Streptococcus mutans glucosyltransferase and surface adhesin (GTF/Adhesin)

Streptococcus mutans glucosyltransferases (GTFs) and surface adhesins are primary virulence factors responsible for the initiation and progression of dental caries [1]. GTFs, specifically GtfB, GtfC, and GtfD, are enzymes that catalyze the conversion of dietary sucrose into water-insoluble and soluble glucans, which constitute the essential structural scaffold of the dental plaque matrix [2]. Surface adhesins, most notably the Antigen I/II family (also known as SpaP, PAc, or P1), facilitate the initial attachment of S. mutans to the salivary pellicle coating the tooth enamel [3]. Together, these proteins enable the formation of a robust, acidogenic biofilm that protects the bacteria from environmental stress and concentrates organic acids, leading to the demineralization of tooth enamel [4]. Therapeutic targeting of these molecules aims to prevent cavities by inhibiting biofilm integrity and bacterial colonization rather than relying on broad-spectrum bactericidal agents [5]. Current pharmacological approaches include the use of fluoride to inhibit enzyme metabolism, chlorhexidine for broad biofilm disruption, and various natural polyphenols that specifically interfere with GTF activity and adhesin binding [6]. [1] https://pubmed.ncbi.nlm.nih.gov/21242687/ [2] https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3055735/ [3] https://pubmed.ncbi.nlm.nih.gov/20633131/ [4] https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3741677/ [5] https://pubmed.ncbi.nlm.nih.gov/21775778/ [6] https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3133681/

Other names

GlucosyltransferasesGTFsAntigen I/IISpaPPAcP1Glucan-binding proteinsGbpGtfBGtfCGtfD

Inhibition of glucosyltransferase enzymatic activity to prevent the synthesis of extracellular glucans and disruption of adhesin-mediated bacterial attachment to the salivary pellicle on tooth surfaces.