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Paper Title :
Structural Evaluation of Purinergic Receptor (P2x4) Receptor Interaction With HCV Envelop Protein E1: A Potential Target For Drug

Author :Madiha Khalid, Sobia Manzoor

Article Citation :Madiha Khalid ,Sobia Manzoor , (2016 ) " Structural Evaluation of Purinergic Receptor (P2x4) Receptor Interaction With HCV Envelop Protein E1: A Potential Target For Drug " , International Journal of Advances in Science, Engineering and Technology(IJASEAT) , pp. 58-62, Volume-4,Issue-3, Spl. Iss-2

Abstract : Hepatitis C virus (HCV) is a foremost public health issue worldwide being major cause of liver associated disorders e.g., chronic hepatitis, cirrhosis, fibrosis and hepatocellular carcinoma. HCV structural envelop protein E1 plays the primary role in viral entry. P2X receptors are non-selective ligand-gated ion channels that are activated by extracellular ATP. Among all P2X receptors expressed in the liver; P2X4 and P2X7 are the most widely expressed proteins. In this study, Immunostaining was used to characterize the P2X4 receptor in Huh7 cell line. Functional activity of P2X receptors was confirmed by using Flex station III by measuring the Ca2+ in the presence of agonist (ATP). Human P2X4 receptor was modeled from zebra fish model (by homology modeling) using molecular operating environment (MOE) software. Proteinprotein interactions (PPIs) of P2X4 and E1 were studied using High Ambiguity Driven biomolecular docking (HADDOCK) webserver. Our results showed HCV envelop E1 protein interactions with P2X4R at few residues. In our findings we confirmed presence and functional activation of P2X4 receptor in Huh7 cell line. Furthermore human P2X4 receptor plausible interactions with HCV E1 protein may be speculative of viral entry and can be exploited for drug targeting in future experiments. Keywords- Hepatitis C virus, Purinergic receptor, Docking, Adenosine triphosphate, Hepatocellular carcinoma

Type : Research paper

Published : Volume-4,Issue-3, Spl. Iss-2


DOIONLINE NO - IJASEAT-IRAJ-DOIONLINE-5678   View Here

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