Getting stoned: Characterisation of the coagulotoxic and neurotoxic effects of reef stonefish (Synanceia verrucosa) venom
| Autor: | Richard J. Harris, Weili Chan, Frank Bosmans, Nicholas J. Youngman, Bryan G. Fry, Karen L. Cheney |
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| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Delayed time Venom Receptors Nicotinic Pharmacology Toxicology complex mixtures Plasma 03 medical and health sciences 0302 clinical medicine Protein Domains Fish Venoms medicine Animals Humans Synanceia verrucosa Envenomation Blood Coagulation Binding Sites biology Fishes Neurotoxicity General Medicine Venomous fish biology.organism_classification Clot formation medicine.disease Thrombelastography Nicotinic acetylcholine receptor 030104 developmental biology 030217 neurology & neurosurgery |
| Zdroj: | Toxicology Letters. 346:16-22 |
| ISSN: | 0378-4274 |
| DOI: | 10.1016/j.toxlet.2021.04.007 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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