NDLI: Crystal structure of a dimeric Ser49 PLA<sub>2</sub>-like myotoxic component of the Vipera ammodytes meridionalis venomics reveals determinants of myotoxicity and membrane damaging activity

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Molecular BioSystems Vol - 8 Issue - 4

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Molecular BioSystems Vol - 8 Issue - 2

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Crystal structure of a dimeric Ser49 PLA₂-like myotoxic component of the Vipera ammodytes meridionalis venomics reveals determinants of myotoxicity and membrane damaging activity

Content Provider	Royal Society of Chemistry (RSC)
Author	Arni, Raghuvir K. Coronado, Monika Betzel, Christian Duhalov, Deyan Buck, Friedrich Oberthür, Dominik Georgieva, Dessislava
Copyright Year	2012
Abstract	Myotoxicity and membrane damage play a central role in the life-threatening effects of the viper envenomation. Myotoxins are an important part of the viper venomics. A Ser49 PLA2-like myotoxin from the venom of Vipera ammodytes meridionalis, the most venomous snake in Europe, was crystallized and its three-dimensional structure determined. The toxin is devoid of phospholipolytic activity. The structure demonstrates a formation of dimers. In the dimers functionally important peptide segments, located on the protein surface, point in the same direction which can strengthen the pharmacological effect. This supports the hypothesis about the physiological importance of the toxin oligomerization for the myotoxicity and membrane damage. The crystallographic model revealed that the structural determinants of myotoxicity (a positively charged C-terminal region and a hydrophobic knuckle) are fully exposed on the protein surface and accessible for interactions with target membranes. Distortion of the catalytic site region explains the absence of enzymatic activity. The structure reveals anion-binding sites which can be considered as possible sites of interactions of the toxin with a negatively charged membrane surface. The high structural similarity of the Ser49 myotoxin and Asp49 PLA2 from the same venom suggests an evolutionary relationship: probably, the Ser49 myotoxin is a product of evolution of the catalytically active phospholipase A2. The first toxin lost the enzymatic activity which is not necessary for the myotoxicity but preserved the cytotoxicity and membrane damaging activity as important components of the venom toxicity.
Starting Page	1405
Ending Page	1411
Page Count	7
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	8
Issue Number	5
Journal	Molecular BioSystems
DOI	10.1039/c2mb05490f
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Fully Exposed Snake Europe Cytotoxicity Viperidae Hydrophobe Protein C-terminus Phospholipase Myotoxin Venom Vipera ammodytes meridionalis Peptide
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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