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. Author manuscript; available in PMC: 2017 Mar 1.

Published in final edited form as: Mol Microbiol. 2015 Dec 15;99(5):945–959. doi: 10.1111/mmi.13277

FIG 5 — (A) Quantitative analysis of expression of glucosyltransferase GtfBCD genes. Expression of gtfB, gtfC and gtfD in the indicated mutants was determined by qRT-PCR using RNA prepared from log-phase grown bacteria. Expression of mRNA was calibrated using 16S rRNA. Values represent the means of three different experiments with standard deviations. * = P < 0.01 of Student’s t test using Prism 5.0. (B) Western blotting analysis of GtfB and other S. mutans proteins. The amount of GtfB, AntigenI/II, GbpA, and GbpD in different S. mutans mutants was examined by Western blotting analysis of cell lysates of 6-h S. mutans cultures. Dnak was set as a loading control. (C) Quantification of Western blotting analysis of GtfB. Values represent the means of three experiments with standard deviations of relative fluorescence intensity of each band analyzed by using ImageJ. * = P < 0.01 of Student’s t test using Prism 5.0.

FIG 5 — (A) Quantitative analysis of expression of glucosyltransferase GtfBCD genes. Expression of gtfB, gtfC and gtfD in the indicated mutants was determined by qRT-PCR using RNA prepared from log-phase grown bacteria. Expression of mRNA was calibrated using 16S rRNA. Values represent the means of three different experiments with standard deviations. * = P < 0.01 of Student’s t test using Prism 5.0. (B) Western blotting analysis of GtfB and other S. mutans proteins. The amount of GtfB, AntigenI/II, GbpA, and GbpD in different S. mutans mutants was examined by Western blotting analysis of cell lysates of 6-h S. mutans cultures. Dnak was set as a loading control. (C) Quantification of Western blotting analysis of GtfB. Values represent the means of three experiments with standard deviations of relative fluorescence intensity of each band analyzed by using ImageJ. * = P < 0.01 of Student’s t test using Prism 5.0.

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