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, Shuhei Naka, P. Senawongse, R. Srisatjaluk, L. Grönroos, S. Alaluusua, Michiyo Nakano, T. Ooshima

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

Objective: Streptococcus 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. Design: A 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. Results: The 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. Conclusions: Our 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.

Original languageEnglish
Pages (from-to)34-39
Number of pages6
JournalArchives of Oral Biology
Volume55
Issue number1
DOIs
Publication statusPublished - Jan 2010
Externally publishedYes

Fingerprint

Streptococcus mutans
Glucans
Collagen
Genes
Geographic Locations
Staphylococcal Protein A
Dental Caries
Gene Silencing
Virulence Factors
Collagen Type I
Endocarditis
Proteins
glucan-binding proteins

Keywords

  • Clinical isolates
  • Collagen-binding adhesin
  • Glucan-binding activity
  • Streptococcus mutans

ASJC Scopus subject areas

  • Otorhinolaryngology
  • Cell Biology
  • Dentistry(all)

Cite this

Molecular characterization of Streptococcus mutans strains containing the cnm gene encoding a collagen-binding adhesin. / Nakano, K.; Nomura, R.; Taniguchi, N.; Lapirattanakul, J.; Kojima, A.; Naka, Shuhei; Senawongse, P.; Srisatjaluk, R.; Grönroos, L.; Alaluusua, S.; Nakano, Michiyo; Ooshima, T.

In: Archives of Oral Biology, Vol. 55, No. 1, 01.2010, p. 34-39.

Research output: Contribution to journalArticle

Nakano, K, Nomura, R, Taniguchi, N, Lapirattanakul, J, Kojima, A, Naka, S, Senawongse, P, Srisatjaluk, R, Grönroos, L, Alaluusua, S, Nakano, M & Ooshima, T 2010, 'Molecular characterization of Streptococcus mutans strains containing the cnm gene encoding a collagen-binding adhesin', Archives of Oral Biology, vol. 55, no. 1, pp. 34-39. https://doi.org/10.1016/j.archoralbio.2009.11.008
Nakano, K. ; Nomura, R. ; Taniguchi, N. ; Lapirattanakul, J. ; Kojima, A. ; Naka, Shuhei ; Senawongse, P. ; Srisatjaluk, R. ; Grönroos, L. ; Alaluusua, S. ; Nakano, Michiyo ; Ooshima, T. / Molecular characterization of Streptococcus mutans strains containing the cnm gene encoding a collagen-binding adhesin. In: Archives of Oral Biology. 2010 ; Vol. 55, No. 1. pp. 34-39.
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abstract = "Objective: Streptococcus 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. Design: A 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. Results: The 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. Conclusions: Our 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.",
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AU - Nakano, K.

AU - Nomura, R.

AU - Taniguchi, N.

AU - Lapirattanakul, J.

AU - Kojima, A.

AU - Naka, Shuhei

AU - Senawongse, P.

AU - Srisatjaluk, R.

AU - Grönroos, L.

AU - Alaluusua, S.

AU - Nakano, Michiyo

AU - Ooshima, T.

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N2 - Objective: Streptococcus 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. Design: A 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. Results: The 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. Conclusions: Our 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.

AB - Objective: Streptococcus 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. Design: A 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. Results: The 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. Conclusions: Our 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.

KW - Clinical isolates

KW - Collagen-binding adhesin

KW - Glucan-binding activity

KW - Streptococcus mutans

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