Platelet-binding domains in 2 fibrinogen-binding proteins of Staphylococcus aureus identified by phage display

J Infect Dis. 2002 Jul 1;186(1):32-9. doi: 10.1086/341081. Epub 2002 Jun 10.


The adherence of microorganisms to platelets previously immobilized on the subendocardium in nonbacterial thrombotic endocarditis is considered an important pathogenic step in Staphylococcus aureus endocarditis. To identify and characterize bacterial factors involved in the adherence to platelets, a phage display library of S. aureus was generated by use of the phagemid pG8H6. The library was affinity panned against purified immobilized platelets. After a second panning against platelets, a significant increase in the number of eluted phagemid particles was observed; 27% of 88 randomly isolated clones expressed overlapping deduced amino acid sequences with high similarity to the C-terminal domain of the S. aureus coagulase. In addition, 22% of the clones expressed the N-terminal domain of the fibrinogen-binding protein Efb. The surface-associated fraction of the C-terminal domain of coagulase or the N-terminal domain of Efb may be involved in bacterial adherence to immobilized platelets, and fibrinogen may act as a bridging molecule in that interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Adhesion / genetics*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Blood Platelets / metabolism*
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Fibrinogen / metabolism*
  • Humans
  • Peptide Library*
  • Protein Binding
  • Staphylococcal Infections / etiology
  • Staphylococcus aureus / genetics*
  • Staphylococcus aureus / metabolism


  • Bacterial Proteins
  • Carrier Proteins
  • Fbe protein, bacteria
  • Peptide Library
  • Fibrinogen