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Monoclonal Antibodies to CNA, a Collagen-binding Microbial Surface Component Recognizing Adhesive Matrix Molecules, DetachStaphylococcus aureus from a Collagen Substrate*

L. Visai,Yi Xu,F. Casolini,S. Rindi,M. Höök,P. Speziale

Published 2000 in Journal of Biological Chemistry

ABSTRACT

Previous studies showed that Staphylococcus aureus expresses a collagen-binding MSCRAMM (Microbial Surface Component Recognizing Adhesive Matrix Molecules), CNA, that is necessary and sufficient for S. aureus cells to adhere to cartilage and is a virulence factor in experimental septic arthritis. We have now used a monoclonal antibody (mAb) approach to further analyze the structure and function of CNA. 22 mAbs raised against the minimal ligand binding domain, CNA-(151–318), were shown to bind to the MSCRAMM with similar affinity. All mAbs appear to recognize conformation-dependent epitopes that were mapped throughout the CNA-(151–318) domain using a chimeric strategy where segments of CNA are grafted on ACE, a structurally related MSCRAMM fromEnterococcus faecalis. These mAbs were able to inhibit125I-collagen binding to CNA-(151–318) as well as to intact S. aureus cells. They also interfered with the attachment of bacteria to collagen substrates. Furthermore, some of the mAbs could effectively displace 125I-collagen bound to the bacteria. These displacing mAbs were also able to detach bacteria that had adhered to a collagen substrate in a preincubation, raising the possibility that some of the mAbs may be used as therapeutic agents.

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