The Journal of Medical Microbiology, Vol 45, Issue 5 338-343, Copyright © 1996 by Society for General Microbiology
Binding of extracellular matrix proteins to the surface of anaerobic bacteria
I. Szoke, C. Pascu, E. Nagy, A. Ljung and T. Wadstrom
Department of Clinical Microbiology, Albert Szent-Gyorgyi Medical University, Szeged, Hungary.
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 same strains
was also tested by means of 125I-labelled proteins. The strains were
isolated from abdominal infections (55%), from the faeces of healthy
subjects (29%) or from the depths of tonsils removed at tonsillectomy
(16%). The binding of fibronectin and collagen to Bacteroides fragilis
strains, tested by the latex agglutination assay, was stronger than their
binding to other species. The vitronectin binding of the strains was less
common, but was always accompanied by fibronectin binding. Binding to
fibronectin-coated beads was inhibited by pre-incubation of the bacterial
cells with soluble fibronectin and by heat or protease treatment of the
bacterial suspension. No inhibition of the binding was observed with
carbohydrates. None of the 65 strains exhibited any binding to fetuin or
asialofetuin; 8% of the strains had a binding site for mucin. The binding
to mucin-coated beads was inhibited by pre-incubation of the cells with
mucin. The radiolabelling method indicated a low binding to
125I-fibronectin. The binding of 125I-collagen-I and 125I-lactoferrin was
higher for the anaerobic strains tested.
