Journal
MICROBIOLOGY-SGM
Volume 154, Issue -, Pages 550-558Publisher
SOC GENERAL MICROBIOLOGY
DOI: 10.1099/mic.0.2007/010868-0
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Funding
- Wellcome Trust Funding Source: Medline
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Clumping factor B (ClfB) of Staphylococcus aureus binds to cytokeratin 10 and to fibrinogen. In this study the binding site in human fibrinogen was localized to a short region within the C terminus of the A alpha-chain. ClfB only bound to the A alpha-chain of fibrinogen in a ligand-affinity blot and in solid-phase assays with purified recombinant fibrinogen chains. A variant of fibrinogen with wild-type B beta- and gamma-chains but with a deletion that lacked the C-terminal residues from 252-610 of the A alpha-chain did not support adherence of S. aureus Newman expressing ClfB. A series of truncated mutants of the recombinant A alpha-chain were tested for their ability to support adherence of S. aureus Newman ClfB(+), which allowed the binding site to be localized to a short segment of the unfolded flexible repeated sequence within the C terminus of the A alpha-chain. This was confirmed by two amino acid substititions within repeat 5 of the recombinant A alpha-chain which did not support adherence of Newman ClfB(+). Lactococcus lactis expressing ClfB mutants with amino acid substitutions (N256 and 0235) located in the putative ligand-binding trench between domains N2 and N3 of the A-domain were defective in adherence to immobilized fibrinogen and cytokeratin 10, suggesting that both ligands bind to the same or overlapping regions.
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