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Cloning and sequence analysis of the gbpC gene encoding a novel glucan-binding protein of Streptococcus mutans.

ABSTRACT: We have isolated dextran-aggregation-negative mutants of Streptococcus mutans following random mutagenesis with plasmid pVA891 clone banks. A chromosomal region responsible for this phenotype was characterized in one of the mutants. A 2.2-kb fragment from the region was cloned in Escherichia coli and sequenced. A gene specifying a putative protein of 583 amino acid residues with a calculated molecular weight of 63,478 was identified. The amino acid sequence deduced from the gene exhibited no similarity to the previously identified S. mutans 74-kDa glucan-binding protein or to glucan-binding domains of glucosyltransferases but exhibited similarity to surface protein antigen (Spa)-family proteins from streptococci. Extract from an E. coli clone of the gene exhibited glucan-binding activity. Therefore, the gene encoded a novel glucan-binding protein.

SUBMITTER: Sato Y

PROVIDER: S-EPMC176112 | biostudies-other | 1997 Feb

REPOSITORIES: biostudies-other

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Cloning and sequence analysis of the gbpC gene encoding a novel glucan-binding protein of Streptococcus mutans.

Sato Y Y Yamamoto Y Y Kizaki H H

Infection and immunity 19970201 2

We have isolated dextran-aggregation-negative mutants of Streptococcus mutans following random mutagenesis with plasmid pVA891 clone banks. A chromosomal region responsible for this phenotype was characterized in one of the mutants. A 2.2-kb fragment from the region was cloned in Escherichia coli and sequenced. A gene specifying a putative protein of 583 amino acid residues with a calculated molecular weight of 63,478 was identified. The amino acid sequence deduced from the gene exhibited no sim ...[more]

PMID: 9009329

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