Molecular basis for the association of glucosyltransferases with the cell surface of oral streptococci (original) (raw)
Journal Article
,
Departments of Microbiology and Pediatric Dentistry, University of Texas Health Science Center, San Antonio, TX, U.S.A.
Correspondence to: C. Kato, Departments of Microbiology and Pediatric Dentistry, University of Texas Health Science Center, San Antonio, TX 78284, U.S.A.
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Departments of Microbiology and Pediatric Dentistry, University of Texas Health Science Center, San Antonio, TX, U.S.A.
Search for other works by this author on:
Received:
30 October 1990
Revision received:
27 November 1990
Accepted:
29 November 1990
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Summary
The expression of Streptococcus mutans mutant glucosyltransferase-I enzymes in S. sanguis and S. milleri suggests that cell-associated glucosyltransferase activity is dependent upon both glucan synthesis and glucan binding by the carboxyl-terminal repeating units of the enzyme. Mutant enzymes lacking these repeating units were only present in the extracellular fluids of these transformed streptococcal strains.
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© 1991 Federation of European Microbiological Societies
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