Streptococcus pyogenes Collagen Type I-binding Cpa Surface Protein

The Streptococcus pyogenes collagen type I-binding protein Cpa (collagen-binding protein of group A streptococci) expressed by 28 serotypes of group A streptococci has been extensively characterized at the gene and protein levels. Evidence for three distinct families of cpa genes was found, all of w...

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Bibliographic Details
Published in:The Journal of biological chemistry 2005-09, Vol.280 (39), p.33228-33239
Main Authors: Kreikemeyer, Bernd, Nakata, Masanobu, Oehmcke, Sonja, Gschwendtner, Caroline, Normann, Jana, Podbielski, Andreas
Format: Article
Language:English
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Summary:The Streptococcus pyogenes collagen type I-binding protein Cpa (collagen-binding protein of group A streptococci) expressed by 28 serotypes of group A streptococci has been extensively characterized at the gene and protein levels. Evidence for three distinct families of cpa genes was found, all of which shared a common sequence encoding a 60-amino acid domain that accounted for selective binding to type I collagen. Surface plasmon resonance-based affinity measurements and functional studies indicated that the expression of Cpa was consistent with an attachment role for bacteria to tissue containing collagen type I. A cpa mutant displayed a significantly decreased internalization rate when incubated with HEp-2 cells but had no effect on the host cell viability. By utilizing serum from patients with a positive titer for streptolysin/DNase antibody, an increased anti-Cpa antibody titer was noted for patients with a clinical history of arthritis or osteomyelitis. Taken together, these results suggest Cpa may be a relevant matrix adhesin contributing to the pathogenesis of S. pyogenes infection of bones and joints.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M502896200