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J. Biol. Chem., Vol. 277, Issue 49, 47428-47435, December 6, 2002
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From the Group A Streptococcus pyogenes has
surface-located fibronectin (Fn)-binding proteins known to be a major
virulence factor, which adheres to and invades host cells. We present a
novel Fn-binding protein of group A streptococcus serotype M3 and M18
strains isolated from patients with toxic shock-like syndrome (TSLS).
By searching the whole genome sequence of an M3 strain from a TSLS
patient, an open reading frame was found among the putative surface
proteins. It possessed an LPXTG motif and Fn-binding repeat
domains in the C-terminal region and was designated as FbaB (Fn-binding
protein of group A streptococci type B). The fbaB gene was
found in all M3 and M18 strains examined, although not in other M
serotypes. Furthermore, FbaB protein was expressed on the cell surface
of TSLS strains but not on non-TSLS ones. Enzyme-linked immunosorbent assay and ligand blotting revealed that recombinant FbaB exhibits a
strong Fn-binding ability. An FbaB-deficient mutant strain showed 6-fold lower adhesion and invasion efficiencies to HEp-2 cells than the
wild type. Moreover, mortality was decreased in mice infected with the
mutant strain in comparison to the wild type. These data suggest that
FbaB is etiologically involved in the development of invasive
streptococcal diseases.
The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession number(s) AB084272.
Molecular Characterization of a Novel
Fibronectin-binding Protein of Streptococcus pyogenes
Strains Isolated from Toxic Shock-like Syndrome Patients*
§,§¶,,, and
Department of Oral and Molecular
Microbiology, Osaka University Graduate School of Dentistry,
Suita-Osaka 565-0871 and § PRESTO, Japan Science and
Technology Corporation, Kawaguchi, Saitama 332-0012, Japan
*
This work was supported by grants from Japan Science and
Technology Corp., the Japan Society for Promotion of Science, the Ministry of Health, Labour and Welfare, and the Ministry of Education, Culture, Sports, Science and Technology.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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