@article{mbs:/content/journal/jmm/10.1099/00222615-33-3-165, author = "Eberspacher, B. and Hugo, F. and Pohl, M. and Bhakdi, S.", title = "Functional similarity between the haemolysins of Escherichia coli and Morganella morganii", journal= "Journal of Medical Microbiology", year = "1990", volume = "33", number = "3", pages = "165-170", doi = "https://doi.org/10.1099/00222615-33-3-165", url = "https://www.microbiologyresearch.org/content/journal/jmm/10.1099/00222615-33-3-165", publisher = "Microbiology Society", issn = "1473-5644", type = "Journal Article", abstract = "Surmmary Haemolysin produced by a clinical isolate of Morganella morganii was examined for antigenic relatedness to the haemolysin of Escherichia coli and for similarities in mode of action. The M. morganii haemolysin migrated in SDS-PAGE as a single protein band with a slightly higher molecular weight than that of E. coli haemolysin. Several murine monoclonal antibodies against E. coli haemolysin cross-reacted with the M. morganii haemolysin in Western blots. Diminished haemolysis in the presence of osmotically-stabilising solutes indicated the formation of a pore by M. morganii 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. M. morganii haemolysin was a potent leucocidin, that caused rapid leakage of ATP and death of human polymorphonuclear leucocytes. Under in-vitro conditions M. morganii haemolysin displayed similar leucocidal and haemolytic efficiency. The data demonstrate that M. morganii haemolysin shows functional properties virtually identical with those of E. coli haemolysin.", }