leu Lys Ile Pro Thr Ile Asn Thr Asn Tyr Tyr Ser Phe Met Gly Ala 680 685 690 695 gaa ctc aaa tac aga agg ctc tat agc gtg tat ttg aac tat gtg ttc 2391 Glu Leu Lys Tyr Arg Arg Leu Tyr Ser Val Tyr Leu Asn Tyr Val Phe 700 705 710 gct tac taatgtttgg ctctttgtga aactcccttt ttaaggggtt tttttttgaa 2447 Ala Tyr ctctcttttt aaattctctt tttaaagaga tttctttttt ttaagctttt ttttgaattc 2507 tttttttttg aattctttgt ttttaagctt tttttaaacc ctttcgtttt taaactccct 2567 tttttaaggg atttcttttt ttgaactccc ttttttgaac cctttttttt aaaccctctt 2627 tttttaaggg gtttcttttt aaagcttttt tgaagtcttt ttttaaattc tttttttggg 2687 ggtttgatct tt 2699 <200> SEQUENCE CHARACTERISTICS: <210> SEQ ID NO 4 <211> LENGTH: 733 <212> TYPE: PRT <213> ORGANISM: Helicobacter pylori <220> FEATURE: <221> NAME/KEY: SIGNAL <222> LOCATION: (1)...(20) <400> SEQUENCE: 4 Met Lys Lys His Ile Leu Ser Leu Ala Leu Gly Ser Leu Leu Val Ser -20 -15 -10 -5 Thr Leu Ser Ala Glu Asp Asp Gly Phe Tyr Thr Ser Val Gly Tyr Gln 1 5 10 Ile Gly Glu Ala Ala Gln Met Val Thr Asn Thr Lys Gly Ile Gln Gln 15 20 25 Leu Ser Asp Asn Tyr Glu Asn Leu Asn Asn Leu Leu Thr Arg Tyr Ser 30 35 40 Thr Leu Asn Thr Leu Ile Lys Leu Ser Ala Asp Pro Ser Ala Ile Asn 45 50 55 60 Ala Val Arg Glu Asn Leu Gly Ala Ser Ala Lys Asn Leu Ile Gly Asp 65 70 75 Lys Ala Asn Ser Pro Ala Tyr Gln Ala Val Leu Leu Ala Ile Asn Ala 80 85 90 Ala Val Gly Phe Trp Asn Val Val Gly Tyr Val Thr Gln Cys Gly Gly 95 100 105 Asn Ala Asn Gly Gln Glu Ser Thr Ser Ser Thr Thr Ile Phe Asn Asn 110 115 120 Glu Pro Gly Tyr Arg Ser Thr Ser Ile Thr Cys Ser Leu Asn Gly His 125 130 135 140 Lys Pro Gly Tyr Tyr Gly Pro Met Ser Ile Glu Asn Phe Lys Lys Leu 145 150 155 Asn Glu Ala Tyr Gln Ile Leu Gln Thr Ala Leu Lys Asn Gly Leu Pro 160 165 170 Ala Leu Lys Glu Asn Asn Gly Lys Val Ser Val Thr Tyr Thr Tyr Thr 175 180 185 Cys Ser Gly Gln Gly Asn Asn Asn Cys Ser Pro Ser Val Asn Gly Thr 190 195 200 Lys Thr Thr Thr Gln Thr Ile Asp Gly Lys Ser Val Thr Thr Thr Ile 205 210 215 220 Ser Ser Lys Val Val Gly Ser Ile Ala Ser Gly Asn Thr Ser His Val 225 230 235 Ile Thr Asn Lys Leu Asp Gly Val Pro Asp Ser Ala Gln Ala Leu Leu 240 245 250 Ala Gln Ala Ser Thr Leu Ile Asn Thr Ile Asn Glu Ala Cys Pro Tyr 255 260 265 Phe His Ala Thr Asn Ser Ser Glu Ala Asn Ala Pro Lys Phe Ser Thr 270 275 280 Thr Thr Gly Lys Ile Cys Gly Ala Phe Ser Glu Glu Ile Ser Ala Ile 285 290 295 300 Gln Lys Met Ile Thr Asp Ala Gln Glu Leu Val Asn Gln Thr Ser Val 305 310 315 Ile Asn Ser Asn Glu Gln Ser Thr Pro Val Gly Asn Asn Asn Gly Lys 320 325 330 Pro Phe Asn Pro Phe Thr Asp Ala Ser Phe Ala Gln Gly Met Leu Ala 335 340 345 Asn Ala Ser Ala Gln Ala Lys Met Leu Asn Leu Ala His Gln Val Gly 350 355 360 Gln Ala Ile Asn Pro Glu Asn Leu Ser Glu Asn Phe Lys Asn Phe Val 365 370 375 380 Thr Gly Phe Leu Ala Thr Cys Asn Asn Lys Ser Thr Ala Gly Thr Gly 385 390 395 Gly Thr Gln Gly Ser Ala Pro Gly Thr Val Thr Thr Gln Thr Phe Ala 400 405 410 Ser Gly Cys Ala Tyr Val Glu Gln Thr Leu Thr Asn Leu Gly Asn Ser 415 420 425 Ile Ala His Phe Gly Thr Gln Glu Gln Gln Ile Gln Gln Ala Glu Asn 430 435 440 Ile Ala Asp Thr Leu Val Asn Phe Lys Ser Arg Tyr Ser Glu Leu Gly 445 450 455 460 Asn Thr Tyr Asn Ser Ile Thr Thr Ala Leu Ser Lys Val Pro Asn Ala 465 470 475 Gln Ser Leu Gln Asn Val Val Ser Lys Lys Asn Asn Pro Tyr Ser Pro 480 485 490 Gln Gly Ile Glu Thr Asn Tyr Tyr Leu Asn Gln Asn Ser Tyr Asn Gln 495 500 505 Ile Gln Thr Ile Asn Gln Glu Leu Gly Arg Asn Pro Phe Arg Lys Val 510 515 520 Gly Ile Val Asn Ser Gln Thr Asn Asn Gly Ala Met Asn Gly Ile Gly 525 530 535 540 Ile Gln Val Gly Tyr Lys Gln Phe Phe Gly Gln Lys Arg Lys Trp Gly 545 550 555 Ala Arg Tyr Tyr Gly Phe Phe Asp Tyr Asn His Ala Phe Ile Lys Ser 560 565 570 Ser Phe Phe Asn Ser Ala Ser Asp Val Trp Thr Tyr Gly Phe Gly Ala 575 580 585 Asp Ala Leu Tyr Asn Phe Ile Asn Asp Lys Ala Thr Asn Phe Leu Gly 590 595 600 Lys Asn Asn Lys Leu Ser Leu Gly Leu Phe Gly Gly Ile Ala Leu Ala 605 610 615 620 Gly Thr Ser Trp Leu Asn Ser Glu Tyr Val Asn Leu Ala Thr Val Asn 625 630 635 Asn Val Tyr Asn Ala Lys Met Asn Val Ala Asn Phe Gln Phe Leu Phe 640 645 650 Asn Met Gly Val Arg Met Asn Leu Ala Arg Ser Lys Lys Lys Gly Ser 655 660 665 Asp His Ala Ala Gln His Gly Ile Glu Leu Gly Leu Lys Ile Pro Thr 670 675 680 Ile Asn Thr Asn Tyr Tyr Ser Phe Met Gly Ala Glu Leu Lys Tyr Arg 685 690 695 700 Arg Leu Tyr Ser Val Tyr Leu Asn Tyr Val Phe Ala Tyr 705 710 <200> SEQUENCE CHARACTERISTICS: <210> SEQ ID NO 5 <211> LENGTH: 2915 <212> TYPE: DNA <213> ORGANISM: Helicobacter pylori <220> FEATURE: <221> NAME/KEY: CDS <222> LOCATION: (365)...(2599) <220> FEATURE: <221> NAME/KEY: sig_peptide <222> LOCATION: (365)...(425) <220> FEATURE: <221> NAME/KEY: misc_feature <222> LOCATION: 2585 <223> OTHER INFORMATION: n = A,T,C or G <400> SEQUENCE: 5 ttttaggcga caaaatcgct tatgttgggg ataaaggcaa cccgcacaat ttcgctcaca 60 agaaataaac cgctcataag gggcaaacgc cccaaaaaag cgatttttaa agaggttacg 120 gcaaaatcaa gctctttagt atttaatctt aaaaaatgct aaaagccttt ttatgggcta 180 acaccacaca aaaagcatca aaatcaaaaa aatgacaaaa tttttaagaa aatgacaaaa 240 aaaaacgctt tatgctataa taccccaaat acattctaat agcaaatgcg ttctaatgca 300 aatgcattcc aatgtatgaa atccctaata ctaaatccaa tttaatccaa aaaggagaaa 360 aaac atg aaa aaa cac atc ctt tca tta gct tta ggc tcg ctt tta gtt 409 Met Lys Lys His Ile Leu Ser Leu Ala Leu Gly Ser Leu Leu Val -20 -15 -10 tcc act ttg agc gct gaa gac gac ggc ttt tac aca agc gta ggc tat 457 Ser Thr Leu Ser Ala Glu Asp Asp Gly Phe Tyr Thr Ser Val Gly Tyr -5 1 5 10 cag atc ggt gaa gcc gct caa atg gta aca aac acc aaa ggc atc caa 505 Gln Ile Gly Glu Ala Ala Gln Met Val Thr Asn Thr Lys Gly Ile Gln 15 20 25 cag ctt tca gac aat tat gaa aat ttg aac aac ctt tta acg aga tac 553 Gln Leu Ser Asp Asn Tyr Glu Asn Leu Asn Asn Leu Leu Thr Arg Tyr 30 35 40 agc acc cta aac acc ctt atc aaa ttg tcc gct gat ccg agc gca att 601 Ser Thr Leu Asn Thr Leu Ile Lys Leu Ser Ala Asp Pro Ser Ala Ile 45 50 55 aat gcg gtg cgg gaa aat ctg ggc gcg agc acg aag aat ttg atc