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.
Highlights
Snake bite is a serious medical problem, in Asia, Africa and in the Middle East, including Israel
Neurotoxic phospholipase A2 (PLA2); 2% myotoxic PLA2; (ii) hemorrhagins: 65% zinc metalloproteinase, 9% different serine proteinases; (iii) angioneurin growth factors: about 2% of the venom is composed of snake homologues of vascular endothelial growth factor (VEGF) [18] and nerve growth factor (NGF) known to induce angiogenesis in blood capillaries, neurite outgrowth, as well as vascular permeability [19,20]
Disintegrins can be divided into three groups according to their integrin selectivity and presence of specific, recognition motifs. This classification includes RGD-disintegrins, MLD-disintegrins, and KTS-disintegrins [48,49]
Summary
Snake bite is a serious medical problem, in Asia, Africa and in the Middle East, including Israel. The above clinical local and systemic symptoms of V.x.p. envenomation are the consequence of the pharmacological activity of these enzymatic and non-enzymatic venom proteins They cause increased capillary permeability, endothelial damage, platelet aggregation and dysfunction, thromboplastin and thrombin inhibition, neutrophilia, leucocytosis, thrombocytopenia, increase fibrinolysis and hypofibrinogenemia, release of histamines, kinins, and different presynaptic neurotoxic effects [6,7]. These pathological syndromes are induced by the large variety of proteins found in V.x.p. venom and by additive and synergistic interactions between them. These considerations are relevant for future improvement of antivenom therapy towards V.x.p. envenomation
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