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Pharmacological Aspects of Vipera xantina palestinae Venom

2011; Multidisciplinary Digital Publishing Institute; Volume: 3; Issue: 11 Linguagem: Inglês

10.3390/toxins3111420

2072-6651

Tatjana Momić, Franziska T. Arlinghaus, Hadar Arien‐Zakay, J. Katzhendler, Johannes A. Eble, Cezary Marcinkiewicz, Philip Lazarovici,

Erythrocyte Function and Pathophysiology

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.