Comparative study of extracellular matrix protein binding to Aeromonas hydrophila isolated from diseased fish and human infection.

Binding of 125I-labelled types I and IV collagen, fibronectin and laminin to Aeromonas cells is a common characteristic among Aeromonas strains isolated from diseased fish and human infections. The proportion of Aeromonas strains which bind to the various proteins were significantly greater for A. hydrophila than for A. sobria or A. caviae. The binding property was specific since it was inhibited by unlabelled homologous proteins. Bacterial cells incubated with proteolytic enzymes lose the ability of binding to 125I-labelled collagen type I and IV, fibronectin, laminin and vitronectin. A bacterial cell surface protein extract, containing active receptors competes with intact cells for 125I-extracellular matrix protein binding. Culture conditions greatly influence the expression of A. hydrophila cell surface binding structures for extracellular matrix proteins. The presence of calcium ions in the growth medium seems to be an important enhancer of the expression of extracellular matrix protein cell surface receptors.