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 language | English |
---|---|
Pages (from-to) | 111-114 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 290 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - Sep 23 1991 |
Keywords
- Bacterium
- Fibronectin
- Fibronectin fragment
- Receptor
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
- Cell Biology
- Genetics
- Structural Biology