[No authors listed]
A proteome-wide mapping of interactions between hepatitis C virus (HCV) and human proteins was performed to provide a comprehensive view of the cellular infection. A total of 314 protein-protein interactions between HCV and human proteins was identified by yeast two-hybrid and 170 by literature mining. Integration of this data set into a reconstructed human interactome showed that cellular proteins interacting with HCV are enriched in highly central and interconnected proteins. A global analysis on the basis of functional annotation highlighted the enrichment of cellular pathways targeted by HCV. A network of proteins associated with frequent clinical disorders of chronically infected patients was constructed by connecting the insulin, and TGFbeta pathways with cellular proteins targeted by HCV. CORE protein appeared as a major perturbator of this network. Focal adhesion was identified as a new function affected by HCV, mainly by NS3 and NS5A proteins.
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HCVgp1, PSME3, CALCOCO2, BCKDK, FBLN5, FRS3, PPP1R13L, DDX3X, FBLN2, EFEMP1, FTH1, GBP2, BIN1, GOLGA2, GPS2, SETD2, UBQLN1, HIVEP2, NR4A1, HOXD8, ITGAL, JUN, KPNA1, NAP1L1, NAP1L2, TXNDC11, RNF31, MOB1A, EIF4ENIF1, PSMB9, TRIM27, VPS52, SMURF2, CEP85, STAT3, VIM, VWF, LTBP4, SORBS2, ACTN1, SLIT2, RASAL2, MAGED1
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