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Originally published In Press as doi:10.1074/jbc.M005297200 on September 15, 2000

J. Biol. Chem., Vol. 275, Issue 51, 39837-39845, December 22, 2000
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Monoclonal Antibodies to CNA, a Collagen-binding Microbial Surface Component Recognizing Adhesive Matrix Molecules, Detach Staphylococcus aureus from a Collagen Substrate*

Livia VisaiDagger §, Yi Xu§, Fabrizia CasoliniDagger , Simonetta RindiDagger , Magnus Höök, and Pietro SpezialeDagger ||

From the Dagger  Department of Biochemistry, University of Pavia, Viale Taramelli 3/B, I-27100 Pavia, Italy and the  Center for Extracellular Matrix Biology and the Department of Biochemistry and Biophysics, Institute of Biosciences and Technology, Texas A & M University System Health Science Center, Houston, Texas 77030-3303

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 from Enterococcus faecalis. These mAbs were able to inhibit 125I-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.

* This work was supported by MURST Cofin. 1998: Cell-Matrix Interactions in Biology and Pathology (to S. R.), FAR (Fondo d'Ateneo per la Ricerca, University of Pavia, to P. S.), and Inhibitex, Inc (to P. S. and M. H.), National Institutes of Health Grant AR44415 (to M. H.), and the Arthritis Foundation (to Y. X.).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.

§ These authors contributed equally to this work.

|| To whom correspondence should be addressed: Tel.: 39-0382-507-787; Fax: 39-0382-4231-08; E-mail: pspeziale@unipv.it.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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