Impairment of melibiose utilization in Streptococcus mutans serotype c gtfA mutants

Author:

Barletta R G1,Curtiss R1

Affiliation:

1. Department of Microbiology, University of Alabama, Birmingham 35294.

Abstract

The Streptococcus mutans serotype c gtfA gene encodes a 55-kilodalton sucrose-hydrolyzing enzyme. Analysis of S. mutans gtfA mutants revealed that the mutant strains were specifically impaired in the ability to use melibiose as a sole carbon source. S. mutans gtfA mutant strains synthesized less alpha-galactosidase activity inducible by raffinose than wild-type strains. Melibiose (an inducer in wild-type strains) failed to induce significant levels of alpha-galactosidase in the mutant strains. We hypothesize that melibiose use by S. mutans requires the interaction of the GtfA enzyme, or another gene product under the control of the gtfA promoter, with other gene product(s) involved in melibiose transport or hydrolysis.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Reference24 articles.

1. Cloning of a Streptococcus mutans glucosyltransferase gene coding for insoluble glucan synthesis;Aoki H.;Infect. Immun.,1986

2. Analysis of the virulence of Streptococcus mutans serotype c gtfA mutants in the rat model system;Barletta R. G.;Infect. Immun.,1988

3. Tight genetic linkage of a glucosyltransferase and dextranase of Streptococcus mutans GS-5;Burne R. A.;J. Dent. Res.,1986

4. Extracellular invertase in Streptococcus mutans;Chassy B. M.;Life Sci.,1974

5. Genetic analysis of Streptococcus mutans virulence;Curtiss R.;Curr. Top. Microbiol. Immunol.,1985

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