Protein F, a fibronectin-binding protein, is an adhesin of the group A streptococcus Streptococcus pyogenes

Emanuel Hanski, Michael Caparon*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

274 Scopus citations

Abstract

Binding to fibronectin has been suggested to play an important role in adherence of the group A streptococcus Streptococcus pyogenes to host epithelial cells; however, the identity of the streptococcal fibronectin receptor has been elusive. Here we demonstrate that the fibronectin-binding property of S. pyogenes is mediated by protein F, a bacterial surface protein that binds fibronectin at high affinity. The gene encoding protein F (prtF) produced a functional fibronectin- binding protein in Escherichia coli. Insertional mutagenesis of the cloned gene generated a mutation that resulted in the loss of fibronectin-binding activity. When this mutation was introduced into the S. pyogenes chromosome by homologous recombination with the wild-type allele, the resulting strains no longer produced protein F and lost their ability to bind fibronectin. The mutation could be complemented by prtF introduced on a plasmid. Mutants lacking protein F had a much lower capacity to adhere to respiratory epithelial cells. These results demonstrate that protein F is an important adhesin of S. pyogenes.

Original languageEnglish
Pages (from-to)6172-6176
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number13
StatePublished - 1 Jul 1992

Keywords

  • Fibronectin receptor
  • Microbial adherence
  • Virulence

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