Brinkman, Diane, and Burnell, James (2008) Partial purification of cytolytic venom proteins from the box jellyfish, Chironex fleckeri. Toxicon, 51 (5). pp. 853-863.

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Abstract

Venom proteins from the nematocysts of Chironex fleckeri were fractionated by size-exclusion and cation-exchange chromatography. Using sheep erythrocyte haemolysis as an indicator of cytolytic activity, two major cytolysins, with native molecular masses of 370 and 145 kDa, and one minor cytolysin (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 (43 and 45 kDa, respectively); the most abundant proteins found in C. fleckeri nematocyst extracts. The 145 kDa haemolysin predominately contains two other major proteins (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 lag phase (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.

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