Identification, cloning and sequencing of the two major venom proteins from box jellyfish, Chironex fleckeri
Brinkman, Diane, and Burnell, James (2007) Identification, cloning and sequencing of the two major venom proteins from box jellyfish, Chironex fleckeri. Toxicon, 50 (6). pp. 850-860.
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Two of the most abundant proteins found in the nematocysts of the box jellyfish Chironex fleckeri have been identified as C. fleckeri toxin-1 (CfTX-1) and toxin-2 (CfTX-2). The molecular masses of CfTX-1 and CfTX-2, as determined by SDS-PAGE, are approximately 43 and 45 kDa, respectively, and both proteins are strongly antigenic to commercially available box jellyfish antivenom and rabbit polyclonal antibodies raised against C. fleckeri nematocyst extracts. The amino acid sequences of mature CfTX-1 and CfTX-2 (436 and 445 residues, respectively) share significant homology with three known proteins: CqTX-A from Chiropsalmus quadrigatus, CrTXs from Carybdea rastoni and CaTX-A from Carybdea alata, all of which are lethal, haemolytic box jellyfish toxins. Multiple sequence alignment of the five jellyfish proteins has identified several short, but highly conserved regions of amino acids that coincide with a predicted transmembrane spanning region, referred to as TSR1, which may be involved in a pore-forming mechanism of action. Furthermore, remote protein homology predictions for CfTX-2 and CaTX-A suggest weak structural similarities to pore-forming insecticidal δ-endotoxins Cry1Aa, Cry3Bb and Cry3A.
|Item Type:||Article (Refereed Research - C1)|
|Keywords:||jellyfish; Chironex; venom proteins|
|Date Deposited:||25 Sep 2009 04:01|
|FoR Codes:||06 BIOLOGICAL SCIENCES > 0601 Biochemistry and Cell Biology > 060199 Biochemistry and Cell Biology not elsewhere classified @ 100%|
|SEO Codes:||96 ENVIRONMENT > 9604 Control of Pests, Diseases and Exotic Species > 960407 Control of Pests, Diseases and Exotic Species in Marine Environments @ 100%|
|Citation Count from Web of Science||