Growth conditions for the expression of fibronectin, collagen type I, vitronectin, and laminin binding to Escherichia coli strain NG7C

The ability of Escherichia coli strains isolated from various human infections to bind fibronectin (Fn), collagen type I (Cn), laminin (Ln), and vitronectin (Vn) was studied. Binding of the proteins was shown to be specific and to be inhibited after protease treatment and heating of bacterial cells at 80 degree C. Binding of Fn, Cn type I, and Ln was not expressed in CFA broth and Voccani's medium with sodium chloride concentration above 0.5%. Fn binding was specifically enhanced for cells grown in CFA broth and Voccani's medium containing CaCl sub(2) (up to 10 mM final concentration), whereas binding of Cn type I was decreased. Growth in liquid medium yielded cells with maximal binding of Fn, Cn type I, Vn, and Ln after 20-22 h of growth. The binding of Fn, Cn type I, and Vn to cells of strain NG7C was inhibited for cells preincubated with antisera raised to the homologous strain; E. coli) NG7C cells seem to have specific binding sites for Fn, Cn type I, Vn.