ggc 649 Asn Ala Val Arg Glu Asn Leu Gly Ala Ser Thr Lys Asn Leu Ile Gly 60 65 70 75 gat aaa gcc aac tcc ccg gcg tat caa gcc gtg ttt tta gcg atc aac 697 Asp Lys Ala Asn Ser Pro Ala Tyr Gln Ala Val Phe Leu Ala Ile Asn 80 85 90 gcg gcg gta ggg ttg tgg aat acc atc ggc tat gcg gtc atg tgc ggg 745 Ala Ala Val Gly Leu Trp Asn Thr Ile Gly Tyr Ala Val Met Cys Gly 95 100 105 aac ggg aac ggc aca gag agt ggg cct ggc agc gtg atc ttt aat gac 793 Asn Gly Asn Gly Thr Glu Ser Gly Pro Gly Ser Val Ile Phe Asn Asp 110 115 120 caa cca gga cag gat tcc acg caa att act tgc aac cgc ttt gaa tca 841 Gln Pro Gly Gln Asp Ser Thr Gln Ile Thr Cys Asn Arg Phe Glu Ser 125 130 135 act ggg cct ggt aaa agc atg tct att gat gaa ttc aaa aaa ctc aat 889 Thr Gly Pro Gly Lys Ser Met Ser Ile Asp Glu Phe Lys Lys Leu Asn 140 145 150 155 gaa gcc tat caa atc atc cag caa gct tta aaa aat caa agt ggg ttt 937 Glu Ala Tyr Gln Ile Ile Gln Gln Ala Leu Lys Asn Gln Ser Gly Phe 160 165 170 cct gaa tta ggc ggg aac ggc aca aaa gtg agt gtt aat tac aat tac 985 Pro Glu Leu Gly Gly Asn Gly Thr Lys Val Ser Val Asn Tyr Asn Tyr 175 180 185 gaa tgc aga caa act gct gat atc aac ggc ggt gtg tat cag ttc tgc 1033 Glu Cys Arg Gln Thr Ala Asp Ile Asn Gly Gly Val Tyr Gln Phe Cys 190 195 200 aag gct aaa aat ggt agt agt agc agt agt aat ggc ggt aat ggc agt 1081 Lys Ala Lys Asn Gly Ser Ser Ser Ser Ser Asn Gly Gly Asn Gly Ser 205 210 215 agc acg caa aca acc gcg aca acc acg caa gac ggc gta acg atc acc 1129 Ser Thr Gln Thr Thr Ala Thr Thr Thr Gln Asp Gly Val Thr Ile Thr 220 225 230 235 act acc tat aat aat aac aaa gcc acc gtc aaa ttt gac atc acc aat 1177 Thr Thr Tyr Asn Asn Asn Lys Ala Thr Val Lys Phe Asp Ile Thr Asn 240 245 250 aac gct gaa cag ctg tta aat caa gcg gca aac atc atg caa gtc ctt 1225 Asn Ala Glu Gln Leu Leu Asn Gln Ala Ala Asn Ile Met Gln Val Leu 255 260 265 aat acg caa tgc cct tta gtg cgt tcc acg aat aac gaa aac act cca 1273 Asn Thr Gln Cys Pro Leu Val Arg Ser Thr Asn Asn Glu Asn Thr Pro 270 275 280 ggg ggt ggt caa cca tgg ggt tta agc aca tcc ggg aat gcg tgc agc 1321 Gly Gly Gly Gln Pro Trp Gly Leu Ser Thr Ser Gly Asn Ala Cys Ser 285 290 295 atc ttc caa caa gaa ttt agc cag gtt act agc atg atc aaa aac gcc 1369 Ile Phe Gln Gln Glu Phe Ser Gln Val Thr Ser Met Ile Lys Asn Ala 300 305 310 315 caa gaa ata atc gcg caa agc aaa atc gtt agt gaa aac gcg caa aat 1417 Gln Glu Ile Ile Ala Gln Ser Lys Ile Val Ser Glu Asn Ala Gln Asn 320 325 330 caa aac aac ttg gat act gga aaa cca ttc aac cct tac acg gac gcc 1465 Gln Asn Asn Leu Asp Thr Gly Lys Pro Phe Asn Pro Tyr Thr Asp Ala 335 340 345 agc ttt gcg caa agc atg ctc aaa aac gct caa gcg caa gca gag atg 1513 Ser Phe Ala Gln Ser Met Leu Lys Asn Ala Gln Ala Gln Ala Glu Met 350 355 360 ttc aat ttg agc gaa caa gtg aaa aag aac ttg gaa gtc atg aaa aac 1561 Phe Asn Leu Ser Glu Gln Val Lys Lys Asn Leu Glu Val Met Lys Asn 365 370 375 aac aat aat gtt aac gag aaa tta gca gga ttt ggg aaa gaa gaa gta 1609 Asn Asn Asn Val Asn Glu Lys Leu Ala Gly Phe Gly Lys Glu Glu Val 380 385 390 395 atg acc aat ttt gtt agc gcc ttt ttg gca agc tgc aaa gat ggt ggc 1657 Met Thr Asn Phe Val Ser Ala Phe Leu Ala Ser Cys Lys Asp Gly Gly 400 405 410 aca ttg cct aat gca ggg gtt act tct aac act tgg ggg gcg ggt tgc 1705 Thr Leu Pro Asn Ala Gly Val Thr Ser Asn Thr Trp Gly Ala Gly Cys 415 420 425 gcg tat gtg gga gag acg ata agc gcc cta acc aac agc atc gct cac 1753 Ala Tyr Val Gly Glu Thr Ile Ser Ala Leu Thr Asn Ser Ile Ala His 430 435 440 ttt ggc act caa gag cag cag ata cag caa gcc gaa aac atc gct gac 1801 Phe Gly Thr Gln Glu Gln Gln Ile Gln Gln Ala Glu Asn Ile Ala Asp 445 450 455 act cta gtg aat ttc aaa tct aga tac agc gaa tta ggc aac acc tat 1849 Thr Leu Val Asn Phe Lys Ser Arg Tyr Ser Glu Leu Gly Asn Thr Tyr 460 465 470 475 aac agc atc acc acc gcg ctc tcc aaa gtc cct aac gcg caa agc ttg 1897 Asn Ser Ile Thr Thr Ala Leu Ser Lys Val Pro Asn Ala Gln Ser Leu 480 485 490 caa aac gtg gtg agc aaa aag aat aac ccc tat agc cct caa ggc ata 1945 Gln Asn Val Val Ser Lys Lys Asn Asn Pro Tyr Ser Pro Gln Gly Ile 495 500 505 gag acc aat tac tac ctc aat caa aat tct tac aac caa atc caa acc 1993 Glu Thr Asn Tyr Tyr Leu Asn Gln Asn Ser Tyr Asn Gln Ile Gln Thr 510 515 520 atc aac caa gaa cta ggg cgt aac ccc ttt agg aaa gtg ggc atc gtc 2041 Ile Asn Gln Glu Leu Gly Arg Asn Pro Phe Arg Lys Val Gly Ile Val 525 530 535 aat tct caa acc aac aat ggt gcc atg aat ggg atc ggc att cag gtg 2089 Asn Ser Gln Thr Asn Asn Gly Ala Met Asn Gly Ile Gly Ile Gln Val 540 545 550 555 ggc tat aag caa ttc ttt ggc caa aaa aga aaa tgg ggc gct agg tat 2137 Gly Tyr Lys Gln Phe Phe Gly Gln Lys Arg Lys Trp Gly Ala Arg Tyr 560 565 570 tac ggc ttt ttt gat tac aac cat gcg ttc atc aaa tcc agc ttt ttc 2185 Tyr Gly Phe Phe Asp Tyr Asn His Ala Phe Ile Lys Ser Ser Phe Phe 575 580 585 aac tcg gct tct gac gtg tgg act tat ggt ttt gga gcg gac gcg ctt 2233 Asn Ser Ala Ser Asp Val Trp Thr Tyr Gly Phe Gly Ala Asp Ala Leu 590 595 600 tat aac ttc atc aac gat aaa gcc acc aat ttc tta ggc aaa aac aac 2281 Tyr Asn Phe Ile Asn Asp Lys Ala Thr Asn Phe Leu Gly Lys Asn Asn 605 610 615 aag ctt tct ttg ggg ctt ttt ggc ggg att gcg tta gcg ggc act tca 2329 Lys Leu Ser Leu Gly Leu Phe Gly Gly Ile Ala Leu Ala Gly Thr Ser 620 625 630 635 tgg ctc aat tct gag tac gtg aat tta gcc acc gtg aat aac gtc tat 2377 Trp Leu Asn Ser Glu Tyr Val Asn Leu Ala Thr Val Asn Asn Val Tyr 640 645 650 aac gct aaa atg aat gtg gcg aat ttc caa ttc tta ttc aat atg gga 2425 Asn Ala Lys Met Asn Val Ala Asn Phe Gln Phe Leu Phe Asn Met Gly 655 660 665 gtg agg atg aat tta gcc aga tcc aag aaa aaa ggc agc gat cat gca 2473 Val Arg Met Asn Leu Ala Arg Ser Lys Lys Lys Gly Ser Asp His Ala 670 675 680 gct cag cat ggg att gag tta ggg ctt aaa atc ccc acc atc aac acg 2521 Ala Gln His Gly Ile Glu Leu Gly Leu Lys Ile Pro Thr Ile Asn Thr 685 690 695 aac tat tat tcc ttt atg ggg gct gaa ctc aaa tac aga agg ctc tat 2569 Asn Tyr Tyr Ser Phe Met Gly Ala Glu Leu Lys Tyr Arg Arg Leu Tyr 700 705 710 715 agc gtg tat ttg aat nat gtg ttc gct tac taagcttttt gtgaaactcc 2619 Ser Val Tyr Leu Asn Xaa Val Phe Ala Tyr 720 725 ctttttaagg ggtttttttt tgaactctct tttaaattct ctttttaaag agatttcttt 2679 ttttaagctt ttttttgaac ttttttttga attctttgtt tttaagcttt ttttaaaccc 2739 tttcgttttt aaactccctt ttttaaggga tttctttttt tgaactccct tttttgaacc 2799 ctttttttta aaccctcttt ttttaagggg tttcttttta aagctttttt gaagtctttt 2859 tttaaattct ttttttgggg gtttgatctt tctttttgcc aatccccact actttc 2915 <200> SEQUENCE CHARACTERISTICS: <210> SEQ ID NO 6 <211> LENGTH: 745 <212> TYPE: PRT <213> ORGANISM: Helicobacter pylori <220> FEATURE: <221> NAME/KEY: SIGNAL <222> LOCATION: (1)...