Lotan A, Fishman L, Zlotkin E
Department of Cell and Animal Biology, Life Sciences Institute, Hebrew University of Jerusalem, Israel.
J Exp Zool. 1996 Aug 15;275(6):444-51. doi: 10.1002/(SICI)1097-010X(19960815)275:6<444::AID-JEZ6>3.0.CO;2-O.
With the aid of dialysis and ion exchange chromatography, a new polypeptide toxin was purified from the tentacles of the Mediterranean jellyfish Rhopilema nomadica. The amino acid sequence of the N-terminal segment of the new toxin revealed that it is a phospholipase A2 (PhA2) toxin closely resembling those previously isolated from reptile and hymenopterous venoms. The occurrence of a PhA2 toxin in the jellyfish tentacles may explain both their local (dermanecrotic) and systemic (cardiac-respiratory) effects upon human envenomation. We used an antibody raised against the above toxin as a probe to explore, for the first time, the site of toxin allocation in cnidarian nematocysts and its morphological route of delivery. Our immunocytochemical approach revealed that the toxin is stored on the outer ("cytoplasmic") surface of the inverted tubule folded in the capsule of the resting nematocyst. During discharge the toxin is translocated to the internal surface surrounding the lumen of the everting tubule, and its delivery via extended spirally arrayed barbs is apparently propelled by the high hydrostatic pressure of the capsule. This is a unique example where subcellular translocation and transfer of a polypetide is driven by mechanical forces.
