| Literature DB >> 9009329 |
Y Sato1, Y Yamamoto, H Kizaki.
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.Entities:
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Year: 1997 PMID: 9009329 PMCID: PMC176112 DOI: 10.1128/iai.65.2.668-675.1997
Source DB: PubMed Journal: Infect Immun ISSN: 0019-9567 Impact factor: 3.441