Adherence of Staphylococcus aureus Is Enhanced by an Endogenous Secreted Protein with Broad Binding Activity
AUTOR(ES)
Palma, Marco
FONTE
American Society for Microbiology
RESUMO
A novel mechanism for enhancement of adherence of Staphylococcus aureus to host components is described. A secreted protein, Eap (extracellular adherence protein), was purified from the supernatant of S. aureus Newman and found to be able to bind to at least seven plasma proteins, e.g., fibronectin, the α-chain of fibrinogen, and prothrombin, and to the surface of S. aureus. Eap bound much less to cells of Staphylococcus epidermidis, Streptococcus mutans, or Escherichia coli. The protein can form oligomeric forms and is able to cause agglutination of S. aureus. Binding of S. aureus to fibroblasts and epithelial cells was significantly enhanced by addition of Eap, presumably due to its affinity both for plasma proteins on the cells and for the bacteria.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=93727Documentos Relacionados
- Identification of a Staphylococcus aureus extracellular matrix-binding protein with broad specificity.
- Transcription of Staphylococcus aureus fibronectin binding protein genes is negatively regulated by agr and an agr-independent mechanism.
- The Extracellular Adherence Protein from Staphylococcus aureus Inhibits Neutrophil Binding to Endothelial Cells
- Penicillin-Binding Protein 1 of Staphylococcus aureus Is Essential for Growth
- Regulation of penicillin-binding protein activity: description of a methicillin-inducible penicillin-binding protein in Staphylococcus aureus.