Partial purification of cytolytic venom proteins from the box jellyfish, Chironex fleckeri

摘要

Venom proteins from the nematocysts of cytolytic activity, two major cytolysins, with chromatography. Using sheep erythrocyte haemolysis as an indicator native molecular masses of similar to 370 and 145 kDa, and one minor cytolysin (similar to 70 kDa) were isolated. SDS-PAGE and western blot protein profiles revealed that the 370 kDa haemolysin is composed of CfTX-1 and CfTX-2 subunits (similar to 43 and 45 kDa,. found in C. fleckeri nematocyst extracts. The 145 kDa haemolysin predominately respectively); the most abundant proteins sh contains two other major proteins (similar to 39 and 41 kDa), which are not antigenic towards commercially available box jellyfish antivenom or rabbit polyclonal antibodies raised against whole C fleckeri nematocyst extracts or CfTX-1 and -2. The kinetics of CfTX-1 and -2 haemolytic activities are temperature dependent and characterised by a pre-lytic tag phase (similar to 6-7 min) prior to initiation of haemolysis. Significant amino acid sequence homology between the CfTX proteins and other box jellyfish toxins suggest that CfTX-1 and -2 may also be lethal and dermonecrotic. Therefore, further in vivo and in vitro studies are required to investigate the potential roles of CfTX-1 and -2 in the lethal effects of C fleckeri venom. Crown Copyright (c) 2008 Published by Elsevier Ltd. All rights reserved.