Characterization of an immunoreactive species-specific 19-kilodalton outer membrane protein from Helicobacter pylori by using a monoclonal antibody

Drouet, Emmanuel; Denoyel, G. A.; Boude, M; Wallano, Eyob; Andujar, Mauricio B.; Montclos, Henri P. De

doi:10.1128/jcm.29.8.1620-1624.1991

Cited by 25 publications

(6 citation statements)

References 28 publications

(22 reference statements)

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“…Several other MAbs which react with H. pylori-specific antigens have been described (3,(5)(6)(7)(8)17). Some of these MAbs have been used for diagnostic purposes and have been employed in immunofluorescence tests (7,8,17).…”

Section: Vol 33 1995mentioning

confidence: 99%

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Identification of Helicobacter pylori by immunological dot blot method based on reaction of a species-specific monoclonal antibody with a surface-exposed protein

1995

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Monoclonal antibodies (MAbs) against membrane preparations of Helicobacter pylori were produced. One MAb was found to be specific for H. pylori, because it did not react with a number of other bacterial species, including Helicobacter felis and Campylobacter jejuni. This MAb reacted with a 30-kDa protein found in outer membrane preparations of H. pylori. The protein was also detected on the cell surface on intact bacteria when analyzed by immunoelectron microscopy. To facilitate the identification of H. pylori isolates after culturing of biopsies, an immunodot blot assay based on the reaction of this MAb was developed. This assay was found to be highly specific for H. pylori. Sixty-six clinical isolates typed as H. pylori by conventional biochemical tests were found to be positive, whereas no other bacterial species tested gave a positive result. By this method, reliable and rapid identification of H. pylori could be accomplished.

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Section: Vol 33 1995mentioning

confidence: 99%

“…Some of these MAbs have been used for diagnostic purposes and have been employed in immunofluorescence tests (7,8,17). Protein antigens with molecular weights of 19,000 and 25,000 recognized by two of these MAbs have been identified (6,7). The function of the 30-kDa protein recognized by MAb HP30-1:1 has yet to be determined.…”

Section: Vol 33 1995mentioning

confidence: 99%

Identification of Helicobacter pylori by immunological dot blot method based on reaction of a species-specific monoclonal antibody with a surface-exposed protein

1995

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“…Peripheral blood samples were obtained from healthy blood donors (laboratory staff) who had no antibodies against H. pylori as determined by immunoblot analysis and enzyme immunoassays with bacterial sonicate [21,22]. The infections with H. pylori in patients were diagnosed by a rapid urease test from biopsy specimens of antral mucosa and by the determination of the presence of antibodies against H. pylori in the patients' sera by the methods mentioned above.…”

Section: Blood Donorsmentioning

confidence: 99%

Immunological activity of lipopolysaccharide of Helicobacter pylori on human peripheral mononuclear blood cells in comparison to lipopolysaccharides of other intestinal bacteria

Birkholz¹

1993

FEMS Immunology and Medical Microbiology

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Lipopolysaccharide of Helicobacter pylori was tested for its mitogenicity and for its ability to stimulate cytokine release in human peripheral blood mononuclear cells (PBMC) of healthy and H. pylori-infected blood donors. Mitogenicity in PBMC induced by H. pylori LPS was similar to that induced by Campylobacter jejuni lipopolysaccharide, but lower than that induced by Escherichia coli lipopolysaccharide in the H. pylori negative blood donor group. Furthermore, H. pylori LPS was able to induce tumour necrosis factor (TNF) interleukin 1 (IL-1) and interleukin 6 (IL-6) secretion of PBMC. Compared with the ability of C. jejuni and E. coli lipopolysaccharides to stimulate cytokine release, H. pylori lipopolysaccharide induced a significantly lower TNF and IL-1 secretion of PBMC than the other tested bacterial lipopolysaccharides. Similar amounts of IL-6 release were obtained by stimulation of PBMC with H. pylori and C. jejuni lipopolysaccharides, whereas a higher IL-6 release was measured by stimulation with E. coli lipopolysaccharide. The results of this study suggest that H. pylori lipopolysaccharide has a lower immunological activity than lipopolysaccharides of other intestinal bacteria. This is probably due to its unusual acylation and phosphorylation pattern of lipid A.

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“…Little is known about the outer membrane structure of H. pylon or the identities of its surface-exposed proteins. Only a few proteins have been identified as being unambiguously localized within the outer membrane (10,24). This is partly because of high-copy-number assemblies of proteins such as urease and GroEL which have copurified with cell envelopes in the past, complicating analysis of the membrane components (36).…”

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confidence: 99%

Identification of surface-exposed outer membrane antigens of Helicobacter pylori

Doig

Trust

1994

Infect Immun

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Despite the potential significance of surface-localized antigens in the colonization by and disease processes ofHelicobacterpylori, few such components have been unequivocally identified and/or characterized. To further investigate the surface of this bacterium, monoclonal antibodies (MAbs) to a sarcosine-insoluble outer membrane fraction prepared from H. pylori NCTC 11637 were raised. MAbs were selected on the basis of their surface reactivity to whole cells by enzyme-linked immunosorbent assay, immunofluorescence, and immunoelectron microscopy. By use of this selection protocol, 14 surface-reactive MAbs were chosen. These MAbs were used to identify six protein antigens (molecular masses, 80, 60, 51, 50, 48, and 31 kDa), all of which were localized within or associated with the outer membrane. Two of the MAbs recognized the core region of lipopolysaccharide (LPS). Only these two anti-LPS MAbs also recognized the flagellar sheath, indicating a structural difference between the sheath and outer membrane. Three of the protein antigens (80, 60, and 51 kDa) were strain specific, while the other three antigens were present in other strains of H. pylori. Both the 51and 48-kDa antigens were heat modifiable and likely are porins. A conserved 31-kDa protein may represent another species of porin. A method involving sucrose density ultracentrifugation and Triton extraction that allows the preparation of H. pylori outer membranes with minimal inner membrane contamination is described. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed that the protein content of the H. pylori outer membrane is similar structurally to those of other species of Helicobacter but markedly different from those of taxonomically related Campylobacter spp. and Escherichia coli. H. pyloni also appeared to lack peptido2lvcan-associatedLproteins.

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Characterization of an immunoreactive species-specific 19-kilodalton outer membrane protein from Helicobacter pylori by using a monoclonal antibody

Cited by 25 publications

References 28 publications

Identification of Helicobacter pylori by immunological dot blot method based on reaction of a species-specific monoclonal antibody with a surface-exposed protein

Identification of Helicobacter pylori by immunological dot blot method based on reaction of a species-specific monoclonal antibody with a surface-exposed protein

Immunological activity of lipopolysaccharide of Helicobacter pylori on human peripheral mononuclear blood cells in comparison to lipopolysaccharides of other intestinal bacteria

Identification of surface-exposed outer membrane antigens of Helicobacter pylori

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