(20) <220> FEATURE: <221> NAME/KEY: VARIANT <222> LOCATION: 721 <223> OTHER INFORMATION: Xaa = Any Amino Acid <400> SEQUENCE: 6 Met Lys Lys His Ile Leu Ser Leu Ala Leu Gly Ser Leu Leu Val Ser -20 -15 -10 -5 Thr Leu Ser Ala Glu Asp Asp Gly Phe Tyr Thr Ser Val Gly Tyr Gln 1 5 10 Ile Gly Glu Ala Ala Gln Met Val Thr Asn Thr Lys Gly Ile Gln Gln 15 20 25 Leu Ser Asp Asn Tyr Glu Asn Leu Asn Asn Leu Leu Thr Arg Tyr Ser 30 35 40 Thr Leu Asn Thr Leu Ile Lys Leu Ser Ala Asp Pro Ser Ala Ile Asn 45 50 55 60 Ala Val Arg Glu Asn Leu Gly Ala Ser Thr Lys Asn Leu Ile Gly Asp 65 70 75 Lys Ala Asn Ser Pro Ala Tyr Gln Ala Val Phe Leu Ala Ile Asn Ala 80 85 90 Ala Val Gly Leu Trp Asn Thr Ile Gly Tyr Ala Val Met Cys Gly Asn 95 100 105 Gly Asn Gly Thr Glu Ser Gly Pro Gly Ser Val Ile Phe Asn Asp Gln 110 115 120 Pro Gly Gln Asp Ser Thr Gln Ile Thr Cys Asn Arg Phe Glu Ser Thr 125 130 135 140 Gly Pro Gly Lys Ser Met Ser Ile Asp Glu Phe Lys Lys Leu Asn Glu 145 150 155 Ala Tyr Gln Ile Ile Gln Gln Ala Leu Lys Asn Gln Ser Gly Phe Pro 160 165 170 Glu Leu Gly Gly Asn Gly Thr Lys Val Ser Val Asn Tyr Asn Tyr Glu 175 180 185 Cys Arg Gln Thr Ala Asp Ile Asn Gly Gly Val Tyr Gln Phe Cys Lys 190 195 200 Ala Lys Asn Gly Ser Ser Ser Ser Ser Asn Gly Gly Asn Gly Ser Ser 205 210 215 220 Thr Gln Thr Thr Ala Thr Thr Thr Gln Asp Gly Val Thr Ile Thr Thr 225 230 235 Thr Tyr Asn Asn Asn Lys Ala Thr Val Lys Phe Asp Ile Thr Asn Asn 240 245 250 Ala Glu Gln Leu Leu Asn Gln Ala Ala Asn Ile Met Gln Val Leu Asn 255 260 265 Thr Gln Cys Pro Leu Val Arg Ser Thr Asn Asn Glu Asn Thr Pro Gly 270 275 280 Gly Gly Gln Pro Trp Gly Leu Ser Thr Ser Gly Asn Ala Cys Ser Ile 285 290 295 300 Phe Gln Gln Glu Phe Ser Gln Val Thr Ser Met Ile Lys Asn Ala Gln 305 310 315 Glu Ile Ile Ala Gln Ser Lys Ile Val Ser Glu Asn Ala Gln Asn Gln 320 325 330 Asn Asn Leu Asp Thr Gly Lys Pro Phe Asn Pro Tyr Thr Asp Ala Ser 335 340 345 Phe Ala Gln Ser Met Leu Lys Asn Ala Gln Ala Gln Ala Glu Met Phe 350 355 360 Asn Leu Ser Glu Gln Val Lys Lys Asn Leu Glu Val Met Lys Asn Asn 365 370 375 380 Asn Asn Val Asn Glu Lys Leu Ala Gly Phe Gly Lys Glu Glu Val Met 385 390 395 Thr Asn Phe Val Ser Ala Phe Leu Ala Ser Cys Lys Asp Gly Gly Thr 400 405 410 Leu Pro Asn Ala Gly Val Thr Ser Asn Thr Trp Gly Ala Gly Cys Ala 415 420 425 Tyr Val Gly Glu Thr Ile Ser Ala Leu Thr Asn Ser Ile Ala His Phe 430 435 440 Gly Thr Gln Glu Gln Gln Ile Gln Gln Ala Glu Asn Ile Ala Asp Thr 445 450 455 460 Leu Val Asn Phe Lys Ser Arg Tyr Ser Glu Leu Gly Asn Thr Tyr Asn 465 470 475 Ser Ile Thr Thr Ala Leu Ser Lys Val Pro Asn Ala Gln Ser Leu Gln 480 485 490 Asn Val Val Ser Lys Lys Asn Asn Pro Tyr Ser Pro Gln Gly Ile Glu 495 500 505 Thr Asn Tyr Tyr Leu Asn Gln Asn Ser Tyr Asn Gln Ile Gln Thr Ile 510 515 520 Asn Gln Glu Leu Gly Arg Asn Pro Phe Arg Lys Val Gly Ile Val Asn 525 530 535 540 Ser Gln Thr Asn Asn Gly Ala Met Asn Gly Ile Gly Ile Gln Val Gly 545 550 555 Tyr Lys Gln Phe Phe Gly Gln Lys Arg Lys Trp Gly Ala Arg Tyr Tyr 560 565 570 Gly Phe Phe Asp Tyr Asn His Ala Phe Ile Lys Ser Ser Phe Phe Asn 575 580 585 Ser Ala Ser Asp Val Trp Thr Tyr Gly Phe Gly Ala Asp Ala Leu Tyr 590 595 600 Asn Phe Ile Asn Asp Lys Ala Thr Asn Phe Leu Gly Lys Asn Asn Lys 605 610 615 620 Leu Ser Leu Gly Leu Phe Gly Gly Ile Ala Leu Ala Gly Thr Ser Trp 625 630 635 Leu Asn Ser Glu Tyr Val Asn Leu Ala Thr Val Asn Asn Val Tyr Asn 640 645 650 Ala Lys Met Asn Val Ala Asn Phe Gln Phe Leu Phe Asn Met Gly Val 655 660 665 Arg Met Asn Leu Ala Arg Ser Lys Lys Lys Gly Ser Asp His Ala Ala 670 675 680 Gln His Gly Ile Glu Leu Gly Leu Lys Ile Pro Thr Ile Asn Thr Asn 685 690 695 700 Tyr Tyr Ser Phe Met Gly Ala Glu Leu Lys Tyr Arg Arg Leu Tyr Ser 705 710 715 Val Tyr Leu Asn Xaa Val Phe Ala Tyr 720 725 <200> SEQUENCE CHARACTERISTICS: <210> SEQ ID NO 7 <211> LENGTH: 2603 <212> TYPE: DNA <213> ORGANISM: Helicobacter pylori <220> FEATURE: <221> NAME/KEY: CDS <222> LOCATION: (210)...(2342) <220> FEATURE: <221> NAME/KEY: sig_peptide <222> LOCATION: (210)...(270) <400> SEQUENCE: 7 atgaccttta ttggtttaat atttgtttag aaataacaca aaaacctttt tttttttttt 60 tgaaagggca aaaacgccta attaatatca aaatcccatg aatttatact atattaacga 120 aagcttgcgg tatggtttca cctaaagaca cacttccgca agatttacta acaatttcaa 180 tcttatttca agtaataaaa ggagaaaac atg aag aaa aaa ttt ctg tca tta 233 Met Lys Lys Lys Phe Leu Ser Leu -20 -15 acc tta ggt tcg ctt tta gtt tcc gct tta agc gct gaa gac aac ggc 281 Thr Leu Gly Ser Leu Leu Val Ser Ala Leu Ser Ala Glu Asp Asn Gly -10 -5 1 ttt ttt gtg agt gcg ggc tat caa atc ggt gaa tcc gct caa atg gtg 329 Phe Phe Val Ser Ala Gly Tyr Gln Ile Gly Glu Ser Ala Gln Met Val 5 10 15 20 aaa aac act aaa ggc att caa gat ctt tca gat agc tat gaa aga ctg 377 Lys Asn Thr Lys Gly Ile Gln Asp Leu Ser Asp Ser Tyr Glu Arg Leu 25 30 35 aac aat ctt tta acg agt tat agt gcc cta aac act ctt att agg cag 425 Asn Asn Leu Leu Thr Ser Tyr Ser Ala Leu Asn Thr Leu Ile Arg Gln 40 45 50 tcc gcc gac ccc aac gct atc aat aac gca agg ggc aat ttg aac gct 473 Ser Ala Asp Pro Asn Ala Ile Asn Asn Ala Arg Gly Asn Leu Asn Ala 55 60 65 agt gcg aag aat ttg atc aat gat aaa aag aat tcc ccg gcg tat caa 521 Ser Ala Lys Asn Leu Ile Asn Asp Lys Lys Asn Ser Pro Ala Tyr Gln 70 75 80 gcg gtg ctt tta gcc ttg aat gcg gca gcg ggg ttg tgg caa gtc atg 