Echis pyramidum
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA1313283 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Echis pyramidum Venom gland transcriptome
| PRJNA253191 | ENA
Project description:we used a combination of bottom-up (BU) and top-down (TD) proteomics approaches to identify and characterize venom protein compositions of Echis carinatus sochureki (ECS) from three different Iranian populations.
2021-01-29 | PXD021183 | Pride
Project description:In order to study the proteome of Echis carinatus carinatus venom of Indian origin, crude venom was fractionated on a Shodex KW-803 gel filtration column coupled to Dionex Ultimate 3000 UHPLC system. The resulting peaks were pooled and subjected to in-solution trypsin digestion and subsequent tandem mass spectrometry analysis. The raw data were then analysed using PEAKS 8.5 software to finally decipher the complex venom proteome.
2017-12-15 | PXD007980 | Pride
Project description:In order to study the proteome of Echis carinatus venom from Sri Lanka (SL ECV), crude SL ECV was subjected to 12.5% SDS-PAGE analysis. The resulting SDS-PAGE bands were subjected to in-gel trypsin digestion and subsequent tandem mass spectrometry analysis. The raw data were then analysed using PEAKS 8.5 software to finally decipher the complex venom proteome.
2020-06-12 | PXD018130 | Pride
Project description:Hydrophilic interaction liquid chromatography coupled with LC- MS/MS was used to analyze the crude venom extracts of Echis ocellatus (Carpet viper) and Bitis arietans (Puff adder). The gel-free proteomic analysis of the crude venom extracts from E. ocellatus and B. arietans yielded the identification of 86 and 80 proteins, respectively. Seventy- nine proteins were common between the two snake species with a 90.8% similarity. The identified proteins belong to 12 protein families where serine proteases (22.31%) and metalloproteinases (21.06%) were the dominant proteins in the venom of B. arietans. Metalloproteinases (34.84%), phospholipase A 2 s (25.69%) and serine proteases (17.25%) represents the major toxins in the E. ocellatus venom. This study provides some valuable insights into the toxin families to be neutralized in case of envenomation.
2021-03-11 | PXD024638 | Pride
Project description:Phospholipase A(2) (PLA(2)), a common toxic component of snake venom, has been implicated in various pharmacological effects. Ecarpholin S, isolated from the venom of the snake Echis carinatus sochureki, is a phospholipase A(2) (PLA(2)) belonging to the Ser(49)-PLA(2) subgroup. It has been characterized as having low enzymatic but potent myotoxic activities. The crystal structures of native ecarpholin S and its complexes with lauric acid, and its inhibitor suramin, were elucidated. This is the first report of the structure of a member of the Ser(49)-PLA(2) subgroup. We also examined interactions of ecarpholin S with phosphatidylglycerol and lauric acid, using surface plasmon resonance, and of suramin with isothermal titration calorimetry. Most Ca(2+)-dependent PLA(2) enzymes have Asp in position 49, which plays a crucial role in Ca(2+) binding. The three-dimensional structure of ecarpholin S reveals a unique conformation of the Ca(2+)-binding loop that is not favorable for Ca(2+) coordination. Furthermore, the endogenously bound fatty acid (lauric acid) in the hydrophobic channel may also interrupt the catalytic cycle. These two observations may account for the low enzymatic activity of ecarpholin S, despite full retention of the catalytic machinery. These observations may also be applicable to other non-Asp(49)-PLA(2) enzymes. The interaction of suramin in its complex with ecarpholin S is quite different from that reported for the Lys(49)-PLA(2)/suramin complex(,) where the interfacial recognition face (i-face), C-terminal region, and N-terminal region of ecarpholin S play important roles. This study provides significant structural and functional insights into the myotoxic activity of ecarpholin S and, in general, of non-Asp(49)-PLA(2) enzymes.
| S-EPMC2547436 | biostudies-literature