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Getting stoned: characterisation of the coagulotoxic and neurotoxic effects of reef stonefish (Synanceia verrucosa) venom
Harris, R.J.; Youngman, N.J.; Chan, W.; Bosmans, F.; Cheney, K.L.; Fry, B.G. (2021). Getting stoned: characterisation of the coagulotoxic and neurotoxic effects of reef stonefish (Synanceia verrucosa) venom. Toxicol. Lett. 346: 16-22. https://dx.doi.org/10.1016/j.toxlet.2021.04.007
In: Toxicology letters. Elsevier Biomedical Press: Tokyo; Oxford; New York; Lausanne; Shannon; Amsterdam. ISSN 0378-4274; e-ISSN 1879-3169
Peer reviewed article  

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Trefwoorden
    Synanceia verrucosa Bloch & Schneider, 1801 [WoRMS]
    Marien/Kust
Author keywords
    Stonefish; Synanceia verrucosa; Venom; Lyophilised; Fresh; Neurotoxicity; Coagulotoxicity

Auteurs  Top 
  • Harris, R.J.
  • Youngman, N.J.
  • Chan, W.
  • Bosmans, F.
  • Cheney, K.L.
  • Fry, B.G.

Abstract
    The reef stonefish (Synanceia verrucosa) is a venomous fish which causes excruciatingly painful envenomations. While some research on the pathophysiology and functions of the venom have been conducted, there are still some gaps in the understanding of the venom effects due to the extreme lability of fish venom toxins and the lack of available testing platforms. Here we set out to assess new functions of the venom whilst also attempting to address some unclear pathophysiological effects from previous literature. Utilising a biolayer interferometry assay, our results highlight that the venom binds to the orthosteric site of the α-1 nicotinic acetylcholine receptor as well as the domain IV of voltage-gated Ca2+ (CaV1.2) channel mimotopes. Both these results add some clarity to the previously ambiguous literature. We further assessed the coagulotoxic effects of the venom using thromboelastography and Stago STA-R Max coagulation analyser assays. We reveal that the venom produced anticoagulant activity and significantly delayed time until clot formation of recalcified human plasma which is likely through the degradation of phospholipids. There was a difference between fresh and lyophilised venom activity toward the nicotinic acetylcholine receptor mimotopes and coagulation assays, whilst no difference was observed in the activity toward the domain IV of CaV1.2 mimotopes. This research adds further insights into the neglected area of fish venom whilst also highlighting the extreme labile nature of fish venom toxins.

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