Danger in the reef: Proteome, toxicity, and neutralization of the venom of the olive sea snake, Aipysurus laevis
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Danger in the reef : Proteome, toxicity, and neutralization of the venom of the olive sea snake, Aipysurus laevis. / Laustsen, Andreas H; Gutiérrez, José María; Rasmussen, Arne Redsted; Engmark, Mikael; Gravlund, Peter; Sanders, Kate L; Lohse, Brian; Lomonte, Bruno.
In: Toxicon, Vol. 107, 01.12.2015, p. 187-96.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Danger in the reef
T2 - Proteome, toxicity, and neutralization of the venom of the olive sea snake, Aipysurus laevis
AU - Laustsen, Andreas H
AU - Gutiérrez, José María
AU - Rasmussen, Arne Redsted
AU - Engmark, Mikael
AU - Gravlund, Peter
AU - Sanders, Kate L
AU - Lohse, Brian
AU - Lomonte, Bruno
N1 - Copyright © 2015 Elsevier Ltd. All rights reserved.
PY - 2015/12/1
Y1 - 2015/12/1
N2 - Four specimens of the olive sea snake, Aipysurus laevis, were collected off the coast of Western Australia, and the venom proteome was characterized and quantitatively estimated by RP-HPLC, SDS-PAGE, and MALDI-TOF-TOF analyses. A. laevis venom is remarkably simple and consists of phospholipases A2 (71.2%), three-finger toxins (3FTx; 25.3%), cysteine-rich secretory proteins (CRISP; 2.5%), and traces of a complement control module protein (CCM; 0.2%). Using a Toxicity Score, the most lethal components were determined to be short neurotoxins. Whole venom had an intravenous LD50 of 0.07 mg/kg in mice and showed a high phospholipase A2 activity, but no proteinase activity in vitro. Preclinical assessment of neutralization and ELISA immunoprofiling showed that BioCSL Sea Snake Antivenom was effective in cross-neutralizing A. laevis venom with an ED50 of 821 μg venom per mL antivenom, with a binding preference towards short neurotoxins, due to the high degree of conservation between short neurotoxins from A. laevis and Enhydrina schistosa venom. Our results point towards the possibility of developing recombinant antibodies or synthetic inhibitors against A. laevis venom due to its simplicity.
AB - Four specimens of the olive sea snake, Aipysurus laevis, were collected off the coast of Western Australia, and the venom proteome was characterized and quantitatively estimated by RP-HPLC, SDS-PAGE, and MALDI-TOF-TOF analyses. A. laevis venom is remarkably simple and consists of phospholipases A2 (71.2%), three-finger toxins (3FTx; 25.3%), cysteine-rich secretory proteins (CRISP; 2.5%), and traces of a complement control module protein (CCM; 0.2%). Using a Toxicity Score, the most lethal components were determined to be short neurotoxins. Whole venom had an intravenous LD50 of 0.07 mg/kg in mice and showed a high phospholipase A2 activity, but no proteinase activity in vitro. Preclinical assessment of neutralization and ELISA immunoprofiling showed that BioCSL Sea Snake Antivenom was effective in cross-neutralizing A. laevis venom with an ED50 of 821 μg venom per mL antivenom, with a binding preference towards short neurotoxins, due to the high degree of conservation between short neurotoxins from A. laevis and Enhydrina schistosa venom. Our results point towards the possibility of developing recombinant antibodies or synthetic inhibitors against A. laevis venom due to its simplicity.
KW - Faculty of Health and Medical Sciences
U2 - 10.1016/j.toxicon.2015.07.008
DO - 10.1016/j.toxicon.2015.07.008
M3 - Journal article
C2 - 26169672
VL - 107
SP - 187
EP - 196
JO - Toxicon
JF - Toxicon
SN - 0041-0101
ER -
ID: 161444192