Immunochemical characterisation and epitope mapping of a novel fimbrial protein (Pg-II fimbria) of Porphyromonas gingivalis |
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Authors: | Tomohiko Ogawa Kenji Yasuda Keiko Yamada Hideharu Mori Keiko Ochiai Mamoru Hasegawa |
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Institution: | Department of Oral Microbiology, Osaka University Faculty of Dentistry, 1-8 Yamadaoka, Suita, Osaka 565, Japan;Nagoya Research Laboratories, Meito Sangyo, Nagoya, Aichi, Japan;Research Laboratories, Kyowa Medex, Sunto-gun, Shizuoka, Japan;Tokyo Research Laboratories, Kyowa Hakko Kogyo, Machida, Tokyo, Japan |
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Abstract: | Abstract Mouse monoclonal antibody (mAb) Pgf-II specific for a 72-kDa major cell-surface protein (72K-CSP) derived from Porphyromonas gingivalis OMZ 409 was prepared. Immunoblotting analysis revealed that mAb Pgf-II reacted with 72K-CSP but not with 41-kDa fimbrial subunit protein (41K-fimbrilin) derived from P. gingivalis 381. Electron microscopic observation revealed that P. gingivalis OMZ 409 possessed peritrichous, thin fimbriae on their surface. Immunogold electron microscopy also demonstrated that mAb Pgf-II bound to the 72K-CSP examined with the gold particles arranged along the fibril array originating from the cell surface of the bacteria. These findings suggested that P. gingivalis 72K-CSP was identifiable as another fimbriae (termed Pg-II fimbriae) different from the fimbriae (termed Pg-I fimbriae) composed of a 41K-fimbrilin. Using multipin peptide synthesis technology, 102 sequential overlapping peptides covering the entire 514 amino-acid stretch of Pg-II fimbriae were synthesised. Seven immunodominant regions within Pg-II fimbrial protein molecule, which definitely reacted with the serum of patients with periodontal diseases, were detected. |
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Keywords: | Fimbriae Epitope mapping Porphyromonas gingivalis Periodontal disease |
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