TAILIEUCHUNG - Báo cáo khoa học: The A domain of fibronectin-binding protein B of Staphylococcus aureus contains a novel fibronectin binding site

The fibronectin-binding proteins FnBPA and FnBPB are multifunctional adhesins than can also bind to fibrinogen and elastin. In this study, the N2N3 subdomains of region A of FnBPB were shown to bind fibrinogen with a similar affinity to those of FnBPA (2lM). | IFEBS Journal The A domain of fibronectin-binding protein B of Staphylococcus aureus contains a novel fibronectin binding site Fiona M. Burke1 Antonella Di Poto2 Pietro Speziale2 and Timothy J. Foster1 1 Department of Microbiology Moyne Institute of Preventive Medicine University of Dublin Trinity College Dublin Ireland 2 Department of Biochemistry University of Pavia Pavia Italy Keywords adhesion fibrinogen fibronectin Staphylococcus surface protein Correspondence T. J. Foster Department of Microbiology Moyne Institute of Preventive Medicine University of Dublin Trinity College Dublin Ireland Fax 0035316799294 Tel 0035318962014 E-mail tfoster@ Received 8 February 2011 revised 19 April 2011 accepted 4 May 2011 doi The fibronectin-binding proteins FnBPA and FnBPB are multifunctional adhesins than can also bind to fibrinogen and elastin. In this study the N2N3 subdomains of region A of FnBPB were shown to bind fibrinogen with a similar affinity to those of FnBPA 2 im . The binding site for FnBPB in fibrinogen was localized to the C-terminus of the y-chain. Like clumping factor A region A of FnBPB bound to the y-chain of fibrinogen in a Ca2 -inhibitable manner. The deletion of 17 residues from the C-ter-minus of domain N3 and the substitution of two residues in equivalent positions for crucial residues for fibrinogen binding in clumping factor A and FnBPA eliminated fibrinogen binding by FnBPB. This indicates that FnBPB binds fibrinogen by the dock-lock-latch mechanism. In contrast the A domain of FnBPB bound fibronectin with KD IM despite lacking any of the known fibronectin-binding tandem repeats. A truncate lacking the C-terminal 17 residues latching peptide bound fibronectin with the same affinity suggesting that the FnBPB A domain binds fibronectin by a novel mechanism. The substitution of the two residues required for fibrinogen binding also resulted in a loss of fibronectin binding. This combined with the observation .

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