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pubmed-article:18466610pubmed:abstractTextFibronectin-binding protein A (FnBPA) mediates adhesion of Staphylococcus aureus to fibronectin, fibrinogen and elastin. We previously reported that S. aureus strain P1 encodes an FnBPA protein where the fibrinogen/elastin-binding domain (A domain) is substantially divergent in amino acid sequence from the archetypal FnBPA of S. aureus NCTC8325, and that these variations created differences in antigenicity. In this study strains from multilocus sequence types (MLST) that spanned the genetic diversity of S.aureus were examined to determine the extent of FnBPA A domain variation within the S. aureus population and its effect on ligand binding and immuno-crossreactivity.lld:pubmed
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pubmed-article:18466610pubmed:articleTitleSequence diversity in the A domain of Staphylococcus aureus fibronectin-binding protein A.lld:pubmed
pubmed-article:18466610pubmed:affiliationDepartment of Microbiology, Moyne Institute of Preventive Medicine, University of Dublin, Trinity College, Dublin, Ireland. loughmaa@tcd.ielld:pubmed
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