Molecular interactions of alanine-rich and proline-rich regions of cell surface protein antigen c in Streptococcus mutans

Michiyo Nakano, M. Tsuji, A. Amano, T. Ooshima

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Introduction: Streptococcus mutans has been implicated as a primary causative agent of dental caries in humans, and its cell surface protein antigen c (PAc) is known to be associated with sucrose-independent adhesion to tooth surfaces. PAc is composed of several domains, including an N-terminal signal sequence, an alanine-rich repeat region (A-region), a proline-rich repeat region (P-region), and an anchor region. Methods: To investigate the functions of each domain, an A-region-deficient mutant strain of S. mutans was constructed, and recombinant PAc and A- and P-region proteins were also constructed. The interactions of each domain with the recombinant proteins were analyzed using surface plasmon resonance spectroscopy with a biomolecular interaction analyzing system. Results: The A-region-deficient mutant strain showed the lowest levels of adherence to saliva-coated hydroxyapatite. Furthermore, findings in an immunoblot assay indicated that the A-region protein reacted strongly with proline-rich proteins in saliva, while the recombinant P-region protein interacted more quickly with PAc than the recombinant A-region protein. Conclusion: These results suggest that the A-region has a strong relationship with adhesion to tooth surfaces, while the P-region has a high affinity for PAc.

Original languageEnglish
Pages (from-to)265-270
Number of pages6
JournalOral Microbiology and Immunology
Volume23
Issue number4
DOIs
Publication statusPublished - Aug 2008
Externally publishedYes

Fingerprint

Streptococcus mutans
Surface Antigens
Proline
Alanine
Membrane Proteins
Proteins
Antigens
Saliva
Recombinant Proteins
Tooth
Surface Plasmon Resonance
Dental Caries
Durapatite
Protein Sorting Signals
Sucrose
Spectrum Analysis

Keywords

  • Functional domain
  • Protein antigen c
  • Streptococcus mutans

ASJC Scopus subject areas

  • Immunology
  • Microbiology (medical)
  • Dentistry(all)

Cite this

Molecular interactions of alanine-rich and proline-rich regions of cell surface protein antigen c in Streptococcus mutans. / Nakano, Michiyo; Tsuji, M.; Amano, A.; Ooshima, T.

In: Oral Microbiology and Immunology, Vol. 23, No. 4, 08.2008, p. 265-270.

Research output: Contribution to journalArticle

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AB - Introduction: Streptococcus mutans has been implicated as a primary causative agent of dental caries in humans, and its cell surface protein antigen c (PAc) is known to be associated with sucrose-independent adhesion to tooth surfaces. PAc is composed of several domains, including an N-terminal signal sequence, an alanine-rich repeat region (A-region), a proline-rich repeat region (P-region), and an anchor region. Methods: To investigate the functions of each domain, an A-region-deficient mutant strain of S. mutans was constructed, and recombinant PAc and A- and P-region proteins were also constructed. The interactions of each domain with the recombinant proteins were analyzed using surface plasmon resonance spectroscopy with a biomolecular interaction analyzing system. Results: The A-region-deficient mutant strain showed the lowest levels of adherence to saliva-coated hydroxyapatite. Furthermore, findings in an immunoblot assay indicated that the A-region protein reacted strongly with proline-rich proteins in saliva, while the recombinant P-region protein interacted more quickly with PAc than the recombinant A-region protein. Conclusion: These results suggest that the A-region has a strong relationship with adhesion to tooth surfaces, while the P-region has a high affinity for PAc.

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