Hemolysins: pore-forming proteins in invertebrates.
Invertebrates possess lytic molecules which lyse vertebrate erythrocytes. In all the species studied so far, hemolytic activity depends on proteins which possess a wide range of reactivity. It is generally calcium-dependent and heat-labile, although calcium-independent and heat-stable hemolysins have also been detected. The molecules interact with sugars or lipids which could represent the membrane receptors by which circular lesions on target membranes are produced. On the basis of some analogies with vertebrate lytic molecules it is conceivable that the hemolysins evolved from a common ancestral gene which also led to vertebrate pore-forming proteins.
Canicatti
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Department of Biology, University of Lecce, Italy.
D000818:Animals; D002118:Calcium / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000473:pathology; D006460:Hemolysin Proteins / Q000378:metabolism / Q000494:pharmacology / Q000502:physiology*; D006461:Hemolysis; D007448:Invertebrates / Q000276:immunology / Q000378:metabolism*; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D011506:Proteins / Q000378:metabolism / Q000494:pharmacology / Q000502:physiology*; D011817:Rabbits
D006460:Hemolysin Proteins; D011506:Proteins; D008274:Magnesium; D002118:Calcium