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RESEARCH REPORT |
1 Department of Oral Biology, College of Dentistry, University of Illinois at Chicago, Chicago, IL 60612; and
2 Department of Oral Diagnosis, School of Dental Medicine, University of Connecticut Health Center, Farmington, CT 06030;
* corresponding author, ltao{at}uic.edu
Streptococcus mutans glucosyltransferases form extracellular glucans from sucrose to promote adhesion to the teeth. We tested whether additional factors are involved in S. mutans sucrose-dependent adhesion. By screening a pVA891-insertion mutant library of S. mutans LT11, we isolated four clones deficient in adhesion to glass in the presence of sucrose, but normal in glucosyltransferase activities. The genetic loci flanking the insertion sites were retrieved and identified. They encode glycerol-3-phosphate dehydrogenase, an ABC transporter, a multidrug-efflux pump, and either the ribulose monophosphate operon or ascorbate metabolism operon. The four mutants were analyzed for their phenotypic expression and in vivo colonization in rats. The multidrug efflux pump mutant failed to colonize the rats. Three other mutants colonized the rats by reverting to the wild type. Therefore, these four factors may contribute to S. mutans sucrose-dependent adhesion.
KEY WORDS: Streptococcus mutans sucrose-dependent adhesion sucrose virulence glucosyltransferases multidrug-efflux pump
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