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Effect of inactivation of gtf genes on adherence of Streptococcus downei

Lookup NU author(s): Emeritus Professor Roy Russell


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The activity of glucosyltransferases (GTF), a group of enzymes that synthesize water-soluble and -insoluble glucans from sucrose, significantly contributes to the cariogenicity of mutans streptococci. Streptococcus downei produces four glucosyltransferases, GTFI, which produces insoluble glucan, and GTFS, GTFT, and GTFU, which synthesize soluble glucans. We have previously reported that inactivation of gtfS results in altered adherence and have now examined its interaction with other enzymes by constructing mutants which were gtfS, gtfS/gtfT, gtfS/gtfT and gtfI. The mutants were tested for their ability to accumulate on wires and on plastic microtiter trays in the presence of sucrose. The gtfS mutant displayed a reduced ability to adhere compared to the wild type but there was no further reduction of adherence in a gtfS/gtfT mutant. In contrast, the gtfS/gtfI double mutant showed a drastic reduction in adherence and when gtfI alone was inactivated, bacteria were unable to adhere to a hard surface. The results confirmed that insoluble glucan is required for strong adherence to a smooth surface but that the amount and structure of this glucan is dependent upon the availability of soluble glucans to act as primer molecules.

Publication metadata

Author(s): Russell RRB; Colby SM; McLaughlin RE; Ferretti JJ

Publication type: Article

Publication status: Published

Journal: Oral Microbiology and Immunology

Year: 1999

Volume: 14

Issue: 1

Pages: 27-32

Print publication date: 01/02/1999

ISSN (print): 0902-0055

ISSN (electronic): 1399-302X

Publisher: Wiley-Blackwell Publishing, Inc.


DOI: 10.1034/j.1399-302X.1999.140103.x

PubMed id: 10204477


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