Disease relevance of gtfD

• Isolation and characterization of the Streptococcus mutans gtfD gene, coding for primer-dependent soluble glucan synthesis [1].
• The vector together with one complete and one incomplete copy of the gtfD gene was removed from the chromosome of strain DP2 following EcoRI digestion, religation, and transformation of E. coli HB101 [1].
• Southern blot analysis further suggested that the gtfD gene does not share demonstrable homology with the gtf genes from Streptococcus sanguis or Streptococcus sobrinus [1].
• Streptococcus mutans produces a number of extracellular sucrose-metabolizing enzymes that contribute to the ability of the organism to cause dental caries, including three glucosyltransferases, the products of the gtfB, gtfC and gtfD genes, and a fructosyltransferase, encoded by the ftf gene [2].

High impact information on gtfD

• Apigenin (0.1 mM) significantly decreased the expression of gtfB and gtfC mRNA (P < 0.05); in contrast, it increased the expression of gtfD in S. mutans growing in the planktonic state [3].
• In the present study, we investigated the influence of apigenin on gtfB, gtfC, and gtfD expression in S. mutans UA159 [3].
• The results of Northern hybridization and/or real-time reverse transcription-PCR experiments reveal increased expression of both Gtf-S and glucan binding protein C (GbpC) in a tarC knockout mutant (GMS900), thereby supporting the notion that TarC acts as a negative transcriptional regulator [4].
• Insertional inactivation of the gtfD gene indicated that this gene is not required for in vitro sucrose-dependent adherence to smooth surfaces [1].
• The resultant plasmid, pNH4, expressed glucosyltransferase S (GTF-S) activity [1].

Chemical compound and disease context of gtfD

• Streptococcus mutans produces three glucosyltransferases, coded by gtfB, gtfC, and gtfD, whose cooperative action is essential for sucrose-dependent cellular adhesion [5].

Biological context of gtfD

• Inactivation of either gtfB and gtfC or ftf dramatically reduced virulence; the subsequent inactivation of gtfD did not enhance the effect of reduced virulence [6].
• An analysis of the transcription start sites for the gtfB, gtfC, gtfD and ftf genes revealed that each transcript was initiated at a purine residue [7].
• The nucleotide sequence of the Streptococcus mutans GS-5 gtfD gene coding for the glucosyltransferase which synthesizes water-soluble glucan (GTF-S) has been determined [8].
• The cell-associated GtfB and GtfC from strain GS-5DD lacking the gtfD gene expression were extracted by urea, renatured by dialysis in sodium phosphate buffer and then separated from the other wall-associated components by column chromatography [9].

Associations of gtfD with chemical compounds

• Furthermore, inactivation of the gtfD gene in a gtfC gtfB mutant indicated that three distinct gtf genes involved in glucan formation are present on the S. mutans GS-5 chromosome [1].
• These findings support the involvement of Cu(2+) as an effector molecule in the regulation of S. mutans gtfD [10].
• In the present study, the levels of expression of the gtfB, gtfC, gtfD and ftf genes coding for polysaccharide-synthesizing enzymes in strain Xc100L were compared with those in strain Xc [11].

Other interactions of gtfD

• Our findings show that dietary carbohydrates have a major influence on the transcription of ftf, gtfB, gtfC and gtfD, but less on vicR [12].

Analytical, diagnostic and therapeutic context of gtfD

• The results of sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Western blotting, and N-terminal sequence analysis confirmed the absence of a 155-kDa glucosyltransferase S (Gtf-S) from GMS315 protein profiles [4].

References