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Biological Activities and Proteomic Profile of the Venom of Vipera ursinii ssp., a very Rare Karst Viper from Croatia

1
University of Zagreb, Centre for Research and Knowledge Transfer in Biotechnology, Rockefellerova 10, HR-10 000 Zagreb, Croatia
2
Jožef Stefan Institute, Department of Molecular and Biomedical Sciences, Jamova cesta 39, SI-1000 Ljubljana, Slovenia
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Toxins 2020, 12(3), 187; https://doi.org/10.3390/toxins12030187
Received: 6 February 2020 / Revised: 10 March 2020 / Accepted: 12 March 2020 / Published: 16 March 2020
(This article belongs to the Section Animal Venoms)
The karst viper (Vipera ursinii ssp.) favours high-mountain dry grasslands in southern and south-eastern Croatia. It is medically less important than other Vipera species, because of its remote habitat and the very small amount of venom that it injects by its relatively short fangs. The scientific literature on Vipera ursinii deals mostly with the morphology, ecology and distribution range of this snake, due to the species’ conservation issues, while the toxinological aspects of its venom have not so far been investigated. Here we report on the composition and biological activity of the Vipera ursinii ssp. venom. Using a proteomics approach, we have identified 25 proteins in the venom that belong to seven protein families: snake venom metalloproteinase, serine protease, secreted phospholipase A2, cysteine-rich secretory protein, snake C-type lectin-like protein, serine protease inhibitor and nerve growth factor. The Vipera ursinii ssp. venom was found to be distinctively insecticidal. Its lethal toxicity towards crickets was more than five times greater than that of Vipera ammodytes ammodytes venom, while the opposite held in mice. Interestingly, the mode of dying after injecting a mouse with Vipera ursinii ssp. venom may suggest the presence of a neurotoxic component. Neurotoxic effects of European vipers have so far been ascribed exclusively to ammodytoxins and ammodytoxin-like basic secreted phospholipases A2. Structural and immunological analyses of the Vipera ursinii ssp. venom, however, confirmed that ammodytoxin-like proteins are not present in this venom. View Full-Text
Keywords: snake venom; Vipera ursinii ssp.; karst viper; toxicity; venomics; insecticide snake venom; Vipera ursinii ssp.; karst viper; toxicity; venomics; insecticide
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MDPI and ACS Style

Lang Balija, M.; Leonardi, A.; Brgles, M.; Sviben, D.; Kurtović, T.; Halassy, B.; Križaj, I. Biological Activities and Proteomic Profile of the Venom of Vipera ursinii ssp., a very Rare Karst Viper from Croatia. Toxins 2020, 12, 187.

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