569 Ala Val Leu Leu Ala Leu Asn Ala Ala Ala Gly Leu Trp Gln Val Met 85 90 95 100 agc tat tcg atc agc gtt tgt ggc cct ggc tct gac aaa aat aaa aat 617 Ser Tyr Ser Ile Ser Val Cys Gly Pro Gly Ser Asp Lys Asn Lys Asn 105 110 115 ggg ggc gtc caa acc ttt gaa aat gtg ccg tca aat ggg ggg act acc 665 Gly Gly Val Gln Thr Phe Glu Asn Val Pro Ser Asn Gly Gly Thr Thr 120 125 130 att gct tgc gat tca ttt tat gaa cca gga aag tgg agc ggt ata tcc 713 Ile Ala Cys Asp Ser Phe Tyr Glu Pro Gly Lys Trp Ser Gly Ile Ser 135 140 145 act gaa aat tac gca aaa atc aat aaa gcc tat caa atc atc caa aag 761 Thr Glu Asn Tyr Ala Lys Ile Asn Lys Ala Tyr Gln Ile Ile Gln Lys 150 155 160 gct ttt gga gca agc ggg caa gat att cct gcc tta agc gac acc aaa 809 Ala Phe Gly Ala Ser Gly Gln Asp Ile Pro Ala Leu Ser Asp Thr Lys 165 170 175 180 gaa ctt aat ttt gaa att aaa ggg aaa aaa aat gat agc gtc cag cca 857 Glu Leu Asn Phe Glu Ile Lys Gly Lys Lys Asn Asp Ser Val Gln Pro 185 190 195 gga gaa aga tgg aaa ttc cca tgg act aat gga aaa ttt gtt tca gtc 905 Gly Glu Arg Trp Lys Phe Pro Trp Thr Asn Gly Lys Phe Val Ser Val 200 205 210 aag tgg gtg aat ggg aag tat gaa gaa att aaa gaa gac atc aaa gtg 953 Lys Trp Val Asn Gly Lys Tyr Glu Glu Ile Lys Glu Asp Ile Lys Val 215 220 225 tca aat aac gct caa gag ctt tta aaa cag gct agc act att tta acc 1001 Ser Asn Asn Ala Gln Glu Leu Leu Lys Gln Ala Ser Thr Ile Leu Thr 230 235 240 act ctt aat gaa gca tgc cca tgg ttg agt aat ggt ggt gca ggc aat 1049 Thr Leu Asn Glu Ala Cys Pro Trp Leu Ser Asn Gly Gly Ala Gly Asn 245 250 255 260 gtg gcc ggt ggc aat agt tta tgg gcc gga ata gat aaa ggc gac ggg 1097 Val Ala Gly Gly Asn Ser Leu Trp Ala Gly Ile Asp Lys Gly Asp Gly 265 270 275 agc gca tgc ggg att ttt aaa aat gaa atc agc gcg att caa gac atg 1145 Ser Ala Cys Gly Ile Phe Lys Asn Glu Ile Ser Ala Ile Gln Asp Met 280 285 290 atc aaa aac gct gaa ata gcc gta gag caa tcc aaa atc gtt acc gcc 1193 Ile Lys Asn Ala Glu Ile Ala Val Glu Gln Ser Lys Ile Val Thr Ala 295 300 305 aac gcg caa aac cag cac aac cta gac act ggg aaa gca ttc aac ccc 1241 Asn Ala Gln Asn Gln His Asn Leu Asp Thr Gly Lys Ala Phe Asn Pro 310 315 320 tat aaa gac gcc aac ttc gcc caa agc atg ttc gct aac gct aga gcg 1289 Tyr Lys Asp Ala Asn Phe Ala Gln Ser Met Phe Ala Asn Ala Arg Ala 325 330 335 340 caa gcg gag att tta aac cgc gct caa gca gtg gtg aag gac ttt gaa 1337 Gln Ala Glu Ile Leu Asn Arg Ala Gln Ala Val Val Lys Asp Phe Glu 345 350 355 aga atc cct gca gcg ttc gtg aaa gac tct tta gga gta tgc cat gaa 1385 Arg Ile Pro Ala Ala Phe Val Lys Asp Ser Leu Gly Val Cys His Glu 360 365 370 aag ggt agc gac ggc aat ctc cgt ggc acg cca tct ggc acg gtt act 1433 Lys Gly Ser Asp Gly Asn Leu Arg Gly Thr Pro Ser Gly Thr Val Thr 375 380 385 tct aac act tgg gga gcc ggc tgc gcg tat gtg gga gaa acc gta acg 1481 Ser Asn Thr Trp Gly Ala Gly Cys Ala Tyr Val Gly Glu Thr Val Thr 390 395 400 aat cta aaa aac agc atc gct cat ttt ggc gac caa gcg gag cga atc 1529 Asn Leu Lys Asn Ser Ile Ala His Phe Gly Asp Gln Ala Glu Arg Ile 405 410 415 420 cat aat gcg cga aat ctc gcc tac act tta gcg aat ttc agc ggc cag 1577 His Asn Ala Arg Asn Leu Ala Tyr Thr Leu Ala Asn Phe Ser Gly Gln 425 430 435 tac aaa aag cta ggc gaa cac tat gac agc atc aca gcg gcg ctc tct 1625 Tyr Lys Lys Leu Gly Glu His Tyr Asp Ser Ile Thr Ala Ala Leu Ser 440 445 450 agc ttg cct gat gcg caa tct tta caa aat gtg gtg agc aaa aag act 1673 Ser Leu Pro Asp Ala Gln Ser Leu Gln Asn Val Val Ser Lys Lys Thr 455 460 465 aac cct aac agc ccg caa ggc ata cag gat aat tac tac att gac tcc 1721 Asn Pro Asn Ser Pro Gln Gly Ile Gln Asp Asn Tyr Tyr Ile Asp Ser 470 475 480 aac atc cat tct caa gtg caa tct agg agt caa gaa ctc ggc agt aac 1769 Asn Ile His Ser Gln Val Gln Ser Arg Ser Gln Glu Leu Gly Ser Asn 485 490 495 500 cct ttc aga cgc gcc ggg cta atc gcc gct tct acc acc aat aac ggc 1817 Pro Phe Arg Arg Ala Gly Leu Ile Ala Ala Ser Thr Thr Asn Asn Gly 505 510 515 gcg atg aat ggg att ggc ttt caa gtg ggc tat aag caa ttc ttt ggg 1865 Ala Met Asn Gly Ile Gly Phe Gln Val Gly Tyr Lys Gln Phe Phe Gly 520 525 530 aaa aac aaa cga tgg ggc gcg aga tac tac ggc ttt gtg gat tac aac 1913 Lys Asn Lys Arg Trp Gly Ala Arg Tyr Tyr Gly Phe Val Asp Tyr Asn 535 540 545 cac acc tat aac aag tcc caa ttt ttc aac tcc gat tct gat gtt tgg 1961 His Thr Tyr Asn Lys Ser Gln Phe Phe Asn Ser Asp Ser Asp Val Trp 550 555 560 act tat ggc gtg ggg agc gat ttg tta gtg aat ttc atc aac gat aaa 2009 Thr Tyr Gly Val Gly Ser Asp Leu Leu Val Asn Phe Ile Asn Asp Lys 565 570 575 580 gcc act aaa cac aat aaa att tct ttt ggc gcg ttt ggc ggt atc caa 2057 Ala Thr Lys His Asn Lys Ile Ser Phe Gly Ala Phe Gly Gly Ile Gln 585 590 595 cta gcc ggg act tca tgg ctt aat tct cag tat gtg aat tta gcg aat 2105 Leu Ala Gly Thr Ser Trp Leu Asn Ser Gln Tyr Val Asn Leu Ala Asn 600 605 610 gtg aac aat tat tat aaa gct aaa atc aac acc tct aac ttc caa ttc 2153 Val Asn Asn Tyr Tyr Lys Ala Lys Ile Asn Thr Ser Asn Phe Gln Phe 615 620 625 tta ttc aat ctg ggc tta agg acc aat ctc gcc aga aat aaa aga ata 2201 Leu Phe Asn Leu Gly Leu Arg Thr Asn Leu Ala Arg Asn Lys Arg Ile 630 635 640 ggc gct gat cat agc gcg caa cat ggc atg gaa tta ggc gtg aag atc 2249 Gly Ala Asp His Ser Ala Gln His Gly Met Glu Leu Gly Val Lys Ile 645 650 655 660 ccc acg atc aac aca aat tac tat tct ttg cta ggc act acc ttg caa 2297 Pro Thr Ile Asn Thr Asn Tyr Tyr Ser Leu Leu Gly Thr Thr Leu Gln 665 670 675 tac aga agg ctt tat agc gtg tat ctc aac tat gtg ttt gct tac 2342 Tyr Arg Arg Leu Tyr Ser Val Tyr Leu Asn Tyr Val Phe Ala Tyr 680 685 690 taaaagctta aactcctttt taaactccct ttttaggggg tttaatcttt ttaactgact 2402 tttcttttag ctttttttaa ttttttccac caaacaaagt tttttgactt caagcgttaa 2462 tcacaaaaaa tactcaaagg cgttttttgc aatctaaata aaaaattagc gttattcaag 2522 cgatcatttt aaaccaccca agcaagaaac cccaaacatc tttagcgttc gcgcgctcca 2582 ctaaccaaaa aacgccccaa a 2603 <200> SEQUENCE CHARACTERISTICS: <210> SEQ ID NO 8 <211> LENGTH: 711 <212> TYPE: PRT <213> ORGANISM: Helicobacter pylori <220> FEATURE: <221> NAME/KEY: SIGNAL <222> LOCATION: (1)...