Role of Hepatitis C virus core protein in viral-induced mitochondrial dysfunction

identification of differentially expressed genes in l02 human hepatocyte induced by hepatitis c virus core protein

Overexpression of Full-Length Core Protein of Hepatitis C Virus by Escherichia coli Cultivated in Stirred Tank Fermentor

The mature core protein of the Hepatitis C virus (HCVC173) carrying pelB as a signal peptide (PelB::core) was overexpressed in Escherichia coli as 18% and 23.3% of the host’s total protein, in flask and fermentor cultivation, respectively. A final specific yield of 25 ± 1 mg HCVC173/g dry cell weight and an overallproductivity of 51±1 mg HCVC173/l/h were obtained in the stirred-tank ferme...

Hepatitis C Virus-Induced Mitochondrial Dysfunctions

Chronic hepatitis C is characterized by metabolic disorders and a microenvironment in the liver dominated by oxidative stress, inflammation and regeneration processes that lead in the long term to hepatocellular carcinoma. Many lines of evidence suggest that mitochondrial dysfunctions, including modification of metabolic fluxes, generation and elimination of oxidative stress, Ca2+ signaling and...

CpG Motif as an Adjuvant in Immunization of a Recombinant Plasmid Encoding Hepatitis C Virus Core Protein

Role of cleavage at the core-E1 junction of hepatitis C virus polyprotein in viral morphogenesis

In hepatitis C virus (HCV) polyprotein sequence, core protein terminates with E1 envelope signal peptide. Cleavage by signal peptidase (SP) separates E1 from the complete form of core protein, anchored in the endoplasmic reticulum (ER) membrane by the signal peptide. Subsequent cleavage of the signal peptide by signal-peptide peptidase (SPP) releases the mature form of core protein, which prefe...