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GLUCAN-BINDING PROTEINS OF THE ORAL STREPTOCOCCI

¹ Center for Immunology and Microbial Disease, Albany Medical College, MC-151, MS-239, 47 New Scotland Avenue, Albany, NY 12208; and ² Department of Oral Surgery and Hospital Dentistry, School of Dentistry, and Department of Microbiology and Immunology, School of Medicine, Indiana University, Indianapolis, IN;

*corresponding author, BanasJ{at}mail.amc.edu

The synthesis of extracellular glucan is an integral component of the sucrose-dependent colonization of tooth surfaces by species of the mutans streptococci. In investigators’ attempts to understand the mechanisms of plaque biofilm development, several glucan-binding proteins (GBPs) have been discovered. Some of these, the glucosyltransferases, catalyze the synthesis of glucan, whereas others, designated only as glucan-binding proteins, have affinities for different forms of glucan and contribute to aspects of the biology of their host organisms. The functions of these latter glucan-binding proteins include dextran-dependent aggregation, dextranase inhibition, plaque cohesion, and perhaps cell wall synthesis. In some instances, their glucan-binding domains share common features, whereas in others the mechanism for glucan binding remains unknown. Recent studies indicate that at least some of the glucan-binding proteins modulate virulence and some can act as protective immunogens within animal models. Overall, the multiplicity of GBPs and their aforementioned properties are testimonies to their importance. Future studies will greatly advance the understanding of the distribution, function, and regulation of the GBPs and place into perspective the facets of their contributions to the biology of the oral streptococci.

Key words. Glucan, glucosyltransferase, GBP, streptococci, plaque