Binding sites in fibronectin for an enterotoxigenic strain of E. coli B342289c.
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.
Visai
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L
Department of Biochemistry, University of Pavia, Italy.
Bozzini
S
S
Petersen
T E
TE
Speciale
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L
Speziale
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P
D001422:Bacterial Adhesion; D001665:Binding Sites; D004768:Enterotoxins / Q000096:biosynthesis*; D004926:Escherichia coli / Q000378:metabolism* / Q000472:pathogenicity; D005353:Fibronectins / Q000737:chemistry / Q000378:metabolism*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D010449:Peptide Mapping; D011485:Protein Binding; D013210:Staphylococcus / Q000378:metabolism; D013291:Streptococcus / Q000378:metabolism
D004768:Enterotoxins; D005353:Fibronectins; D010446:Peptide Fragments