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Glucan-binding proteins (GBPs) of Streptococcus mutans are a family of cell-surface and secreted proteins that serve as receptors for glucan polymers, which are synthesized from sucrose by glucosyltransferases (Banas, 2003). These proteins, including GbpA, GbpB, GbpC, and GbpD, are fundamental to the virulence of S. mutans as they mediate the sucrose-dependent adhesion and aggregation of bacteria on the tooth surface (Lynch et al., 2015). This process leads to the development of a complex biofilm known as dental plaque, where bacterial fermentation of carbohydrates produces organic acids that demineralize tooth enamel, resulting in dental caries (Mattos-Graner et al., 2001). GbpB is particularly notable as it is essential for cell wall integrity and has been identified as a primary target for the development of dental vaccines aimed at inducing protective mucosal IgA responses (Smith, 2002). Therapeutic strategies targeting GBPs focus on disrupting the molecular interactions between the bacteria and the glucan matrix to prevent biofilm maturation and subsequent tooth decay. Experimental approaches include the use of subunit vaccines and small-molecule inhibitors designed to block the glucan-binding domains of these proteins.
Inhibition of bacterial adhesion and biofilm formation by blocking the interaction between the protein and glucan polymers.
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