(20) <400> SEQUENCE: 8 Met Lys Lys Lys Phe Leu Ser Leu Thr Leu Gly Ser Leu Leu Val Ser -20 -15 -10 -5 Ala Leu Ser Ala Glu Asp Asn Gly Phe Phe Val Ser Ala Gly Tyr Gln 1 5 10 Ile Gly Glu Ser Ala Gln Met Val Lys Asn Thr Lys Gly Ile Gln Asp 15 20 25 Leu Ser Asp Ser Tyr Glu Arg Leu Asn Asn Leu Leu Thr Ser Tyr Ser 30 35 40 Ala Leu Asn Thr Leu Ile Arg Gln Ser Ala Asp Pro Asn Ala Ile Asn 45 50 55 60 Asn Ala Arg Gly Asn Leu Asn Ala Ser Ala Lys Asn Leu Ile Asn Asp 65 70 75 Lys Lys Asn Ser Pro Ala Tyr Gln Ala Val Leu Leu Ala Leu Asn Ala 80 85 90 Ala Ala Gly Leu Trp Gln Val Met Ser Tyr Ser Ile Ser Val Cys Gly 95 100 105 Pro Gly Ser Asp Lys Asn Lys Asn Gly Gly Val Gln Thr Phe Glu Asn 110 115 120 Val Pro Ser Asn Gly Gly Thr Thr Ile Ala Cys Asp Ser Phe Tyr Glu 125 130 135 140 Pro Gly Lys Trp Ser Gly Ile Ser Thr Glu Asn Tyr Ala Lys Ile Asn 145 150 155 Lys Ala Tyr Gln Ile Ile Gln Lys Ala Phe Gly Ala Ser Gly Gln Asp 160 165 170 Ile Pro Ala Leu Ser Asp Thr Lys Glu Leu Asn Phe Glu Ile Lys Gly 175 180 185 Lys Lys Asn Asp Ser Val Gln Pro Gly Glu Arg Trp Lys Phe Pro Trp 190 195 200 Thr Asn Gly Lys Phe Val Ser Val Lys Trp Val Asn Gly Lys Tyr Glu 205 210 215 220 Glu Ile Lys Glu Asp Ile Lys Val Ser Asn Asn Ala Gln Glu Leu Leu 225 230 235 Lys Gln Ala Ser Thr Ile Leu Thr Thr Leu Asn Glu Ala Cys Pro Trp 240 245 250 Leu Ser Asn Gly Gly Ala Gly Asn Val Ala Gly Gly Asn Ser Leu Trp 255 260 265 Ala Gly Ile Asp Lys Gly Asp Gly Ser Ala Cys Gly Ile Phe Lys Asn 270 275 280 Glu Ile Ser Ala Ile Gln Asp Met Ile Lys Asn Ala Glu Ile Ala Val 285 290 295 300 Glu Gln Ser Lys Ile Val Thr Ala Asn Ala Gln Asn Gln His Asn Leu 305 310 315 Asp Thr Gly Lys Ala Phe Asn Pro Tyr Lys Asp Ala Asn Phe Ala Gln 320 325 330 Ser Met Phe Ala Asn Ala Arg Ala Gln Ala Glu Ile Leu Asn Arg Ala 335 340 345 Gln Ala Val Val Lys Asp Phe Glu Arg Ile Pro Ala Ala Phe Val Lys 350 355 360 Asp Ser Leu Gly Val Cys His Glu Lys Gly Ser Asp Gly Asn Leu Arg 365 370 375 380 Gly Thr Pro Ser Gly Thr Val Thr Ser Asn Thr Trp Gly Ala Gly Cys 385 390 395 Ala Tyr Val Gly Glu Thr Val Thr Asn Leu Lys Asn Ser Ile Ala His 400 405 410 Phe Gly Asp Gln Ala Glu Arg Ile His Asn Ala Arg Asn Leu Ala Tyr 415 420 425 Thr Leu Ala Asn Phe Ser Gly Gln Tyr Lys Lys Leu Gly Glu His Tyr 430 435 440 Asp Ser Ile Thr Ala Ala Leu Ser Ser Leu Pro Asp Ala Gln Ser Leu 445 450 455 460 Gln Asn Val Val Ser Lys Lys Thr Asn Pro Asn Ser Pro Gln Gly Ile 465 470 475 Gln Asp Asn Tyr Tyr Ile Asp Ser Asn Ile His Ser Gln Val Gln Ser 480 485 490 Arg Ser Gln Glu Leu Gly Ser Asn Pro Phe Arg Arg Ala Gly Leu Ile 495 500 505 Ala Ala Ser Thr Thr Asn Asn Gly Ala Met Asn Gly Ile Gly Phe Gln 510 515 520 Val Gly Tyr Lys Gln Phe Phe Gly Lys Asn Lys Arg Trp Gly Ala Arg 525 530 535 540 Tyr Tyr Gly Phe Val Asp Tyr Asn His Thr Tyr Asn Lys Ser Gln Phe 545 550 555 Phe Asn Ser Asp Ser Asp Val Trp Thr Tyr Gly Val Gly Ser Asp Leu 560 565 570 Leu Val Asn Phe Ile Asn Asp Lys Ala Thr Lys His Asn Lys Ile Ser 575 580 585 Phe Gly Ala Phe Gly Gly Ile Gln Leu Ala Gly Thr Ser Trp Leu Asn 590 595 600 Ser Gln Tyr Val Asn Leu Ala Asn Val Asn Asn Tyr Tyr Lys Ala Lys 605 610 615 620 Ile Asn Thr Ser Asn Phe Gln Phe Leu Phe Asn Leu Gly Leu Arg Thr 625 630 635 Asn Leu Ala Arg Asn Lys Arg Ile Gly Ala Asp His Ser Ala Gln His 640 645 650 Gly Met Glu Leu Gly Val Lys Ile Pro Thr Ile Asn Thr Asn Tyr Tyr 655 660 665 Ser Leu Leu Gly Thr Thr Leu Gln Tyr Arg Arg Leu Tyr Ser Val Tyr 670 675 680 Leu Asn Tyr Val Phe Ala Tyr 685 690 <200> SEQUENCE CHARACTERISTICS: <210> SEQ ID NO 9 <211> LENGTH: 2427 <212> TYPE: DNA <213> ORGANISM: Helicobacter pylori <220> FEATURE: <221> NAME/KEY: CDS <222> LOCATION: (232)...(2247) <220> FEATURE: <221> NAME/KEY: sig_peptide <222> LOCATION: (232)...(292) <400> SEQUENCE: 9 aaaacgcgca gcaaaaaatc tctgttaagc ttttatcatt agcgttccat tgaaacaaaa 60 tctaaaaacc ctttccaata ccacccaaac aaacgcgcaa aaaatgcaaa aattctaaat 120 tttctccaaa tgacaaaaaa aaaaaaaacg attttatgct acaatgcttt taatacattc 180 ttacttaatg tataaaatct caatcactca atttaatttc aaaggatatt t atg aaa 237 Met Lys -20 aaa acc ctt tta ctc tct ctc tct ctc tct ctc tcg tca tcg ctt tta 285 Lys Thr Leu Leu Leu Ser Leu Ser Leu Ser Leu Ser Ser Ser Leu Leu -15 -10 -5 aac gct gaa gac aac ggc ttt ttt atc agc gcg ggc tat caa atc ggt 333 Asn Ala Glu Asp Asn Gly Phe Phe Ile Ser Ala Gly Tyr Gln Ile Gly 1 5 10 gaa gcc gct caa atg gtg aaa aac acc ggc gaa ttg aaa aaa ctt tca 381 Glu Ala Ala Gln Met Val Lys Asn Thr Gly Glu Leu Lys Lys Leu Ser 15 20 25 30 gac act tat gag aat ttg agc aac ctt tta acc aat ttt aac aac ctc 429 Asp Thr Tyr Glu Asn Leu Ser Asn Leu Leu Thr Asn Phe Asn Asn Leu 35 40 45 aat caa gcg gta acg aac gcg agc agc cct tca gaa atc aat gcc acg 477 Asn Gln Ala Val Thr Asn Ala Ser Ser Pro Ser Glu Ile Asn Ala Thr 50 55 60 atc gat aat tta aaa gca aac acg caa ggg ctg att ggc gaa aaa acc 525 Ile Asp Asn Leu Lys Ala Asn Thr Gln Gly Leu Ile Gly Glu Lys Thr 65 70 75 aat tcc ccg gcg tat caa gcg gtg tat ttg gcg ctc aat gcg gcg gtg 573 Asn Ser Pro Ala Tyr Gln Ala Val Tyr Leu Ala Leu Asn Ala Ala Val 80 85 90 ggg ctg tgg aat gtg ata gcc tat aat gtc caa tgc ggt cct ggt aag 621 Gly Leu Trp Asn Val Ile Ala Tyr Asn Val Gln Cys Gly Pro Gly Lys 95 100 105 110 agt ggg gat caa agc gta att ttt gat ggc caa cca gga cat gat tca 669 Ser Gly Asp Gln Ser Val Ile Phe Asp Gly Gln Pro Gly His Asp Ser 115 120 125 aga tcc att aat tgc aat tta acc ggt tat aac aac ggg gtt agc ggc 717 Arg Ser Ile Asn Cys Asn Leu Thr Gly Tyr Asn Asn Gly Val Ser Gly 130 135 140 cct tta tcc att gac aat ttt aaa acg ctt aat caa gct tat caa act 765 Pro Leu Ser Ile Asp Asn Phe Lys Thr Leu Asn Gln Ala Tyr Gln Thr 145 150 155 atc caa caa gct tta aaa caa gat agc gga ttt cct gtt ttg gat agt 813 Ile Gln Gln Ala Leu Lys Gln Asp Ser Gly Phe Pro Val Leu Asp Ser 160 165 170 aaa gga aaa caa gta act ata aaa ata aca aca caa act aat gga gct 861 Lys Gly Lys Gln Val Thr