Proteome and Peptidome of Vipera berus berus Venom

Abstract

Snake venom is a rich source of peptides and proteins with a wide range of actions Many of the venom components are currently being tested for their usefulness in the treatmen of many diseases ranging from neurological and cardiovascular to cancer. It is also important t constantly search for new proteins and peptides with properties not yet described. The venom o Vipera berus berus has hemolytic, proteolytic and cytotoxic properties, but its exact composition an the factors responsible for these properties are not known. Therefore, an attempt was made to identif proteins and peptides derived from this species venom by using high resolution two-dimensiona electrophoresis and MALDI ToF/ToF mass spectrometry. A total of 11 protein classes have bee identified mainly proteases but also L-Amino acid oxidases, C-Type lectin like proteins, cysteine-ric venom proteins and phospholipases A2 and 4 peptides of molecular weight less than 1500 Da. Most o the identified proteins are responsible for the highly hemotoxic properties of the venom. Presence o venom phospholipases A2 and L-Amino acid oxidases cause moderate neuro-, myo-and cytotoxicity All successfully identified peptides belong to the bradykinin-potentiating peptides family. The mas spectrometry data are available via ProteomeXchange with identifier PXD004958.