Affordable Access

Access to the full text

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

Authors
  • Lang Balija, Maja1
  • Leonardi, Adrijana
  • Brgles, Marija1
  • Sviben, Dora1
  • Kurtović, Tihana1
  • Halassy, Beata1
  • Križaj, Igor
  • 1 (T.K.)
Type
Published Article
Journal
Toxins
Publisher
MDPI AG
Publication Date
Mar 16, 2020
Volume
12
Issue
3
Identifiers
DOI: 10.3390/toxins12030187
PMID: 32188060
PMCID: PMC7150868
Source
PubMed Central
Keywords
License
Green

Abstract

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.

Report this publication

Statistics

Seen <100 times