Ile Lys Ile Thr Thr Gln Thr Asn Gly Ala 175 180 185 190 aat aaa agt gaa act act act act act act act act aat gac gct caa 909 Asn Lys Ser Glu Thr Thr Thr Thr Thr Thr Thr Thr Asn Asp Ala Gln 195 200 205 acc ctt ttg caa gaa gcc agt aaa atg ata agc gtc ctc act aca aac 957 Thr Leu Leu Gln Glu Ala Ser Lys Met Ile Ser Val Leu Thr Thr Asn 210 215 220 tgc cca tgg gta aat acc gct cat aac tca aac ggg ggt gca ccg tgg 1005 Cys Pro Trp Val Asn Thr Ala His Asn Ser Asn Gly Gly Ala Pro Trp 225 230 235 aat tta aat acg aca ggg aat gtg tgt cag gtt ttt gcc acg gag ttt 1053 Asn Leu Asn Thr Thr Gly Asn Val Cys Gln Val Phe Ala Thr Glu Phe 240 245 250 agc gcc gtt act agc atg atc aaa aac gcg caa gaa atc gta acg caa 1101 Ser Ala Val Thr Ser Met Ile Lys Asn Ala Gln Glu Ile Val Thr Gln 255 260 265 270 gct caa agc ctt aac aac ccg caa agc aat caa aac gcg ccg aaa gat 1149 Ala Gln Ser Leu Asn Asn Pro Gln Ser Asn Gln Asn Ala Pro Lys Asp 275 280 285 ttc aat cct tac acc tct gct gat agg gct ttc gct caa aac atg ctc 1197 Phe Asn Pro Tyr Thr Ser Ala Asp Arg Ala Phe Ala Gln Asn Met Leu 290 295 300 aat cac gcg caa gcg caa gcc aag atg ctt gaa cta gcc gat caa atg 1245 Asn His Ala Gln Ala Gln Ala Lys Met Leu Glu Leu Ala Asp Gln Met 305 310 315 aaa aaa gac ctt aac act atc cca aaa caa ttt atc aca aac tac ttg 1293 Lys Lys Asp Leu Asn Thr Ile Pro Lys Gln Phe Ile Thr Asn Tyr Leu 320 325 330 gca gct tgc cgc aat ggg ggt ggg aca tta cct gat gca ggg gtt act 1341 Ala Ala Cys Arg Asn Gly Gly Gly Thr Leu Pro Asp Ala Gly Val Thr 335 340 345 350 tct aac act tgg ggg gcc ggt tgc gcc tat gtg gaa gag acg ata acc 1389 Ser Asn Thr Trp Gly Ala Gly Cys Ala Tyr Val Glu Glu Thr Ile Thr 355 360 365 gcc cta aat aac agc ctt gcg cat ttt ggc act caa gcc gat caa atc 1437 Ala Leu Asn Asn Ser Leu Ala His Phe Gly Thr Gln Ala Asp Gln Ile 370 375 380 aag caa tct gag ttg ttg gcg cgc acg ata ctt gat ttt aga ggc agc 1485 Lys Gln Ser Glu Leu Leu Ala Arg Thr Ile Leu Asp Phe Arg Gly Ser 385 390 395 ctt aag gat tta aac aac act tat aac agc atc acc acg acc gct tca 1533 Leu Lys Asp Leu Asn Asn Thr Tyr Asn Ser Ile Thr Thr Thr Ala Ser 400 405 410 aac acg ccc aat tcc cca ttc ctt aaa aat ttg ata agc caa tcc act 1581 Asn Thr Pro Asn Ser Pro Phe Leu Lys Asn Leu Ile Ser Gln Ser Thr 415 420 425 430 aac cct aat aac ccc ggg ggc tta cag gcc gtt tat caa gtc aac caa 1629 Asn Pro Asn Asn Pro Gly Gly Leu Gln Ala Val Tyr Gln Val Asn Gln 435 440 445 agc gct tat tcg caa tta tta agc gcc acg caa gaa tta ggg cat aac 1677 Ser Ala Tyr Ser Gln Leu Leu Ser Ala Thr Gln Glu Leu Gly His Asn 450 455 460 cct ttc aga cgc gtt ggc tta atc agc tct caa acc aac aac ggt gcg 1725 Pro Phe Arg Arg Val Gly Leu Ile Ser Ser Gln Thr Asn Asn Gly Ala 465 470 475 atg aat ggg atc ggc gtg caa ata ggg tat aaa caa ttt ttt ggt gaa 1773 Met Asn Gly Ile Gly Val Gln Ile Gly Tyr Lys Gln Phe Phe Gly Glu 480 485 490 aaa aga aga tgg ggg tta agg tat tat ggt ttt ttt gat tac aac cat 1821 Lys Arg Arg Trp Gly Leu Arg Tyr Tyr Gly Phe Phe Asp Tyr Asn His 495 500 505 510 gct tat atc aaa tcc agc ttt ttc aac tcc gcc tct gat gtg ttc act 1869 Ala Tyr Ile Lys Ser Ser Phe Phe Asn Ser Ala Ser Asp Val Phe Thr 515 520 525 tat ggg gta gga aca gat gtc ctc tat aac ttt atc aac gat aaa gcc 1917 Tyr Gly Val Gly Thr Asp Val Leu Tyr Asn Phe Ile Asn Asp Lys Ala 530 535 540 acc aaa aac aat aag att tct ttt ggg gtg ttt ggg ggg att gcg tta 1965 Thr Lys Asn Asn Lys Ile Ser Phe Gly Val Phe Gly Gly Ile Ala Leu 545 550 555 gct ggc act tcg tgg ctt aat tct caa tac gtg aat tta gcg aca ttc 2013 Ala Gly Thr Ser Trp Leu Asn Ser Gln Tyr Val Asn Leu Ala Thr Phe 560 565 570 aat aat ttt tac agc gct aaa atg aat gtg gcg aat ttc caa ttc tta 2061 Asn Asn Phe Tyr Ser Ala Lys Met Asn Val Ala Asn Phe Gln Phe Leu 575 580 585 590 ttc aac ttg ggc ttg aga atg aat ctc gct aaa aac aaa aag aaa gcg 2109 Phe Asn Leu Gly Leu Arg Met Asn Leu Ala Lys Asn Lys Lys Lys Ala 595 600 605 agc gat cat gta gct cag cat ggc gtg gaa cta ggc gtg aag atc cct 2157 Ser Asp His Val Ala Gln His Gly Val Glu Leu Gly Val Lys Ile Pro 610 615 620 acg atc aac acg aat tac tat tct ttg cta ggc act caa ctc caa tac 2205 Thr Ile Asn Thr Asn Tyr Tyr Ser Leu Leu Gly Thr Gln Leu Gln Tyr 625 630 635 cgc agg ctt tat agc gtg tat ttg aat tat gtg ttt gct tac 2247 Arg Arg Leu Tyr Ser Val Tyr Leu Asn Tyr Val Phe Ala Tyr 640 645 650 taatatctgt ctttttgtga aactcccttt ttaagggatt ttttttgaag cctttctttt 2307 tttaaaccct cttttttggg ggtcaagcgt aaaattcacc cctatccctt taagaaaata 2367 aaataaaaga aaatgcgttt tataacaaaa taagatctaa aacaataaaa caaaaaccca 2427 <200> SEQUENCE CHARACTERISTICS: <210> SEQ ID NO 10 <211> LENGTH: 672 <212> TYPE: PRT <213> ORGANISM: Helicobacter pylori <220> FEATURE: <221> NAME/KEY: SIGNAL <222> LOCATION: (1)...(20) <400> SEQUENCE: 10 Met Lys Lys Thr Leu Leu Leu Ser Leu Ser Leu Ser Leu Ser Ser Ser -20 -15 -10 -5 Leu Leu Asn Ala Glu Asp Asn Gly Phe Phe Ile Ser Ala Gly Tyr Gln 1 5 10 Ile Gly Glu Ala Ala Gln Met Val Lys Asn Thr Gly Glu Leu Lys Lys 15 20 25 Leu Ser Asp Thr Tyr Glu Asn Leu Ser Asn Leu Leu Thr Asn Phe Asn 30 35 40 Asn Leu Asn Gln Ala Val Thr Asn Ala Ser Ser Pro Ser Glu Ile Asn 45 50 55 60 Ala Thr Ile Asp Asn Leu Lys Ala Asn Thr Gln Gly Leu Ile Gly Glu 65 70 75 Lys Thr Asn Ser Pro Ala Tyr Gln Ala Val Tyr Leu Ala Leu Asn Ala 80 85 90 Ala Val Gly Leu Trp Asn Val Ile Ala Tyr Asn Val Gln Cys Gly Pro 95 100 105 Gly Lys Ser Gly Asp Gln Ser Val Ile Phe Asp Gly Gln Pro Gly His 110 115 120 Asp Ser Arg Ser Ile Asn Cys Asn Leu Thr Gly Tyr Asn Asn Gly Val 125 130 135 140 Ser Gly Pro Leu Ser Ile Asp Asn Phe Lys Thr Leu Asn Gln Ala Tyr 145 150 155 Gln Thr Ile Gln Gln Ala Leu Lys Gln Asp Ser Gly Phe Pro Val Leu 160 165 170 Asp Ser Lys Gly Lys Gln Val Thr Ile Lys Ile Thr Thr Gln Thr Asn 175 180 185 Gly Ala Asn Lys Ser Glu Thr Thr Thr Thr Thr Thr Thr Thr Asn Asp 190 195 200 Ala Gln Thr Leu Leu Gln Glu Ala Ser Lys Met Ile Ser Val Leu Thr 205 210 215 220 Thr Asn Cys Pro Trp Val Asn Thr Ala His Asn Ser Asn Gly