Identification of Immunodominant Antigens from
            <i>Helicobacter pylori</i>
            and Evaluation of Their Reactivities with Sera from Patients with Different Gastroduodenal Pathologies

Kimmel, Brigitte; Bosserhoff, Anja‐Katrin; Frank, Rainer; Gross, Roy; Goebel, Werner; Beier, Dagmar

doi:10.1128/iai.68.2.915-920.2000

Cited by 115 publications

(118 citation statements)

References 38 publications

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“…12, which is published as supporting information on the PNAS web site). These results are consistent with other reports that have failed to identify BabA or BabB as immunodominant antigens in humans (25,26). Taken together, the findings that rhesus-derived strains of H. pylori and most J166 output strains have two copies of babB suggest to us that BabB may function as an adhesin and that overexpression of BabB is advantageous.…”

Section: Discussionsupporting

confidence: 82%

Modification of Helicobacter pylori outer membrane protein expression during experimental infection of rhesus macaques

Solnick

Hansen

Salama

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

213

215

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Clinical isolates of Helicobacter pylori show marked diversity, which may derive from genomic changes that occur during the often lifelong association of the bacterium with its human host. We used the rhesus macaque model, together with DNA microarrays, to examine genomic changes in H. pylori that occur early during experimental infection. Microarray analysis showed that H. pylori recovered from challenged macaques had deleted babA, a member of a large family of paralogous outer membrane proteins (OMPs) that mediates attachment of H. pylori to the Lewis B blood group antigen on gastric epithelium. In some cases the babA gene was replaced by babB, an uncharacterized OMP that is closely related to babA. In other cases the babA gene was present but was not expressed because of alteration in dinucleotide CT repeats in the 5 coding region. In either case, strains lacking babA did not adhere to Lewis B, which is expressed on macaque gastric epithelium. Absence of babA and duplication of babB was also seen in H. pylori isolates derived from human clinical samples, suggesting that this gene conversion event is not unique to experimentally infected rhesus monkeys. These results demonstrate in real time with a relevant animal model that H. pylori regulates OMP expression in vivo by using both antigenic variation and phase variation. We suggest that changes in babA and babB after experimental infection of macaques represent a dynamic response in the H. pylori outer membrane that facilitates adherence to the gastric epithelium and promotes chronic infection.

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Section: Discussionsupporting

confidence: 82%

Modification of Helicobacter pylori outer membrane protein expression during experimental infection of rhesus macaques

Solnick

Hansen

Salama

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

213

215

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“…Indeed, 11 of 18 identified proteins are among the previously described 32 antigens that are recognized by a majority of sera from infected humans (41,50,51). This indicates that our identification procedure strongly enriched for highly immunogenic antigens (11 antigens of 18 surface proteins versus 32 antigens of 1560 total proteins).…”

Section: Identification Of Surface Proteins Of H Pylori 27900mentioning

confidence: 81%

Identification of Surface Proteins of Helicobacter pylori by Selective Biotinylation, Affinity Purification, and Two-dimensional Gel Electrophoresis

Sabarth

Lamer

Zimny‐Arndt

et al. 2002

Journal of Biological Chemistry

144

124

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Helicobacter pylori is a widespread human pathogen that can cause gastric ulcers and cancer. To identify surface proteins that may play a role in pathogen-host interactions and represent potential targets for the control of this infection, we selectively biotinylated intact H. pylori with the hydrophilic reagent sulfosuccinimidyl-6-(biotinamido)-hexanoate and purified the labeled proteins by membrane isolation, solubilization, and affinity chromatography. After separation of 82 biotinylated proteins on two-dimensional gels, 18 were identified with comparison to proteome data and peptide mass fingerprinting. Among the identified proteins, 9 have previously been shown to be surface-exposed, 7 are associated with virulence, and 11 are highly immunogenic in infected patients. In conclusion, this generally applicable combined proteome approach facilitates the rapid identification of promising targets for the control of H. pylori and might be applicable to numerous other human pathogens although larger biotinylation reagents might be required in some cases to prevent permeation of porin channels in the outer membrane.

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“…Most of them have been predicted or documented previously to be extracytoplasmic, and some described as immunodominant. In contrast, most immunoreactive proteins identified in the proteome of H. pylori G27 represented housekeeping gene products [23].…”

Section: Introductionmentioning

confidence: 99%

“…Jungblut et al and Haas et al screened the proteome of H. pylori 26695 using single sera and determined differences in the immune response of patients with various clinical manifestations [16,19,23,34]. Furthermore, comparative analysis conducted by Mini et al revealed a significant heterogeneity between selected antigens that is dependent on both the bacterial strain and the sera used for analysis [38].…”

Section: Introductionmentioning

confidence: 99%

Tip-α (hp0596 Gene Product) Is a Highly Immunogenic Helicobacter pylori Protein Involved in Colonization of Mouse Gastric Mucosa

et al. 2008

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A product of the Helicobacter pylori hp0596 gene (Tip-a) is a highly immunogenic homodimeric protein, unique for this bacterium. Cell fractionation experiments indicate that Tip-a is anchored to the inner membrane. In contrast, the three-dimensional model of the protein suggests that Tip-a is soluble or, at least, largely exposed to the solvent. hp0596 gene knockout resulted in a significant decrease in the level of H. pylori colonization as measured by real-time PCR assay. In addition, the Tip-a recombinant protein was determined to stimulate macrophage to produce IL-1a and TNF-a. Both results imply that Tip-a is rather loosely connected to the inner membrane and potentially released during infection.

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Identification of Immunodominant Antigens from Helicobacter pylori and Evaluation of Their Reactivities with Sera from Patients with Different Gastroduodenal Pathologies

Cited by 115 publications

References 38 publications

Modification of Helicobacter pylori outer membrane protein expression during experimental infection of rhesus macaques

Modification of Helicobacter pylori outer membrane protein expression during experimental infection of rhesus macaques

Identification of Surface Proteins of Helicobacter pylori by Selective Biotinylation, Affinity Purification, and Two-dimensional Gel Electrophoresis

Tip-α (hp0596 Gene Product) Is a Highly Immunogenic Helicobacter pylori Protein Involved in Colonization of Mouse Gastric Mucosa

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