Composite venom proteome of Vipera ammodytes and Vipera berus

The composite venom proteome of Vipera ammodytes and Vipera berus represents the total protein content of the venoms from the nose-horned viper and the common European adder, respectively. These proteomes are complex mixtures containing several families of toxic enzymes and non-enzymatic proteins, most notably phospholipases A2 (PLA2), snake venom metalloproteinases (SVMPs), and snake venom serine proteases (SVSPs) [PubMed: 25448275, 28602973]. The biological activity of these venoms includes potent neurotoxicity, particularly from the ammodytoxins in V. ammodytes, and significant hemotoxicity and local tissue damage from both species [PubMed: 15533319, 31137710]. Clinically, these proteomes are the targets of polyvalent antivenom therapy, which employs purified antibodies to neutralize the various toxic components and prevent systemic envenomation [WHO Guidelines]. While the proteome itself is not a single therapeutic target, its characterization is essential for the development of effective treatments and for understanding the pathophysiology of viper bites. Individual components of the proteome are also investigated for their potential as diagnostic biomarkers or as leads for novel drug development in areas such as anticoagulation and pain management.

Other names

Vipera ammodytes venomVipera berus venomEuropean viper venom proteomeNose-horned viper venomCommon adder venom

Neutralization of venom toxins via antibody binding, preventing interaction with physiological targets.