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J. Biol. Chem., Vol. 279, Issue 37, 39017-39025, September 10, 2004

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High Affinity Streptococcal Binding to Human Fibronectin Requires Specific Recognition of Sequential F1 Modules^*

Ulrich Schwarz-Linek, Ewa S. Pilka, Andrew R. Pickford, Jung Hwa Kim, Magnus Höök, Iain D. Campbell, and Jennifer R. Potts¶

From the Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom and the Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A&M University System Health Science Center, Houston, Texas 77030-3303

Fibronectin (Fn) binding by the Streptococcus pyogenes protein SfbI has been shown to trigger integrin-dependent internalization of this pathogen by human epithelial and endothelial cells. Here, using nuclear magnetic resonance spectroscopy and isothermal titration calorimetry in a dissection approach, the basis for the specificity and high affinity of the interaction between the N-terminal domain of Fn and SfbI is revealed. Each of the five Fn type 1 modules is directly involved in the interaction and is recognized by short consecutive motifs within the repeat region of SfbI. Crucially, these motifs must be combined in the correct order to form a high affinity ligand for the N-terminal domain of Fn.

Received for publication, May 7, 2004 , and in revised form, June 18, 2004.

^* This research was supported by the Biotechnology and Biological Sciences Research Council and the Wellcome Trust. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed. Tel.: 44-1865-275772; Fax: 44-1865-275253; E-mail: jennifer.potts{at}bioch.ox.ac.uk.

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