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pubmed-article:7934883pubmed:abstractTextStaphylococcus aureus has been shown to interact specifically with fibrinogen. Three different extracellular fibrinogen-binding proteins, two of which have coagulase activity, are produced by S. aureus strain Newman. The role of these fibrinogen-binding proteins during staphylococcal colonization and infection has not yet been fully elucidated. Here we describe the cloning, sequencing and expression of a gene for a 19 kDa fibrinogen-binding protein. This gene, called fib, encodes a 165-amino-acid polypeptide, including a 29-amino-acid signal sequence. The recombinant protein, which has an estimated molecular mass of 15.9 kDa, bound fibrinogen and was recognized by a polyclonal antiserum against the native Fib protein. Homologies between the Fib protein and the fibrinogen-binding domain of coagulase suggest that amino acids within this domain are involved in the binding to fibrinogen.lld:pubmed
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pubmed-article:7934883pubmed:authorpubmed-author:FlockJ IJIlld:pubmed
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pubmed-article:7934883pubmed:articleTitleCloning and characterization of a gene for a 19 kDa fibrinogen-binding protein from Staphylococcus aureus.lld:pubmed
pubmed-article:7934883pubmed:affiliationCentre for Biotechnology, Karolinska Institute, NOVUM, Huddinge, Sweden.lld:pubmed
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