Streptococcus salivariusmutants defective in mannose phosphotransferase systems show reduced sensitivity to mutacins I-T9 and R-3B

Author:

Nicolas Guillaume G.12345,Frenette Michel12345,Lavoie Marc C.12345

Affiliation:

1. Département de biochimie, microbiologie et bioinformatique, Faculté des sciences et de génie, Université Laval, Québec, QC G1K 7P4, Canada.

2. Food Science and Nutrition Department, Institute for Nutraceuticals and Functional Foods, Université Laval, Québec, QC G1K 7P4, Canada.

3. Groupe de recherche en écologie buccale, Faculté de médecine dentaire, Université Laval, Québec, QC G1K 7P4, Canada.

4. Department of Biological and Chemical Sciences, Faculty of Pure and Applied Sciences, The University of the West Indies, Cave Hill Campus, P.O. Box 64, Bridgetown 11000, Barbados.

5. Département de stomatologie, Faculté de médecine dentaire, Université de Montréal, C.P. 6128, succursale Centre-ville, Montréal, QC H3C 3J7, Canada.

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.

Publisher

Canadian Science Publishing

Subject

Genetics,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Immunology,Microbiology

Reference27 articles.

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