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

Abstract

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
Volume290
Issue number1-2
DOIs
Publication statusPublished - Sep 23 1991

Keywords

  • Bacterium
  • Fibronectin
  • Fibronectin fragment
  • Receptor

ASJC Scopus subject areas

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

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