Interaction of fibrinogen with staphylococcal clumping factor and with platelets.

Hawiger J, Kloczewiak M, Timmons S, Strong D, Doolittle RF
Ann N Y Acad Sci. 1983 408: 521-35

PMID: 6223560 · DOI:10.1111/j.1749-6632.1983.tb23270.x

Fibrinogen, a clottable plasma glycoprotein, participates in cell adhesion phenomena involving prokaryotic cells, e.g. staphylococci, and eukaryotic cell fragments, e.g. platelets. Among the three chains (alpha, beta, gamma) of human fibrinogen, the gamma chain bears the main site recognizing the staphylococcal clumping receptor and human platelet receptor induced by ADP. The platelet receptors are also recognized, albeit less avidly, by a site associated with the alpha chain. The gamma chain site recognizing staphylococcal clumping factor exists on the COOH-terminal segment of this chain encompassing the 15 residues (gamma 397-411) including the COOH-terminal valine. The location of the gamma chain site interacting with the human platelet receptor had been pinpointed to the 27 residue CNBr COOH-terminal segment (gamma 385-411). The results of enzymatic degradation of the 27-residue peptide indicate that the continuity of the last 15 amino acid residues at the COOH-terminal end of the gamma chain of human fibrinogen seems to be essential for its interaction with human platelets. The sequence of the gamma chain interacting with the platelet receptor (gamma 385-411) indicates that this segment is a unique region of fibrinogen endowed with three important functions: cross-linking of fibrin, clumping of staphylococci, and aggregation of platelets. [Note added in proof: Recently we obtained evidence that dodecapeptide gamma 393-411 fully retains platelet receptor recognition site (Kloczewiak et al. 1983. Clin. Res 31:534A.)]

MeSH Terms (12)

Amino Acid Sequence Blood Platelets Coagulase Fibrin Fibrinogen Degradation Products Fibrinogen Fibrinolysin Humans Immunoglobulin Fab Fragments Models, Biological Molecular Weight Receptors, Immunologic Staphylococcus

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