Pharmacological aspects of Vipera xantina palestinae venom

Tatjana Momic, Franziska T. Arlinghaus, Hadar Arien-Zakay, Jeoshua Katzhendler, Johannes A. Eble, Cezary Marcinkiewicz, Philip Lazarovici*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

25 Scopus citations

Abstract

In Israel, Vipera xantina palestinae (V.x.p.) is the most common venomous snake, accounting for several hundred cases of envenomation in humans and domestic animals every year, with a mortality rate of 0.5 to 2%. In this review we will briefly address the research developments relevant to our present understanding of the structure and function of V.x.p. venom with emphasis on venom disintegrins. Venom proteomics indicated the presence of four families of pharmacologically active compounds: (i) neurotoxins; (ii) hemorrhagins; (iii) angioneurin growth factors; and (iv) different types of integrin inhibitors. Viperistatin, a α1β1selective KTS disintegrin and VP12, a α2β1 selective C-type lectin were discovered. These snake venom proteins represent promising tools for research and development of novel collagen receptor selective drugs. These discoveries are also relevant for future improvement of antivenom therapy towards V.x.p. envenomation.

Original languageAmerican English
Pages (from-to)1420-1432
Number of pages13
JournalToxins
Volume3
Issue number11
DOIs
StatePublished - Nov 2011

Keywords

  • Antivenom
  • Hemorrhagin
  • Integrin inhibitors
  • Neurotoxin
  • Venom
  • Vipera xantina palestinae

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