Yersinia enterocolitica immunodominant 60 kDa antigen, common to a broad range of bacteria, is a heat-shock protein

Yamaguchi, Hiroyuki; Yamamoto, Tomoko; Taguchi, Haruhiko; Ogata, Sachio

doi:10.1099/00221287-136-6-1091

Cited by 26 publications

(34 citation statements)

References 35 publications

(23 reference statements)

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“…MAb was prepared by the method described previously [25]. The 60-kDa antigen derived from H. pylori TK 1029, partially purified by extraction from the separation gel by SDS-PAGE.…”

Section: Preparation Of Monoclonal Antibodiesmentioning

confidence: 99%

Production and characterisation of monoclonal antibodies to heat-shock protein 60 of Helicobacter pylori

Yamaguchi

Osaki²,

Taguchi³

et al. 1997

Journal of Medical Microbiology

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Two monoclonal antibodies (MAbs), designated as H9 (IgG2a) and H20 (IgM), directed against heat-shock protein 60 (HSP60) of Helicobacter pylori strain TK1029 were established. Affinity-purified antigens cross-qeacted in immunoblots with MAb H9 and MAb H20 respectively. These antigens also reacted with the 3C8 MAb previously established in this laboratory, which recognised Yersinia enterocolitica HSP60. By aminoacid sequence analysis, the N-terminal amino-acid sequence of the protein recognised by both H9 and H20 MAbs was confirmed as the amino-acid sequence of H. pylori HSP60 reported previously. Both MAbs reacted with nine strains of H. pylori in enzyme-linked immunosorbent assay (ELISA) and immunoblot analysis. In addition, MAb H9 reacted with extracts of other bacteria including H. mustelae, Pseudomonas aeruginosa, Vibrio cholerae, Serratia marcescens, Proteus mirabilis, Escherichia coli and Shigella sonnei. In contrast, MAb H20 reacted only with strains H. pylori. These results suggest that both the species-specific epitope recognised by MAb H20 and the common epitope recognised by MAb H9 exist on HSP60 of the bacterial cell. Both MAbs also reacted with the 60-kDa protein in the lysate of human gastric carcinoma (MKN45) cells. It was shown by immunohistochemical staining that gastric epithelial cells of four out of six biopsy specimens examined stained positively with MAb H20. These results suggest that there is a common epitope in H. pylori HSP60 and human gastric epithelial cells.

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“…MAb was prepared by the method described previously [25]. The 60-kDa antigen derived from H. pylori TK 1029, partially purified by extraction from the separation gel by SDS-PAGE.…”

Section: Preparation Of Monoclonal Antibodiesmentioning

confidence: 99%

Production and characterisation of monoclonal antibodies to heat-shock protein 60 of Helicobacter pylori

Yamaguchi

Osaki²,

Taguchi³

et al. 1997

Journal of Medical Microbiology

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“…mAbs, termed 5C3 and 3C8, directed to Y. enterocolitica HSP60, were prepared as described previously (20,21). mAb3C8 with the broadest reactivity could recognize Gram-negative and Gram-positive rods.…”

Section: Hiroyukimentioning

confidence: 99%

“…3, Table 1). Immunoblot analysis was performed by the methods previously (21). The results of the immunoblot analysis indicated that 3C8 reacted with all 60-kDa antigens of the cells used, suggesting that leucine, glycine and valine detected in the amino acid sequences might be responsible for the reaction with 3C8.…”

Section: Hiroyukimentioning

confidence: 99%

Analysis of the Epitopes Recognized by Mouse Monoclonal Antibodies Directed to Yersinia enterocolitica Heat‐Shock Protein 60

Yamaguchi

Miura²,

Ohsumi³

et al. 1996

Microbiology and Immunology

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To determine amino acid sequences of the epitopes recognized by monoclonal antibodies (mAbs) 3C8 and 5C3 directed against Yersinia enterocolitica heat-shock protein (HSP60), a dot blot analysis was perfomed using synthesized peptides of Y. enterocolitica HSP60 such as peptides p316-342, p327-359, p340-366, p316-326, p316-321, p319-323, and p321-326 which represent positions of amino acids in Y. enterocolitica HSP60. The dot blot analysis revealed that 5C3 mAb reacted with p316-342, p316-326 and p321-326, and 3C8 mAb p316-342 and p316-326. These results indicate that the epitopes recognized by the mAbs were associated with eleven amino acids, Asp Leu Gly Gln Ala Lys Arg Val Val Ile Asn, of p316-326. The sequence homology between p316-326 of Y. enterocolitica HSP60 and the rest of the HSP60 family suggests that the five amino acids of Lys, Arg, Val, Ile and Asn, which are highly conserved in the HSP60 family, might be related with the epitope recognized by 3C8. In contrast, it was also demonstrated that three amino acids of Leu, Gly and Val, which are not well conserved in the HSP60 family, might be related to the epitope recognized by 5C3.

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“…To detect HSP antigens, monoclonal antibodies against Helicobacter pylori HSP 60 (Wako Pure Chemical Industries, Ltd., Osaka, Japan) were used 25) . Grown cells of isolated mycoplasma strains including M. salivarium ATCC 23060 and M. orale ATCC 23714 were also examined in this study.…”

Section: Production Of Hspmentioning

confidence: 99%

Heat shock protein of Mycoplasma salivarium and Mycoplasma orale strains isolated from HIV-seropositive patients.

Chattin-Kacouris

Ishihara

Miura

et al. 2002

Bull. Tokyo Dent. Coll.

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It has been suggested that infection by some mycoplasma species can act as possible cofactors in the acceleration of immunodeficiency in HIV-infected patients. The present study was designed to examine infections by oral mycoplasma species in HIV-seropositive (HIV(‫))ם‬ patients. Mycoplasma salivarium and Mycoplasma orale were isolated from 59.5% and 16.7% of 42 HIV(‫)ם‬ patients, respectively. Non-M. salivarium and non-M. orale species were isolated from 40.5% of saliva samples from the HIV(‫)ם‬ group and 20.8% of those from 24 HIV-seronegative (HIV(‫))מ‬ subjects, respectively. Although the production of superantigen by human peripheral lymphocytes in the isolated mycoplasma species from HIV(‫)ם‬ and HIV ‫)מ(‬ subjects was evaluated, none of the examined mycoplasma strains, including ATCC strains of M.salivarium, M. orale, Mycoplasma buccae and Mycoplasma penetrans, were found to produce superantigen. Production of heat shock proteins (HSPs) by isolated mycoplasma strains was examined by immunoblotting using monoclonal antibodies against Helicobacter pylori HSP60. It was found that all the strains of M. salivarium, M.orale, and unidentified mycoplasma species isolated from HIV(‫)ם‬ and HIV(‫)מ‬ groups produced heat shock proteins. HSP production by oral mycoplasma may play a role in the immunomodulation of HIV(‫)ם‬ patients.

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Yersinia enterocolitica immunodominant 60 kDa antigen, common to a broad range of bacteria, is a heat-shock protein

Abstract: Monoclonal antibodies (mAbs) against the

Cited by 26 publications

References 35 publications

Production and characterisation of monoclonal antibodies to heat-shock protein 60 of Helicobacter pylori

Production and characterisation of monoclonal antibodies to heat-shock protein 60 of Helicobacter pylori

Analysis of the Epitopes Recognized by Mouse Monoclonal Antibodies Directed to Yersinia enterocolitica Heat‐Shock Protein 60

Heat shock protein of Mycoplasma salivarium and Mycoplasma orale strains isolated from HIV-seropositive patients.

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