BINDING OF EXTRACELLULAR-MATRIX PROTEINS TO THE SURFACE OF ANAEROBIC-BACTERIA

The binding of fibronectin, vitronectin, collagen and sialoprotein to 65 anaerobic strains was investigated by means of latex agglutination tests, The binding of fibronectin, collagen and lactoferrin to the sam e strains was also tested by means of I-125-labelled proteins, The str ains were isolated from abdominal infections (55%), from the faeces of healthy subjects (29%) or from the depths of tonsils removed at tonsi llectomy (16%), The binding of fibronectin and collagen to Bacteroides fragilis strains, tested by the lates agglutination assay, was strong er than their binding to other species, The vitronectin binding of the strains was less common, but was always accompanied by fibronectin bi nding, Binding to fibronectin-coated beads was inhibited by pre-incuba tion of the bacterial cells with soluble fibronectin and by heat or pr otease treatment of the bacterial suspension, No inhibition of the bin ding was observed with carbohydrates. None of the 65 strains exhibited any binding to fetuin or asialofetuin; 8% of the strains had a bindin g site for mucin. The binding to mucin-coated beads was inhibited by p reincubation of the cells with mucin, The radiolabelling method indica ted a low binding to I-125-fibronectin, The binding of I-125-collagen- I and I-125-lactoferrin was higher for the anaerobic strains tested.