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Infection and Immunity, November 2001, p. 6931-6941, Vol. 69, No. 11
Department of
Immunology1 and Department of Molecular
Genetics,2 The Forsyth Institute, Boston,
Massachusetts 02115
Received 6 June 2001/Returned for modification 23 July
2001/Accepted 22 August 2001
Streptococcus mutans, the primary etiological agent of
dental caries, produces several activities that promote its
accumulation within the dental biofilm. These include
glucosyltransferases, their glucan products, and proteins that bind
glucan. At least three glucan binding proteins have been identified,
and GbpB, the protein characterized in this study, appears to be novel. The gbpB gene was cloned and the predicted protein sequence
contained several unusual features and shared extensive homology with a putative peptidoglycan hydrolase from group B streptococcus.
Examination of gbpB genes from clinical isolates of
S. mutans revealed that DNA polymorphisms, and hence amino
acid changes, were limited to the central region of the gene,
suggesting functional conservation within the amino and carboxy termini
of the protein. The GbpB produced by clinical isolates and laboratory
strains showed various distributions between cells and culture medium,
and amounts of protein produced by individual strains correlated
positively with their ability to grow as biofilms in an in vitro assay.
0019-9567/01/$04.00+0 DOI: 10.1128/IAI.69.11.6931-6941.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Cloning of the Streptococcus mutans Gene
Encoding Glucan Binding Protein B and Analysis of Genetic Diversity and
Protein Production in Clinical Isolates
*
Corresponding author. Mailing address: Department of
Molecular Genetics, The Forsyth Institute, 140 Fenway, Boston, MA
02115. Phone: (617) 262-5200, ext. 344. Fax: (617) 262-4021. E-mail: mduncan{at}forsyth.org.
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