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Danger in the reef: Proteome, toxicity, and neutralization of the venom of the olive sea snake, Aipysurus laevis.
Toxicon. 2015 Dec 01; 107(Pt B):187-96.T

Abstract

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.

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Authors+Show Affiliations

Laustsen AH
Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Denmark.
Gutiérrez JM
Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica.
Rasmussen AR
Royal Danish Academy of Fine Arts, Schools of Architecture, Design and Conservation, Denmark.
Engmark M
Department of Systems Biology, Technical University of Denmark, Denmark.
Gravlund P
National Aquarium of Denmark (Den Blå Planet), Denmark.
Sanders KL
School of Earth & Environmental Sciences, University of Adelaide, Australia.
Lohse B
Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Denmark.
Lomonte B
Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica. Electronic address: bruno.lomonte@ucr.ac.cr.

MeSH

Amino Acid SequenceAnimalsAntiveninsAustraliaChromatography, High Pressure LiquidCross ReactionsElapid VenomsElapidaeEnzyme-Linked Immunosorbent AssayLethal Dose 50MiceMolecular Sequence DataProteomeReptilian ProteinsSequence Alignment

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

26169672

Citation

Laustsen, Andreas H., et al. "Danger in the Reef: Proteome, Toxicity, and Neutralization of the Venom of the Olive Sea Snake, Aipysurus Laevis." Toxicon : Official Journal of the International Society On Toxinology, vol. 107, no. Pt B, 2015, pp. 187-96.
Laustsen AH, Gutiérrez JM, Rasmussen AR, et al. Danger in the reef: Proteome, toxicity, and neutralization of the venom of the olive sea snake, Aipysurus laevis. Toxicon. 2015;107(Pt B):187-96.
Laustsen, A. H., Gutiérrez, J. M., Rasmussen, A. R., Engmark, M., Gravlund, P., Sanders, K. L., Lohse, B., & Lomonte, B. (2015). Danger in the reef: Proteome, toxicity, and neutralization of the venom of the olive sea snake, Aipysurus laevis. Toxicon : Official Journal of the International Society On Toxinology, 107(Pt B), 187-96. https://doi.org/10.1016/j.toxicon.2015.07.008
Laustsen AH, et al. Danger in the Reef: Proteome, Toxicity, and Neutralization of the Venom of the Olive Sea Snake, Aipysurus Laevis. Toxicon. 2015 Dec 1;107(Pt B):187-96. PubMed PMID: 26169672.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Danger in the reef: 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 R, AU - Engmark,Mikael, AU - Gravlund,Peter, AU - Sanders,Kate L, AU - Lohse,Brian, AU - Lomonte,Bruno, Y1 - 2015/07/11/ PY - 2015/06/11/received PY - 2015/07/03/revised PY - 2015/07/08/accepted PY - 2015/7/15/entrez PY - 2015/7/15/pubmed PY - 2016/10/13/medline KW - Aipysurus laevis KW - Olive sea snake KW - Proteomics KW - Snake venom KW - Toxicity KW - Venomics SP - 187 EP - 96 JF - Toxicon : official journal of the International Society on Toxinology JO - Toxicon VL - 107 IS - Pt B 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. SN - 1879-3150 UR - https://www.unboundmedicine.com/medline/citation/26169672/Danger_in_the_reef:_Proteome_toxicity_and_neutralization_of_the_venom_of_the_olive_sea_snake_Aipysurus_laevis_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0041-0101(15)30017-9 DB - PRIME DP - Unbound Medicine ER -