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Infect Immun. 1990 March; 58(3): 667-673

Sequence analysis of the gene for the glucan-binding protein of Streptococcus mutans Ingbritt.

J A Banas, R R Russell and J J Ferretti

Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City 73190.

ABSTRACT

The nucleotide sequence of the gbp gene, which encodes the glucan-binding protein (GBP) of Streptococcus mutans, was determined. The reading frame for gbp was 1,689 bases. A ribosome-binding site and putative promoter preceded the start codon, and potential stem-loop structures were identified downstream from the termination codon. The deduced amino acid sequence of the GBP revealed the presence of a signal peptide of 35 amino acids. The molecular weight of the processed protein was calculated to be 59,039. Two series of repeats spanned three-quarters of the carboxy-terminal end of the protein. The repeats were 32 to 34 and 17 to 20 amino acids in length and shared partial identity within each series. The repeats were found to be homologous to sequences hypothesized to be involved in glucan binding in the GTF-I of S. downei and to sequences within the protein products encoded by gtfB and gtfC of S. mutans. The repeated sequences may represent peptide segments that are important to glucan binding and may be distributed among GBPs from other bacterial inhabitants of plaque or the oral cavity.

Infect Immun. 1990 March; 58(3): 667-673




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