The first hydrophobic domain of the hepatitis C virus E1 protein is important for interaction with the capsid protein
- 1 December 2002
- journal article
- Published by Microbiology Society in Journal of General Virology
- Vol. 83 (12) , 3085-3092
- https://doi.org/10.1099/0022-1317-83-12-3085
Abstract
The interaction between the hepatitis C virus capsid protein and the envelope protein E1 has been demonstrated previously in vivo. To determine the binding region of the E1 protein with the capsid protein, this interaction was characterized in vitro. This study shows that the interaction between these proteins should occur in the endoplasmic reticulum membrane rather than in the cytosol and that the first hydrophobic domain of the E1 protein (aa 261–291) is important for the interaction with the capsid protein.Keywords
This publication has 38 references indexed in Scilit:
- Analysis of the C-Terminal Membrane Anchor Domains of Hepatitis C Virus Glycoproteins E1 and E2: toward a Topological ModelJournal of Virology, 2002
- Activation of p53 Tumor Suppressor by Hepatitis C Virus Core ProteinVirology, 1999
- The core protein of hepatitis C virus induces hepatocellular carcinoma in transgenic miceNature Medicine, 1998
- Hepatitis C Virus Core Protein Interacts with Heterogeneous Nuclear Ribonucleoprotein KJournal of Biological Chemistry, 1998
- Homotypic Interaction and Multimerization of Hepatitis C Virus Core ProteinVirology, 1996
- Differential Subcellular Localization of Hepatitis C Virus Core Gene ProductsVirology, 1995
- Sequence analysis of the core gene of 14 hepatitis C virus genotypes.Proceedings of the National Academy of Sciences, 1994
- At least 12 genotypes of hepatitis C virus predicted by sequence analysis of the putative E1 gene of isolates collected worldwide.Proceedings of the National Academy of Sciences, 1993
- Gene mapping of the putative structural region of the hepatitis C virus genome by in vitro processing analysis.Proceedings of the National Academy of Sciences, 1991
- Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase.Proceedings of the National Academy of Sciences, 1986