Cloning and characterization of a gene for a 19 kDa fibrinogen-binding protein from Staphylococcus aureus

Mol Microbiol. 1994 May;12(4):599-606. doi: 10.1111/j.1365-2958.1994.tb01046.x.


Staphylococcus aureus has been shown to interact specifically with fibrinogen. Three different extracellular fibrinogen-binding proteins, two of which have coagulase activity, are produced by S. aureus strain Newman. The role of these fibrinogen-binding proteins during staphylococcal colonization and infection has not yet been fully elucidated. Here we describe the cloning, sequencing and expression of a gene for a 19 kDa fibrinogen-binding protein. This gene, called fib, encodes a 165-amino-acid polypeptide, including a 29-amino-acid signal sequence. The recombinant protein, which has an estimated molecular mass of 15.9 kDa, bound fibrinogen and was recognized by a polyclonal antiserum against the native Fib protein. Homologies between the Fib protein and the fibrinogen-binding domain of coagulase suggest that amino acids within this domain are involved in the binding to fibrinogen.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Base Sequence
  • Carrier Proteins / genetics*
  • Carrier Proteins / metabolism
  • Cloning, Molecular
  • DNA, Bacterial / genetics
  • Escherichia coli / genetics
  • Fibrinogen / metabolism*
  • Genes, Bacterial*
  • Molecular Sequence Data
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Restriction Mapping
  • Sequence Homology, Amino Acid
  • Sequence Homology, Nucleic Acid
  • Species Specificity
  • Staphylococcus aureus / genetics*
  • Staphylococcus aureus / metabolism


  • Bacterial Proteins
  • Carrier Proteins
  • DNA, Bacterial
  • Fib protein, Staphylococcus aureus
  • Recombinant Proteins
  • Fibrinogen

Associated data

  • GENBANK/X72013
  • GENBANK/X72014