Sequence diversity in the A domain of Staphylococcus aureus fibronectin-binding protein A.

ABSTRACT:

Background

Fibronectin-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.

Results

Seven different isotype forms (I - VII) of the FnBPA A domain were identified which were

SUBMITTER: Loughman A 

PROVIDER: S-EPMC2390562 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature