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The Tandem ß-Zipper Model Defines High Affinity Fibronectin-binding Repeats within Staphylococcus aureus FnBPA

Meenan, N.A.G., Visai, L., Valtulina, V., Schwarz-Linek, U., Norris, N.C., Gurusiddappa, S., Höök, M., Speziale, P. and Potts, J.R. (2007) The Tandem ß-Zipper Model Defines High Affinity Fibronectin-binding Repeats within Staphylococcus aureus FnBPA. Journal of Biological Chemistry, 282 (35). pp. 25893-258902. ISSN 0021-9258

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Binding of the fibronectin-binding protein FnBPA from Staphylococcus aureus to the human protein fibronectin has previously been implicated in the development of infective endocarditis, specifically in the processes of platelet activation and invasion of the endothelium. We recently proposed a model for binding of fibronectin to FnBPA in which the bacterial protein contains 11 potential binding sites (FnBPA-1 to FnBPA-11), each composed of motifs that bind to consecutive fibronectin type 1 modules in the N-terminal domain of fibronectin. Here we show that six of the 11 sites bind with dissociation constants in the nanomolar range; other sites bind more weakly. The high affinity binding sites include FnBPA-1, the sequence of which had previously been thought to be encompassed by the fibrinogen-binding A domain of FnBPA. Both the number and sequence conservation of the type-1 module binding motifs appears to be important for high affinity binding. The in vivo relevance of the in vitro binding studies is confirmed by the presence of antibodies in patients with S. aureus infections that specifically recognize complexes of these six high affinity repeats with fibronectin.

Item Type: Article
Institution: The University of York
Academic Units: The University of York > Biology (York)
Depositing User: York RAE Import
Date Deposited: 09 Feb 2009 12:30
Last Modified: 09 Feb 2009 12:30
Published Version: http://dx.doi.org/10.1074/jbc.M703063200
Status: Published
Publisher: The American Society for Biochemistry and Molecular Biology
Identification Number: 10.1074/jbc.M703063200
URI: http://eprints.whiterose.ac.uk/id/eprint/7663

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