| Autor: |
Visai, Livia, Xu, Yi, Casolini, Fabrizia, Rindi, Simonetta, Höök, Magnus, Speziale, Pietro |
| Zdroj: |
Journal of Biological Chemistry; December 2000, Vol. 275 Issue: 51 p39837-39845, 9p |
| Abstrakt: |
Previous studies showed that Staphylococcus aureusexpresses a collagen-binding MSCRAMM (Microbial Surface Component Recognizing Adhesive Matrix Molecules), CNA, that is necessary and sufficient for S. aureuscells 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. aureuscells. 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. |
| Databáze: |
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