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Vipera ammodytes and Vipera berus venom toxins are complex mixtures of proteins and peptides that serve as the primary pathological agents in envenomation by the nose-horned viper and the common European adder [1][2]. These venoms contain a variety of enzymes and non-enzymatic proteins, most notably phospholipases A2 (PLA2), snake venom metalloproteinases (SVMPs), snake venom serine proteases (SVSPs), and C-type lectin-like proteins [3][4]. Biologically, these toxins function to immobilize and digest prey by disrupting the nervous system, damaging vascular integrity, and interfering with the blood coagulation cascade [1][5]. In clinical settings, they are the direct targets of antivenom therapies, which utilize purified antibodies or antibody fragments to neutralize the toxins' activity and prevent systemic damage [2][6]. Beyond their role in pathology, individual components like disintegrins are studied for their potential as therapeutic leads in treating cardiovascular diseases and cancer due to their ability to inhibit platelet aggregation and cell adhesion [4][7].
Neutralization of venom toxins through passive immunotherapy using specific immunoglobulin (IgG) or Fab fragments [2][6].
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