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Identification of B- and T-cell epitopes within the fibronectin-binding domain of the SfbI protein of Streptococcus pyogenes.

ABSTRACT: The fibronectin-binding repeats of the SfbI protein of Streptococcus pyogenes constitute the minimal domain able to confer protection against lethal infection. We investigated the presence of B- and T-cell epitopes within this region in congenic mice. One linear B-cell epitope was recognized by BALB/b and BALB/k mice, whereas two epitopes were found in BALB/c animals. A unique T-cell epitope was recognized by all three mouse strains. All identified epitopes clustered in a 30-amino-acid fragment. These results suggest that this polypeptide may be suitable for incorporation into a polyepitope-based vaccine formulation against S. pyogenes.

SUBMITTER: Schulze K

PROVIDER: S-EPMC308920 | biostudies-literature | 2003 Dec

REPOSITORIES: biostudies-literature

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Identification of B- and T-cell epitopes within the fibronectin-binding domain of the SfbI protein of Streptococcus pyogenes.

Schulze Kai K Medina Eva E Chhatwal Gursharan S GS Guzmán Carlos A CA

Infection and immunity 20031201 12

The fibronectin-binding repeats of the SfbI protein of Streptococcus pyogenes constitute the minimal domain able to confer protection against lethal infection. We investigated the presence of B- and T-cell epitopes within this region in congenic mice. One linear B-cell epitope was recognized by BALB/b and BALB/k mice, whereas two epitopes were found in BALB/c animals. A unique T-cell epitope was recognized by all three mouse strains. All identified epitopes clustered in a 30-amino-acid fragment. ...[more]

PMID: 14638816

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Project description:The sequence of the fibronectin-binding domain of the fibronectin-binding protein of Streptococcus pyogenes (Sfb protein) was determined, and its role in streptococcal adherence was investigated by use of an Sfb fusion protein in adherence studies. A 1-kb DNA fragment coding for the binding domain of Sfb protein was cloned into the expression vector pEX31 to produce an Sfb fusion protein consisting of the N-terminal part of MS2 polymerase and a C-terminal fragment of the streptococcal protein. Induction of the vector promoter resulted in hyperexpression of fibronectin-binding fusion protein in the cytoplasm of the recombinant Escherichia coli cells. Sequence determination of the cloned 1-kb fragment revealed an in-frame reading frame for a 268-amino-acid peptide composed of a 37-amino-acid sequence which is completely repeated three times and incompletely repeated a fourth time. Cloning of one repeat into pEX31 resulted in expression of small fusion peptides that show fibronectin-binding activity, indicating that one repeat contains at least one binding domain. Each repeat exhibits two charged domains and shows high homology with the 38-amino-acid D3 repeat of the fibronectin-binding protein of Staphylococcus aureus. Sequence comparison with other streptococcal ligand-binding surface proteins, including M protein, failed to reveal significant homology, which suggests that Sfb protein represents a novel type of functional protein in S. pyogenes. The Sfb fusion protein isolated from the cytoplasm of recombinant cells was purified by fast protein liquid chromatography. It showed a strong competitive inhibition of fibronectin binding to S. pyogenes and of the adherence of bacteria to cultured epithelial cells. In contrast, purified streptococcal lipoteichoic acid showed only a weak inhibition of fibronectin binding and streptococcal adherence. These results demonstrate that Sfb protein is directly involved in the fibronectin-mediated adherence of S. pyogenes to epithelial cells.

Dataset Information

Identification of B- and T-cell epitopes within the fibronectin-binding domain of the SfbI protein of Streptococcus pyogenes.

Publications

Identification of B- and T-cell epitopes within the fibronectin-binding domain of the SfbI protein of Streptococcus pyogenes.

Similar Datasets

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