Gly Ala 225 230 235 Pro Trp Asn Leu Asn Thr Thr Gly Asn Val Cys Gln Val Phe Ala Thr 240 245 250 Glu Phe Ser Ala Val Thr Ser Met Ile Lys Asn Ala Gln Glu Ile Val 255 260 265 Thr Gln Ala Gln Ser Leu Asn Asn Pro Gln Ser Asn Gln Asn Ala Pro 270 275 280 Lys Asp Phe Asn Pro Tyr Thr Ser Ala Asp Arg Ala Phe Ala Gln Asn 285 290 295 300 Met Leu Asn His Ala Gln Ala Gln Ala Lys Met Leu Glu Leu Ala Asp 305 310 315 Gln Met Lys Lys Asp Leu Asn Thr Ile Pro Lys Gln Phe Ile Thr Asn 320 325 330 Tyr Leu Ala Ala Cys Arg Asn Gly Gly Gly Thr Leu Pro Asp Ala Gly 335 340 345 Val Thr Ser Asn Thr Trp Gly Ala Gly Cys Ala Tyr Val Glu Glu Thr 350 355 360 Ile Thr Ala Leu Asn Asn Ser Leu Ala His Phe Gly Thr Gln Ala Asp 365 370 375 380 Gln Ile Lys Gln Ser Glu Leu Leu Ala Arg Thr Ile Leu Asp Phe Arg 385 390 395 Gly Ser Leu Lys Asp Leu Asn Asn Thr Tyr Asn Ser Ile Thr Thr Thr 400 405 410 Ala Ser Asn Thr Pro Asn Ser Pro Phe Leu Lys Asn Leu Ile Ser Gln 415 420 425 Ser Thr Asn Pro Asn Asn Pro Gly Gly Leu Gln Ala Val Tyr Gln Val 430 435 440 Asn Gln Ser Ala Tyr Ser Gln Leu Leu Ser Ala Thr Gln Glu Leu Gly 445 450 455 460 His Asn Pro Phe Arg Arg Val Gly Leu Ile Ser Ser Gln Thr Asn Asn 465 470 475 Gly Ala Met Asn Gly Ile Gly Val Gln Ile Gly Tyr Lys Gln Phe Phe 480 485 490 Gly Glu Lys Arg Arg Trp Gly Leu Arg Tyr Tyr Gly Phe Phe Asp Tyr 495 500 505 Asn His Ala Tyr Ile Lys Ser Ser Phe Phe Asn Ser Ala Ser Asp Val 510 515 520 Phe Thr Tyr Gly Val Gly Thr Asp Val Leu Tyr Asn Phe Ile Asn Asp 525 530 535 540 Lys Ala Thr Lys Asn Asn Lys Ile Ser Phe Gly Val Phe Gly Gly Ile 545 550 555 Ala Leu Ala Gly Thr Ser Trp Leu Asn Ser Gln Tyr Val Asn Leu Ala 560 565 570 Thr Phe Asn Asn Phe Tyr Ser Ala Lys Met Asn Val Ala Asn Phe Gln 575 580 585 Phe Leu Phe Asn Leu Gly Leu Arg Met Asn Leu Ala Lys Asn Lys Lys 590 595 600 Lys Ala Ser Asp His Val Ala Gln His Gly Val Glu Leu Gly Val Lys 605 610 615 620 Ile Pro Thr Ile Asn Thr Asn Tyr Tyr Ser Leu Leu Gly Thr Gln Leu 625 630 635 Gln Tyr Arg Arg Leu Tyr Ser Val Tyr Leu Asn Tyr Val Phe Ala Tyr 640 645 650 <200> SEQUENCE CHARACTERISTICS: <210> SEQ ID NO 11 <211> LENGTH: 2429 <212> TYPE: DNA <213> ORGANISM: Helicobacter pylori <220> FEATURE: <221> NAME/KEY: CDS <222> LOCATION: (205)...(2277) <220> FEATURE: <221> NAME/KEY: sig_peptide <222> LOCATION: (205)...(259) <400> SEQUENCE: 11 tgaaagaaga ctgattagtc tttcttttag gggcgattca agccttaaaa gccgggtcaa 60 aatccccatt tttcccaatt tttacaaaaa aaaaaaaaac aaaatctcta aaatttagag 120 ctaaaattag ccataaaatt ccatttattg cttataatat gaagtttctt tgtatcaaag 180 aaaaatctat taaaaggaga aaac atg aaa aaa tcc ctc tta ctc tct ctt 231 Met Lys Lys Ser Leu Leu Leu Ser Leu -15 -10 tct ctc atc gct tcc tta tca aga gct gaa gat gac gga ttt tat acg 279 Ser Leu Ile Ala Ser Leu Ser Arg Ala Glu Asp Asp Gly Phe Tyr Thr -5 1 5 agt gtg ggc tat cag atc ggt gaa gcg gtc caa caa gtg aaa aac aca 327 Ser Val Gly Tyr Gln Ile Gly Glu Ala Val Gln Gln Val Lys Asn Thr 10 15 20 gga gca ttg caa aat ctt gca gac aga tac gat aac tta aac aac ctt 375 Gly Ala Leu Gln Asn Leu Ala Asp Arg Tyr Asp Asn Leu Asn Asn Leu 25 30 35 tta aac caa tac aat tat tta aat tcc tta gtc aat tta gcc agc acg 423 Leu Asn Gln Tyr Asn Tyr Leu Asn Ser Leu Val Asn Leu Ala Ser Thr 40 45 50 55 ccg agc gcg atc acc ggt gcg att gat aat tta agc tca agc gcg att 471 Pro Ser Ala Ile Thr Gly Ala Ile Asp Asn Leu Ser Ser Ser Ala Ile 60 65 70 aac ctc act agc gcc acc acc act tcc ccc gcc tat caa gct gtg gct 519 Asn Leu Thr Ser Ala Thr Thr Thr Ser Pro Ala Tyr Gln Ala Val Ala 75 80 85 tta gcg ctc aat gcc gct gtg ggc atg tgg caa gtc ata gcc ctt ttt 567 Leu Ala Leu Asn Ala Ala Val Gly Met Trp Gln Val Ile Ala Leu Phe 90 95 100 att ggc tgt ggc cct ggc cct acc aat aat caa agc tat caa tcg ttt 615 Ile Gly Cys Gly Pro Gly Pro Thr Asn Asn Gln Ser Tyr Gln Ser Phe 105 110 115 ggt aac aca cca gcc ctt aat ggg acc acc acc act tgc aat caa gca 663 Gly Asn Thr Pro Ala Leu Asn Gly Thr Thr Thr Thr Cys Asn Gln Ala 120 125 130 135 tat ggg aca ggc cct aat ggc atc cta tct att gat gaa tac caa aaa 711 Tyr Gly Thr Gly Pro Asn Gly Ile Leu Ser Ile Asp Glu Tyr Gln Lys 140 145 150 ctc aac caa gct tat cag atc atc caa acc gct tta aac caa aat caa 759 Leu Asn Gln Ala Tyr Gln Ile Ile Gln Thr Ala Leu Asn Gln Asn Gln 155 160 165 ggg ggt ggg atg cct gcc ttg aat gac acc acc aaa aca ggg gta gtc 807 Gly Gly Gly Met Pro Ala Leu Asn Asp Thr Thr Lys Thr Gly Val Val 170 175 180 aac ata caa caa acc aat tat agg acc acc aca caa aac aat atc ata 855 Asn Ile Gln Gln Thr Asn Tyr Arg Thr Thr Thr Gln Asn Asn Ile Ile 185 190 195 gag cat tat tat aca gag aat ggg aaa gag atc cca gtc tct tat tca 903 Glu His Tyr Tyr Thr Glu Asn Gly Lys Glu Ile Pro Val Ser Tyr Ser 200 205 210 215 ggc gga tca tca ttc tcg cct aca ata caa ttg aca tac cat aat aac 951 Gly Gly Ser Ser Phe Ser Pro Thr Ile Gln Leu Thr Tyr His Asn Asn 220 225 230 gct gaa aac ctt ttg caa caa gcc gcc act atc atg caa gtc ctt att 999 Ala Glu Asn Leu Leu Gln Gln Ala Ala Thr Ile Met Gln Val Leu Ile 235 240 245 act caa aag ccg cat gtg caa acg agc aat ggc ggt aaa gcg tgg ggg 1047 Thr Gln Lys Pro His Val Gln Thr Ser Asn Gly Gly Lys Ala Trp Gly 250 255 260 ttg agt tct acg cct ggg aat gtg atg gat att ttt ggt cct tct ttt 1095 Leu Ser Ser Thr Pro Gly Asn Val Met Asp Ile Phe Gly Pro Ser Phe 265 270 275 aac gct att aat gag atg att aaa aac gct caa aca gcc cta gca aaa 1143 Asn Ala Ile Asn Glu Met Ile Lys Asn Ala Gln Thr Ala Leu Ala Lys 280 285 290 295 acc caa cag ctt aac gct aat gaa aac gcc caa atc acg caa ccc aac 1191 Thr Gln Gln Leu Asn Ala Asn Glu Asn Ala Gln Ile Thr Gln Pro Asn 300 305 310 aat ttc aac ccc tac acc tct aaa gac aaa ggg ttc gct caa gaa atg 1239 Asn Phe Asn Pro Tyr Thr Ser Lys Asp Lys Gly Phe Ala Gln Glu Met 315 320 325 ctc aat aga gct gaa gct caa gca gag att tta aat tta gct aag caa 1287 Leu Asn Arg Ala Glu Ala Gln Ala Glu Ile Leu Asn Leu Ala Lys Gln 330 335 340 gta gcg aac aat ttc cac agc att caa ggg cct att caa ggg gat tta 1335 Val Ala Asn Asn Phe