Mapping the Fibrinogen-Binding Domain of Serum Opacity Factor of Group A Streptococci |
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Authors: | Harry S Courtney James B Dale David L Hasty |
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Institution: | (1) Veterans Affairs Medical Center, Research Service (151), 1030 Jefferson Avenue, Memphis, TN 38104, USA, US;(2) Department of Medicine, University of Tennessee, Memphis, TN, USA, US;(3) Department of Anatomy and Neurobiology, University of Tennessee, Memphis, TN, USA, US |
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Abstract: | Serum opacity factor (SOF) is a large, extracellular, and cell-bound protein of group A streptococci that has two known functions,
opacification of serum and binding of fibronectin. Herein, we describe a new function of SOF, the binding of fibrinogen. Utilizing
purified, truncated recombinant SOF proteins, the fibrinogen-binding domain was localized to a region in the C-terminus of
SOF encompassing amino acid residues 844–1047. Western-blot analysis revealed that SOF bound primarily to the β subunit of
fibrinogen. A SOF-negative mutant bound 50% less fibrinogen than did its wild-type parent. Furthermore, fibrinogen blocked
the binding of SOF to fibronectin. These data suggest that fibrinogen and fibronectin bind to the same domain within SOF.
It remains to be determined whether the binding of fibrinogen to SOF contributes to the virulence of group A streptococci.
Received: 13 June 2001 / Accepted: 20 July 2001 |
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