tailieunhanh - Báo cáo khoa học: Functional analysis of a murine monoclonal antibody against the repetitive region of the fibronectin-binding adhesins fibronectin-binding protein A and fibronectin-binding protein B from Staphylococcus aureus

Fibronectin-binding proteins A and B are multifunctional LPXTG staphy-lococcal adhesins, comprising an N-terminal region that binds fibrinogen and elastin, and a C-terminal domain that interacts with fibronectin. The C-terminal domain of fibronectin-binding protein A is organized into 11 tandem repeats, six of which bind the ligand with high affinity; other sites bind more weakly. | Functional analysis of a murine monoclonal antibody against the repetitive region of the fibronectin-binding adhesins fibronectin-binding protein A and fibronectin-binding protein B from Staphylococcus aureus Giulio Provenza1 Maria Provenzano1 Livia Visai1 2 Fiona M. Burke3 Joan A. Geoghegan3 Matteo Stravalaci4 Marco Gobbi4 Giuliano Mazzini5 Carla Renata Arciola6 Timothy J. Foster3 and Pietro Speziale1 1 Department of Biochemistry University of Pavia Italy 2 Center for Tissue Engineering CIT University of Pavia Italy 3 Department of Microbiology Moyne Institute of Preventive Medicine University of Dublin Ireland 4 Department of Biochemistry and Molecular Pharmacology Istituto di Ricerche Farmacologiche Mario Negri Milan Italy 5 IGM-CNR Histochemistry Cytometry Department of AnimalBiology University of Pavia Italy 6 Research Unit on Implant Infections Rizzoli Orthopedic Institute Bologna Italy Keywords adhesin antibody fibronectin repeat Staphylococcus Correspondence P. Speziale University of Pavia Department of Biochemistry Viale Taramelli 3 b 27100 Pavia Italy Fax 39 0382 423108 Tel 39 0382 987787 E-mail pspeziale@ These authors contributed equally to this work Received 17 June 2010 revised 22 July 2010 accepted 25 August 2010 doi Fibronectin-binding proteins A and B are multifunctional LPXTG staphylococcal adhesins comprising an N-terminal region that binds fibrinogen and elastin and a C-terminal domain that interacts with fibronectin. The C-terminal domain of fibronectin-binding protein A is organized into 11 tandem repeats six of which bind the ligand with high affinity other sites bind more weakly. Fibronectin-binding protein B has been postulated to harbor 10 rather than 11 repeats but it contains the same number of high-affinity fibronectin-binding sites as fibronectin-binding protein A. In this study we confirm this prediction and show that six of 10 sites bind with dissociation constants in the nanomolar range. We .

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