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Updated: Jun 10, 2026

Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
Streptococcus salivarius mutants defective in mannose phosphotransferase systems show reduced sensitivity to mutacins
Guillaume G Nicolas1, Michel Frenette, Marc C Lavoie
1Département de biochimie, microbiologie et bioinformatique, Faculté des sciences et de génie, Université Laval, Québec, QC G1K 7P4, Canada. guillaume.nicolas.1@ulaval.ca
Abstract:
Twenty-four mutacin-producing Streptococcus mutans strains were screened for their propensity to produce class II one-peptide bacteriocin using a deferred antagonism assay. Streptococcus salivarius and 3 mutants defective in their mannose phosphotransferase systems (mannose-PTS) were used as sensitive strains to identify which mannose-PTS could act as the docking site for class II one-peptide bacteriocin activity. We observed that only 2 strains of S. mutans, T9 and 3B, potentially produce class II one-peptide bacteriocin, namely mutacins I-T9 and R-3B, but with no preference for any mannose-PTS complex as a target.
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