Inactivation of srtA gene of Streptococcus mutans inhibits dextran-dependent aggregation by glucan-binding protein C

Authors: Igarashi T.¹; Asaga E.¹; Sato Y.²; Goto N.¹

Source: Oral Microbiology and Immunology, Volume 19, Number 1, February 2004 , pp. 57-60(4)

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Abstract:

Igarashi T, Asaga E, Sato Y, Goto N. Inactivation of srtA gene of Streptococcus mutans inhibits dextran-dependent aggregation by glucan-binding protein C.

Oral Microbiol Immunol 2004: 19: 57–60.© Blackwell Munksgaard, 2004.

A sortase-deficient mutant of Streptococcus mutans was prepared by insertional inactivation of a sortase gene (srtA). The srtA mutant was defective in cell wall-anchoring of two surface proteins 200 and 75 kDa in size. A previous study has shown that the 200 kDa protein is a surface protein antigen PAc and that the sortase catalyzes cell wall-anchoring of PAc in S. mutans. In this study another surface protein 75 kDa in size was examined by immunologic and physiologic methods. Western blot analysis with a specific antiserum showed that the 75 kDa protein was a surface protein, glucan-binding protein C. The protein was overexpressed under a stress condition including a sublethal concentration of tetracycline. The srtA mutant cells also lost the ability of dextran-dependent aggregation. These results suggest that the S. mutans sortase mediates cell wall-anchoring of the glucan-binding protein C and dextran-dependent aggregation of this organism.

Keywords: cell wall anchoring; dextran-dependent aggregation; GbpC; LPXTG motif; sortase; Streptococcus mutans

Document Type: Short communication

DOI: http://dx.doi.org/10.1046/j.0902-0055.2003.00104.x

Affiliations: 1: Department of Oral Microbiology, Showa University School of Dentistry, Tokyo, 2: Department of Biochemistry, Tokyo Dental College, Chiba City, Japan

Publication date: 2004-02-01