Virulent Escherichia coli strains for chicks bind fibronectin and type II collagen

• Published in: Microbios Vol. 62; no. 251; p. 113
• Main Authors: Gonzalez, E A, Blanco, J, Baloda, S B, Fröman, G, Dho, M, Lafont, J P, Wadström, T
• Format: Journal Article
• Language: English
• Published: England 1990
• Subjects: Animals; Binding Sites; Chickens; Collagen - metabolism; Escherichia coli - metabolism; Escherichia coli - pathogenicity; Escherichia coli Infections - microbiology; Escherichia coli Infections - veterinary; Fibronectins - metabolism; Hemagglutination; Poultry Diseases - microbiology; Surface Properties; Virulence
• ISSN: 0026-2633

125I-fibronectin and 125I-collagen (type II) binding was detected in Escherichia coli strains isolated from chickens and poults. High fibronectin binding-strains also bind the 29 kD aminoterminal fragment of fibronectin. Binding properties in strain CK28 were partially characterized. The highest binding of 125I-fibronectin and 125I-collagen for strain CK28 was obtained with bacteria grown at 33 degrees C. Binding of 125I-fibronectin, its 125I-29 kD fragment, and 125I-collagen, was very rapid, reaching a maximum in 5 min. Binding of 125I-fibronectin and 125I-collagen was considerably inhibited by preincubation of bacteria with unlabelled fibronectin and unlabelled type I collagen respectively, but not inhibited with human immunoglobulin G or bovine serum albumin. Inhibition experiments showed that the reversibility of 125I-fibronectin binding was estimated at approximately 50%, while reversibility for 125I-collagen binding was higher than 90%. Receptors for fibronectin, its 29 kD fragment, and collagen were released from the bacterial surface by treatment at different temperatures, and surface material released at 100 degrees C inhibited binding. There was cross-inhibition for both fibronectin and collagen binding when unlabelled fibronectin and unlabelled collagen were used as inhibitors, suggesting that binding receptors for both proteins may be closely located.