Binding of Glucosyltransferase and Glucan Synthesis by Streptococcus mutans and Other Bacteria

Author:

Hamada Shigeyuki1,Tai S.1,Slade Hutton D.1

Affiliation:

1. Department of Microbiology-Immunology, Northwestern University Medical and Dental Schools, Chicago, Illinois 60611

Abstract

Lyophilized and heat-treated cells from the seven serotypes of Streptococcus mutans were examined for their ability to bind added insoluble-product glucosyl-transferase (GTase) and to synthesize cell-associated glucan from [ 14 C]sucrose. Lyophilized cells of serotypes a and g did not synthesize any more additional glucan than did the controls after exposure to GTase. These cells, however, synthesized four- to eightfold-greater quantities of glucan than did the cells of the remaining serotypes. Lyophilized cells of serotypes b, c, d, e , and f synthesized two- to threefold-greater quantities of glucan after exposure to GTase than did the controls without added enzyme. Lyophilized cells of serotypes a and g synthesized 6- to 10-fold-greater quantities of glucan than did heat-treated cells of the same strain after binding of GTase. Lyophilized cells of the remaining serotypes synthesized only 1.6- to 3.3-fold-greater quantities of glucan than did the heat-treated cells. These results demonstrate that heat treatment to inactivate cell-associated GTase does not create additional GTase binding sites in S. mutans and that serotypes a and g are considerably more active in cell-associated glucan synthesis than cells of the other five serotypes. Ten species of gram-positive and gram-negative bacteria from five genera which do not produce in vitro plaque synthesized 10- to 100-fold-less glucan than did the S. mutans strains after exposure to GTase. Of these species, S. sanguis, Actinomyces viscosus , and A. naeslundii synthesized the largest quantities of glucan. Three mutant strains of S. mutans which possess a reduced ability for in vitro adherence but do agglutinate with glucan or dextran synthesized only one-third as much glucan after binding of GTase as the control. These results are discussed in relation to in vitro and in vivo plaque development and the agglutination of S. mutans. The results support earlier findings which indicate that the presence of bacterial species other than S. mutans in smooth-surface dental plaque is due in part to contact of the cells with glucan in the developing plaque and not to the binding of cell-free GTase and the in situ synthesis of glucan. The results obtained with these representative strains of the seven serotypes of S. mutans may not apply to the same extent to other strains within the serotypes.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Reference65 articles.

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3. Hydrogen ion activity in dental plaques of hamsters during metabolism of sucrose, glucose and fructose;Charlton G.;Arch. Oral Biol.,1971

4. Determination of saliva and dental plaque pH in hamsters with glass micro-electrodes;Charlton G.;Arch. Oral Biol.,1971

5. Ciardi J. E. 1976. Glucosyltransferases of S. mutans p. 101-110. In W. H. Bowen R. J. Genco and T. C. O'Brien (ed.) Immunologic aspects of dental caries a special supplement to Immunology Abstracts. Information Retrieval Inc. Washington D.C.

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