Haemolysin produced by a clinical isolate of was examined for antigenic relatedness to the haemolysin of and for similarities in mode of action. The haemolysin migrated in SDS-PAGE as a single protein band with a slightly higher molecular weight than that of haemolysin. Several murine monoclonal antibodies against haemolysin cross-reacted with the haemolysin in Western blots. Diminished haemolysis in the presence of osmotically-stabilising solutes indicated the formation of a pore by haemolysin with an effective diameter of 1.5-3 nm. Results from dose-response experiments indicated that a single hit was sufficient for lysis of an erythrocyte. Detergent solubilisation of toxin-treated membranes led to recovery of bound toxin exclusively in monomeric form. haemolysin was a potent leucocidin, that caused rapid leakage of ATP and death of human polymorphonuclear leucocytes. Under in-vitro conditions haemolysin displayed similar leucocidal and haemolytic efficiency. The data demonstrate that haemolysin shows functional properties virtually identical with those of haemolysin.


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