Binding sites in fibronectin for an enterotoxigenic strain of E. coli B342289c

Livia Visai, Silvia Bozzini, Torben E. Petersen, Livianna Speciale, Pietro Speziale

Research output: Contribution to journalArticlepeer-review


The binding of fibronectin and fibronectin fragments to the enterotoxigenic strain E. coli B34289c was studied. E. coli cells bound to two distinct sites of fibronectin, one being the N-terminal domain, which also contains the binding sites for staphylococci and streptococci, and the other located within the central heparin binding region. In addition, the N-terininal and the heparin binding domain mediated the attachment of bacteria in a solid phase binding assay. E. coli cells expressed two classes of receptors, the first, a 17 kDa protein, recognized by the N-terminal fragment and the second, having a mol. mass of 55 kDa, which interacts with the internal heparin binding domain. Bacterial receptors, which bind the N-terminal end of fibronectin, may be structurally related.

Original languageEnglish
Pages (from-to)111-114
Number of pages4
JournalFEBS Letters
Issue number1-2
Publication statusPublished - Sep 23 1991


  • Bacterium
  • Fibronectin
  • Fibronectin fragment
  • Receptor

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Cell Biology
  • Genetics
  • Structural Biology


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