The molecular basis of fibronectin-mediated bacterial adherence to host cells

Ulrich Schwarz-Linek, Magnus Höök, Jennifer R. Potts

Research output: Contribution to journalArticlepeer-review

208 Citations (Scopus)

Abstract

Many pathogenic Gram-positive bacteria produce cell wall-anchored proteins that bind to components of the extracellular matrix (ECM) of the host. These bacterial MSCRAMMs (microbial surface components recognizing adhesive matrix molecules) are thought to play a critical role in infection. One group of MSCRAMMs, produced by staphylococci and streptococci, targets fibronectin (Fn, a glycoprotein found in the ECM and body fluids of vertebrates) using repeats in the C-terminal region of the bacterial protein. These bacterial Fn-binding proteins (FnBPs) mediate adhesion to host tissue and bacterial uptake into non-phagocytic host cells. Recent studies on interactions between the host and bacterial proteins at the residue-specific level and on the mechanism of host cell invasion are providing a much clearer picture of these processes.

Original languageEnglish
Pages (from-to)631-641
Number of pages11
JournalMolecular Microbiology
Volume52
DOIs
Publication statusPublished - May 2004

Keywords

  • PROTECTIVE IMMUNE-RESPONSE
  • NATIVELY UNFOLDED PROTEINS
  • GROUP-A STREPTOCOCCI
  • F1 MODULE PAIR
  • STAPHYLOCOCCUS-AUREUS
  • BINDING-PROTEIN
  • EPITHELIAL-CELLS
  • LIGAND-BINDING
  • ENDOTHELIAL-CELLS
  • IONIC-STRENGTH

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