Identification and characterization of a collagen-binding protein, Cbm, in Streptococcus mutans
Streptococcus mutans, a major pathogen of dental caries, is occasionally isolated from the blood of patients with infective endocarditis. Bacterial attachment of exposed collagen tissue in the impaired endothelium is an important step in the onset of infective endocarditis. In our previous studies,...
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th-mahidol.140792018-06-11T12:07:26Z Identification and characterization of a collagen-binding protein, Cbm, in Streptococcus mutans R. Nomura K. Nakano S. Naka H. Nemoto K. Masuda J. Lapirattanakul S. Alaluusua M. Matsumoto S. Kawabata T. Ooshima Osaka University Mahidol University Helsinki University Hospital Helsingin Yliopisto Dentistry Immunology and Microbiology Medicine Streptococcus mutans, a major pathogen of dental caries, is occasionally isolated from the blood of patients with infective endocarditis. Bacterial attachment of exposed collagen tissue in the impaired endothelium is an important step in the onset of infective endocarditis. In our previous studies, some S. mutans strains were shown to possess collagen-binding activities and most of them had an approximately 120-kDa cell-surface collagen-binding protein called Cnm. However, several strains without Cnm proteins show collagen-binding properties. In the present study, another collagen-binding protein, Cbm, was characterized and its coding gene cbm was sequenced in these strains. The amino acid alignment in the putative collagen-binding domain of Cbm was shown to have approximately 80% identity and 90% similarity to the comparable region of Cnm. Cbm-deficient isogenic mutant strains constructed by insertional inactivation of the cbm gene, lacked collagen-binding properties, which were recovered in the complemented mutant. Analyses of a large number of clinical isolates from Japan, Thailand and Finland revealed that cbm-positive strains were present in all of these countries and that cnm-positive and cbm-positive strains were detected in the oral cavity of approximately 10 and 2% of systemically healthy subjects, respectively. In addition, cnm-positive strains were predominantly identified in the serotype f group, whereas cbm-positive strains were frequently detected in serotype k. These results suggest that Cbm as well as Cnm are major cell surface proteins of S. mutans associated with binding to type I collagen and predominantly identified in serotype k strains. © 2012 John Wiley & Sons A/S. 2018-06-11T04:46:14Z 2018-06-11T04:46:14Z 2012-08-01 Article Molecular Oral Microbiology. Vol.27, No.4 (2012), 308-323 10.1111/j.2041-1014.2012.00649.x 20411014 20411006 2-s2.0-84863599161 https://repository.li.mahidol.ac.th/handle/123456789/14079 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84863599161&origin=inward |
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Dentistry Immunology and Microbiology Medicine R. Nomura K. Nakano S. Naka H. Nemoto K. Masuda J. Lapirattanakul S. Alaluusua M. Matsumoto S. Kawabata T. Ooshima Identification and characterization of a collagen-binding protein, Cbm, in Streptococcus mutans |
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Streptococcus mutans, a major pathogen of dental caries, is occasionally isolated from the blood of patients with infective endocarditis. Bacterial attachment of exposed collagen tissue in the impaired endothelium is an important step in the onset of infective endocarditis. In our previous studies, some S. mutans strains were shown to possess collagen-binding activities and most of them had an approximately 120-kDa cell-surface collagen-binding protein called Cnm. However, several strains without Cnm proteins show collagen-binding properties. In the present study, another collagen-binding protein, Cbm, was characterized and its coding gene cbm was sequenced in these strains. The amino acid alignment in the putative collagen-binding domain of Cbm was shown to have approximately 80% identity and 90% similarity to the comparable region of Cnm. Cbm-deficient isogenic mutant strains constructed by insertional inactivation of the cbm gene, lacked collagen-binding properties, which were recovered in the complemented mutant. Analyses of a large number of clinical isolates from Japan, Thailand and Finland revealed that cbm-positive strains were present in all of these countries and that cnm-positive and cbm-positive strains were detected in the oral cavity of approximately 10 and 2% of systemically healthy subjects, respectively. In addition, cnm-positive strains were predominantly identified in the serotype f group, whereas cbm-positive strains were frequently detected in serotype k. These results suggest that Cbm as well as Cnm are major cell surface proteins of S. mutans associated with binding to type I collagen and predominantly identified in serotype k strains. © 2012 John Wiley & Sons A/S. |
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Osaka University |
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Osaka University R. Nomura K. Nakano S. Naka H. Nemoto K. Masuda J. Lapirattanakul S. Alaluusua M. Matsumoto S. Kawabata T. Ooshima |
format |
Article |
author |
R. Nomura K. Nakano S. Naka H. Nemoto K. Masuda J. Lapirattanakul S. Alaluusua M. Matsumoto S. Kawabata T. Ooshima |
author_sort |
R. Nomura |
title |
Identification and characterization of a collagen-binding protein, Cbm, in Streptococcus mutans |
title_short |
Identification and characterization of a collagen-binding protein, Cbm, in Streptococcus mutans |
title_full |
Identification and characterization of a collagen-binding protein, Cbm, in Streptococcus mutans |
title_fullStr |
Identification and characterization of a collagen-binding protein, Cbm, in Streptococcus mutans |
title_full_unstemmed |
Identification and characterization of a collagen-binding protein, Cbm, in Streptococcus mutans |
title_sort |
identification and characterization of a collagen-binding protein, cbm, in streptococcus mutans |
publishDate |
2018 |
url |
https://repository.li.mahidol.ac.th/handle/123456789/14079 |
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1763495526912753664 |