Cysteine-rich venom proteins from the snakes of Viperinae subfamily - molecular cloning and phylogenetic relationship
| Autor: | Yuri N. Utkin, Victor I. Tsetlin, Anna S. Ramazanova, Rustam H. Ziganshin, Sergey Yu. Filkin, Alexey V. Osipov, Vladislav G. Starkov |
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| Rok vydání: | 2008 |
| Předmět: |
DNA
Complementary Vipera berus Molecular Sequence Data Venom Viper Venoms Toxicology complex mixtures Cysteine-rich secretory protein Viperidae biology.animal Colubridae Animals Crotalinae Amino Acid Sequence Cysteine Cloning Molecular Phylogeny Genetics Viperinae biology Base Sequence Proteins biology.organism_classification Molecular biology biology.protein RNA |
| Zdroj: | Toxicon : official journal of the International Society on Toxinology. 53(1) |
| ISSN: | 0041-0101 |
| Popis: | Cysteine-rich proteins found in animal venoms (CRISP-Vs) are members of a large family of cysteine-rich secretory proteins (CRISPs). CRISP-Vs acting on different ion channels were found in venoms or mRNA (cDNA) encoding CRISP-Vs were cloned from snakes of three main families (Elapidae, Colubridae and Viperidae). About thirty snake CRISP-Vs were sequenced so far, however no complete sequence for CRISP-V from Viperinae subfamily was reported. We have cloned and sequenced for the first time cDNAs encoding CRISP-Vs from Vipera nikolskii and Vipera berus vipers (Viperinae). The deduced mature CRISP-V amino acid sequences consist of 220 amino acid residues. Phylogenetic analysis showed that viper proteins are closely related to those of Crotalinae snakes. The presence of CRISP-V in the V. berus venom was revealed using a combination of gel-filtration chromatography, electrophoresis and MALDI mass spectrometry. The finding of the putative channel blocker in viper venom may indicate its action on prey nervous system. |
| Databáze: | OpenAIRE |
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