Project description:The nose-horned viper, its nominotypical subspecies Vipera ammodytes ammodytes (Vaa) in particular is, medically, the most relevant snake in Europe. The local and systemic clinical manifestations of poisoning by the venom of this snake are the result of the pathophysiological effects inflicted by enzymatic and non-enzymatic venom components acting, most prominently, on blood, cardiovascular and nerve systems. This venom comprises the most complex mixture of pharmacologically active proteins and peptides of all European snakes. To help improve the current antivenom therapy towards higher specificity and efficiency, and to assist drug discovery, we have constructed, by combining transcriptomic and proteomic analyses, the most comprehensive library yet of the Vaa venom proteins and peptides. At the protein level, 57 venom proteins belonging to 16 different protein families have been identified and, with SVSPs, sPLA2s, snaclecs and SVMPs, comprise about 80% of all venom proteins.

2019-05-06 | PXD012752 | Pride

Proteome and peptidome of Vipera berus berus venom

Project description:Snake venom is a rich source of peptides and proteins with a wide range of actions. Many of the components of the venom are currently being tested for their usefulness in the treatment of many diseases ranging from neurological and cardiovascular to cancer. It is also important to constantly search for new proteins and peptides with properties not yet described. The venom of Vipera berus berus has hemolytic, proteolytic and cytotoxic properties, but its exact composition and the factors responsible for these properties are not known. Therefore, an attempt was made to identify proteins and peptides derived from this species venom by using high resolution two-dimensional electrophoresis and MALDI ToF/ToF mass spectrometry. A total of 11 protein classes have been identified mainly proteases but also L-amino acid oxidases, C-type lectin like proteins, cysteine-rich venom proteins and phospholipases A2 and 5 peptides of molecular weight less than 1500 Da. Most of the identified proteins are responsible for the highly hemotoxic properties of the venom. Presence of venom phospholipases A2 and L- amino acid oxidases cause moderate neuro-, myo- and cytotoxicity. All successfully identified peptides belong to the bradikinin-potentiating peptides family.

2016-12-12 | PXD004958 | Pride

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