| Literature DB >> 1915860 |
L Visai1, S Bozzini, T E Petersen, L Speciale, P Speziale.
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-terminal 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.Entities:
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Year: 1991 PMID: 1915860 DOI: 10.1016/0014-5793(91)81238-4
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124