Journal
JOURNAL OF DENTAL RESEARCH
Volume 81, Issue 2, Pages 109-113Publisher
INT AMER ASSOC DENTAL RESEARCHI A D R/A A D R
DOI: 10.1177/154405910208100205
Keywords
glucosyltransferase; Streptococcus mutans; real-time RT-PCR; gene expression
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Streptococcus mutans produces three glucosyl-transferases, coded by gtfB, gtfC, and gtfD, whose cooperative action is essential for sucrose-dependent cellular adhesion. This cellular adhesion plays an important role in the formation of dental plaque and the initiation of dental caries. Since they bear genetic similarities and are large in size, differentiation of their gene expression has been difficult, and little is known about the dynamic process of gtf expression. Using a real-time reverse-transcription/polymerase chain-reaction, we determined the expression of each gtf. Under various conditions, the relative levels of transcription were gtfB > gtfD > gtfC. Sucrose enhanced gtfD expression, whereas it reduced that of gtfB and gtfC, suggesting the presence of independent promoters, Quantitative analyses demonstrated coincidence between the ratio of expression of each gtf and the ratio previously identified as optimal for sucrose-dependent adhesion in vitro, suggesting that S. mutans produces GTF at an optimal ratio to adhere to the tooth surface.
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