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Archives of oral biology · Jan 2010
Molecular characterization of Streptococcus mutans strains containing the cnm gene encoding a collagen-binding adhesin.
- K Nakano, R Nomura, N Taniguchi, J Lapirattanakul, A Kojima, S Naka, P Senawongse, R Srisatjaluk, L Grönroos, S Alaluusua, M Matsumoto, and T Ooshima.
- Department of Pediatric Dentistry, Osaka University Graduate School of Dentistry, Suita, Osaka, Japan.
- Arch. Oral Biol. 2010 Jan 1; 55 (1): 34-9.
ObjectiveStreptococcus mutans, known to be a major pathogen of dental caries, is also considered to cause infective endocarditis. Its 120-kDa Cnm protein binds to type I collagen, which may be a potential virulence factor. In this study, we characterized S. mutans clinical strains focusing on the cnm gene encoding Cnm.DesignA total of 528 S. mutans strains isolated from Japanese, Finnish, and Thai subjects were investigated. Using molecular techniques, the distribution frequency of cnm-positive strains and location of the inserted cnm were analyzed. Furthermore, isogenic mutant strains were constructed by inactivation of the cnm gene, then their biological properties of collagen-binding and glucan-binding were evaluated. Southern hybridization of the genes encoding glucan-binding proteins was also performed.ResultsThe distribution frequency of cnm-positive strains from Thai subjects was 12%, similar to that previously reported for Japanese and Finnish subjects. Furthermore, the location of insertion of cnm was the same in all cnm-positive clinical isolates. As for the cnm-inactivated mutant strains constructed from 28 clinical isolates, their collagen-binding activity was negligible. In addition, glucan-binding activity in the cnm-positive clinical isolates was significantly reduced and corresponded to a lack of gbpA encoding glucan-binding protein A.ConclusionsOur results indicate that strains with cnm genes, the most crucial factor for the collagen-binding property of S. mutans, are detectable at similar frequencies over several different geographic locations. In addition, the common properties of these strains are a high level of collagen-binding activity and tendency for a low level of glucan-binding activity.Copyright 2009 Elsevier Ltd. All rights reserved.
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