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 journalJournal articleResearchpeer-review

Harvard

Laustsen, AH, Gutiérrez, JM, Rasmussen, AR, Engmark, M, Gravlund, P, Sanders, KL, Lohse, B & Lomonte, B 2015, 'Danger in the reef: Proteome, toxicity, and neutralization of the venom of the olive sea snake, Aipysurus laevis' Toxicon, vol. 107, pp. 187-96. https://doi.org/10.1016/j.toxicon.2015.07.008

APA

Laustsen, A. H., Gutiérrez, J. M., Rasmussen, A. R., Engmark, M., Gravlund, P., Sanders, K. L., ... Lomonte, B. (2015). Danger in the reef: Proteome, toxicity, and neutralization of the venom of the olive sea snake, Aipysurus laevis. Toxicon, 107, 187-96. https://doi.org/10.1016/j.toxicon.2015.07.008

Vancouver

Laustsen AH, Gutiérrez JM, Rasmussen AR, Engmark M, Gravlund P, Sanders KL et al. Danger in the reef: Proteome, toxicity, and neutralization of the venom of the olive sea snake, Aipysurus laevis. Toxicon. 2015 Dec 1;107:187-96. https://doi.org/10.1016/j.toxicon.2015.07.008

Author

Laustsen, Andreas H ; Gutiérrez, José María ; Rasmussen, Arne Redsted ; Engmark, Mikael ; Gravlund, Peter ; Sanders, Kate L ; Lohse, Brian ; Lomonte, Bruno. / Danger in the reef : Proteome, toxicity, and neutralization of the venom of the olive sea snake, Aipysurus laevis. In: Toxicon. 2015 ; Vol. 107. pp. 187-96.

Bibtex

@article{d8a05b26083a4e2da4b7b6134aaf00b6,
title = "Danger in the reef: Proteome, toxicity, and neutralization of the venom of the olive sea snake, Aipysurus laevis",
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.",
keywords = "The Faculty of Health and Medical Sciences",
author = "Laustsen, {Andreas H} and Guti{\'e}rrez, {Jos{\'e} Mar{\'i}a} and Rasmussen, {Arne Redsted} and Mikael Engmark and Peter Gravlund and Sanders, {Kate L} and Brian Lohse and Bruno Lomonte",
note = "Copyright {\circledC} 2015 Elsevier Ltd. All rights reserved.",
year = "2015",
month = "12",
day = "1",
doi = "10.1016/j.toxicon.2015.07.008",
language = "English",
volume = "107",
pages = "187--96",
journal = "Toxicon",
issn = "0041-0101",
publisher = "Pergamon Press",

}

RIS

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 - The 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

VL - 107

SP - 187

EP - 196

JO - Toxicon

JF - Toxicon

SN - 0041-0101

ER -

ID: 161444192