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

• Published in: FEBS letters Vol. 290; no. 1; pp. 111 - 114
• Main Authors: Visai, Livia, Bozzini, Silvia, Petersen, Torben E., Speciale, Livianna, Speziale, Pietro
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 23-09-1991; Elsevier
• Subjects: Bacterial Adhesion; Bacteriology; Bacterium; binding; Binding Sites; Biological and medical sciences; cell surface; Enterotoxins - biosynthesis; Escherichia coli; Escherichia coli - metabolism; Escherichia coli - pathogenicity; Fibronectin; Fibronectin fragment; Fibronectins - chemistry; Fibronectins - metabolism; Fundamental and applied biological sciences. Psychology; Microbiology; Molecular Weight; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains; Peptide Fragments - chemistry; Peptide Fragments - metabolism; Peptide Mapping; Protein Binding; radioactive labelling; Receptor; Staphylococcus - metabolism; Streptococcus - metabolism; Fibronectin fragment; Bacterium; Receptor; Fibronectin; Iodination; Membrane receptor; Radiolabelling; Escherichia coli; Bacteria; Glycoproteins; Binding site; Comparative study; Enterobacteriaceae
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(91)81238-4

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.