His Ser Ile Gln Gly Pro Ile Gln Gly Asp Leu 345 350 355 gaa gaa tgt aaa gca gga tcg gct ggc gtg atc act aat aac act tgg 1383 Glu Glu Cys Lys Ala Gly Ser Ala Gly Val Ile Thr Asn Asn Thr Trp 360 365 370 375 ggt tca ggt tgc gcg ttt gtg aaa gaa act tta aac tct tta gag caa 1431 Gly Ser Gly Cys Ala Phe Val Lys Glu Thr Leu Asn Ser Leu Glu Gln 380 385 390 cac acc gct tat tac ggc aac cag gtc aat cag gat agg gct ttg gct 1479 His Thr Ala Tyr Tyr Gly Asn Gln Val Asn Gln Asp Arg Ala Leu Ala 395 400 405 caa acc att ttg aat ttt aaa gaa gcc ctt aac acc ctg aat aaa gac 1527 Gln Thr Ile Leu Asn Phe Lys Glu Ala Leu Asn Thr Leu Asn Lys Asp 410 415 420 tca aaa gcg atc aat agc ggt atc tcc aac ttg cct aac gct aaa tct 1575 Ser Lys Ala Ile Asn Ser Gly Ile Ser Asn Leu Pro Asn Ala Lys Ser 425 430 435 ctt caa aac atg acg cat gcc act caa aac cct aat tcc cca gaa ggt 1623 Leu Gln Asn Met Thr His Ala Thr Gln Asn Pro Asn Ser Pro Glu Gly 440 445 450 455 ctg ctc act tat tct ttg gat tca agc aaa tac aac cag ctc caa acc 1671 Leu Leu Thr Tyr Ser Leu Asp Ser Ser Lys Tyr Asn Gln Leu Gln Thr 460 465 470 atc gcg caa gaa ttg ggc aaa aac cct ttc agg cgc ttt ggc gtg att 1719 Ile Ala Gln Glu Leu Gly Lys Asn Pro Phe Arg Arg Phe Gly Val Ile 475 480 485 gac ttt caa aac aac aac ggc gca atg aac ggg atc ggc gtg caa gtg 1767 Asp Phe Gln Asn Asn Asn Gly Ala Met Asn Gly Ile Gly Val Gln Val 490 495 500 ggt tat aaa caa ttc ttt ggt aaa aaa agg aat tgg ggg tta agg tat 1815 Gly Tyr Lys Gln Phe Phe Gly Lys Lys Arg Asn Trp Gly Leu Arg Tyr 505 510 515 tat ggt ttc ttt gat tat aac cat gct tat atc aaa tct aat ttt ttc 1863 Tyr Gly Phe Phe Asp Tyr Asn His Ala Tyr Ile Lys Ser Asn Phe Phe 520 525 530 535 aac tcc gct tct gat gtg tgg act tat ggg gtg ggt atg gac gct ctc 1911 Asn Ser Ala Ser Asp Val Trp Thr Tyr Gly Val Gly Met Asp Ala Leu 540 545 550 tat aac ttc atc aac gat aaa aac acc aac ttt tta ggc aag aac aac 1959 Tyr Asn Phe Ile Asn Asp Lys Asn Thr Asn Phe Leu Gly Lys Asn Asn 555 560 565 aag ctt tca gta ggg ctt ttt gga ggc ttt gcg tta gcc ggg act tcg 2007 Lys Leu Ser Val Gly Leu Phe Gly Gly Phe Ala Leu Ala Gly Thr Ser 570 575 580 tgg ctt aat tcc caa caa gtg aat ttg acc atg atg aat ggc att tat 2055 Trp Leu Asn Ser Gln Gln Val Asn Leu Thr Met Met Asn Gly Ile Tyr 585 590 595 aac gct aat gtc agc act tct aac ttc caa ttt ttg ttt gat tta ggc 2103 Asn Ala Asn Val Ser Thr Ser Asn Phe Gln Phe Leu Phe Asp Leu Gly 600 605 610 615 ttg aga atg aac ctc gct agg cct aag aaa aaa gac agc gat cat gcc 2151 Leu Arg Met Asn Leu Ala Arg Pro Lys Lys Lys Asp Ser Asp His Ala 620 625 630 gct cag cat ggc att gaa cta ggt ttt aag atc ccc acg atc aac acc 2199 Ala Gln His Gly Ile Glu Leu Gly Phe Lys Ile Pro Thr Ile Asn Thr 635 640 645 aac tat tat tct ttc atg ggc gct aaa cta gaa tac aga agg atg tat 2247 Asn Tyr Tyr Ser Phe Met Gly Ala Lys Leu Glu Tyr Arg Arg Met Tyr 650 655 660 agc ctt ttt ctc aat tat gtg ttt gct tac taaaaattct ttttgaaccc 2297 Ser Leu Phe Leu Asn Tyr Val Phe Ala Tyr 665 670 ctcttttttt gggggagtgt tgcaaaaatg cccccctatt tgcttgtgag ttttggttaa 2357 aattttagtt acccacgctt aaaaagcgcc aagcctttta cacacaactc ctttaatttt 2417 gtttttaaga aa 2429 <200> SEQUENCE CHARACTERISTICS: <210> SEQ ID NO 12 <211> LENGTH: 691 <212> TYPE: PRT <213> ORGANISM: Helicobacter pylori <220> FEATURE: <221> NAME/KEY: SIGNAL <222> LOCATION: (1)...(18) <400> SEQUENCE: 12 Met Lys Lys Ser Leu Leu Leu Ser Leu Ser Leu Ile Ala Ser Leu Ser -15 -10 -5 Arg Ala Glu Asp Asp Gly Phe Tyr Thr Ser Val Gly Tyr Gln Ile Gly 1 5 10 Glu Ala Val Gln Gln Val Lys Asn Thr Gly Ala Leu Gln Asn Leu Ala 15 20 25 30 Asp Arg Tyr Asp Asn Leu Asn Asn Leu Leu Asn Gln Tyr Asn Tyr Leu 35 40 45 Asn Ser Leu Val Asn Leu Ala Ser Thr Pro Ser Ala Ile Thr Gly Ala 50 55 60 Ile Asp Asn Leu Ser Ser Ser Ala Ile Asn Leu Thr Ser Ala Thr Thr 65 70 75 Thr Ser Pro Ala Tyr Gln Ala Val Ala Leu Ala Leu Asn Ala Ala Val 80 85 90 Gly Met Trp Gln Val Ile Ala Leu Phe Ile Gly Cys Gly Pro Gly Pro 95 100 105 110 Thr Asn Asn Gln Ser Tyr Gln Ser Phe Gly Asn Thr Pro Ala Leu Asn 115 120 125 Gly Thr Thr Thr Thr Cys Asn Gln Ala Tyr Gly Thr Gly Pro Asn Gly 130 135 140 Ile Leu Ser Ile Asp Glu Tyr Gln Lys Leu Asn Gln Ala Tyr Gln Ile 145 150 155 Ile Gln Thr Ala Leu Asn Gln Asn Gln Gly Gly Gly Met Pro Ala Leu 160 165 170 Asn Asp Thr Thr Lys Thr Gly Val Val Asn Ile Gln Gln Thr Asn Tyr 175 180 185 190 Arg Thr Thr Thr Gln Asn Asn Ile Ile Glu His Tyr Tyr Thr Glu Asn 195 200 205 Gly Lys Glu Ile Pro Val Ser Tyr Ser Gly Gly Ser Ser Phe Ser Pro 210 215 220 Thr Ile Gln Leu Thr Tyr His Asn Asn Ala Glu Asn Leu Leu Gln Gln 225 230 235 Ala Ala Thr Ile Met Gln Val Leu Ile Thr Gln Lys Pro His Val Gln 240 245 250 Thr Ser Asn Gly Gly Lys Ala Trp Gly Leu Ser Ser Thr Pro Gly Asn 255 260 265 270 Val Met Asp Ile Phe Gly Pro Ser Phe Asn Ala Ile Asn Glu Met Ile 275 280 285 Lys Asn Ala Gln Thr Ala Leu Ala Lys Thr Gln Gln Leu Asn Ala Asn 290 295 300 Glu Asn Ala Gln Ile Thr Gln Pro Asn Asn Phe Asn Pro Tyr Thr Ser 305 310 315 Lys Asp Lys Gly Phe Ala Gln Glu Met Leu Asn Arg Ala Glu Ala Gln 320 325 330 Ala Glu Ile Leu Asn Leu Ala Lys Gln Val Ala Asn Asn Phe His Ser 335 340 345 350 Ile Gln Gly Pro Ile Gln Gly Asp Leu Glu Glu Cys Lys Ala Gly Ser 355 360 365 Ala Gly Val Ile Thr Asn Asn Thr Trp Gly Ser Gly Cys Ala Phe Val 370 375 380 Lys Glu Thr Leu Asn Ser Leu Glu Gln His Thr Ala Tyr Tyr Gly Asn 385 390 395 Gln Val Asn Gln Asp Arg Ala Leu Ala Gln Thr Ile Leu Asn Phe Lys 400 405 410 Glu Ala Leu Asn Thr Leu Asn Lys Asp Ser Lys Ala Ile Asn Ser Gly 415 420 425 430 Ile Ser Asn Leu Pro Asn Ala Lys Ser Leu Gln Asn Met Thr His Ala 435 440 445 Thr Gln Asn Pro Asn Ser Pro Glu Gly Leu Leu Thr Tyr Ser Leu Asp 450 455 460 Ser Ser Lys Tyr Asn Gln Leu Gln Thr Ile Ala Gln Glu Leu Gly Lys 465 470 475 Asn Pro Phe Arg Arg Phe Gly Val Ile Asp Phe Gln Asn Asn Asn Gly 480 485 490 Ala Met Asn Gly Ile Gly Val Gln Val Gly Tyr Lys Gln Phe Phe Gly 495 500 505 510 Lys Lys Arg Asn Trp Gly Leu Arg Tyr Tyr Gly Phe P |