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Possible involvement of red cell membrane proteins in the hemolytic action of Portuguese Man-of-War toxin

1979; Elsevier BV; Volume: 91; Issue: 3 Linguagem: Inglês

10.1016/0006-291x(79)91945-4

1090-2104

David C. Lin, David A. Hessinger,

Yersinia bacterium, plague, ectoparasites research

Glycophorin and the fragments isolated from trypsinizing intact rat, dog, sheep and human red blood cells (rbc's) neutralize the hemolytic action of the Portuguese Man-of-War venom. This action can be blocked by rabbit antisheep hemolysin and phytohemagglutinin, a lectin which preferentially binds to glycophorin. Concanavalin A, which binds to band-3 protein of rbc membranes, does not block the neutralizing action of rbc tryptic fragments or glycophorin. The concentrations of rat, dog, human and sheep glycophorin which half neutralize venom induced hemolysis are inversely and linearly proportional to the hemolytic sensitivities of these rbc's to the venom. These data implicate glycophorin as a possible binding site for the hemolytic component of the Portuguese Man-of-War venom.