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Infect Immun. 1993 April; 61(4): 1547-1552

Identification of a salivary agglutinin-binding domain within cell surface adhesin P1 of Streptococcus mutans.

P J Crowley, L J Brady, D A Piacentini and A S Bleiweis

Department of Oral Biology, University of Florida, Gainesville 32610.

ABSTRACT

DNA encoding the alanine-rich region (A-region) of the cell surface adhesin, P1, from Streptococcus mutans was subcloned and expressed as a fusion protein with the maltose-binding protein (MBP) of Escherichia coli. The A-region fusion protein was shown to competitively inhibit both adherence of S. mutans to salivary agglutinin-coated hydroxyapatite and fluid-phase agglutinin-mediated aggregation of this organism. MBP alone or an MBP-paramyosin fusion protein was not inhibitory. Proteolytic cleavage of the fusion protein into its component moieties, MBP and A-region, resulted in breakdown of the A-region into three main fragments. Western immunoblot analysis of calcium-dependent agglutinin binding to this preparation revealed binding specificity for a 28-kDa fragment. Thus, the A-region of P1 is an important domain which interacts directly with salivary agglutinin, and this interaction interferes with both the aggregation and the adherence mechanisms in vitro.

Infect Immun. 1993 April; 61(4): 1547-1552




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