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PMID:18243272
| Citation |
Brinkman, D and Burnell, J (2008) Partial purification of cytolytic venom proteins from the box jellyfish, Chironex fleckeri. Toxicon 51:853-63 |
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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 approximately 370 and 145kDa, and one minor cytolysin ( approximately 70kDa) were isolated. SDS-PAGE and western blot protein profiles revealed that the 370kDa haemolysin is composed of CfTX-1 and CfTX-2 subunits ( approximately 43 and 45kDa, respectively); the most abundant proteins found in C. fleckeri nematocyst extracts. The 145kDa haemolysin predominately contains two other major proteins ( approximately 39 and 41kDa), 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 ( approximately 6-7min) 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. |
| Links |
PubMed Online version:10.1016/j.toxicon.2007.12.017 |
| Keywords |
Agar/chemistry; Amino Acid Sequence; Animals; Blotting, Western; Chromatography, Gel; Chromatography, Ion Exchange; Cnidarian Venoms/chemistry; Cnidarian Venoms/metabolism; Cubozoa/metabolism; Cytotoxins/chemistry; Cytotoxins/isolation & purification; Electrophoresis, Polyacrylamide Gel; Hemolysin Proteins/chemistry; Hemolysin Proteins/isolation & purification; Hemolysis; Proteins/chemistry; Proteomics |
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