ArticleJournal of virology2010
The C-terminal alpha-helix domain of apolipoprotein E is required for interaction with nonstructural protein 5A and assembly of hepatitis C virus.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
77 citing papers in PubMed, 118 citations in OpenAlex.
- Depressive symptoms in chronic hepatitis C are associated with plasma apolipoprotein E deficiency.Metabolic brain disease · 2014Trial
- Promotion of hepatitis B virus infection by extracellular apolipoprotein E.Journal of virology · 2026Article
- Recruitment of apolipoprotein E facilitates Herpes simplex virus 1 attachment and release.Npj viruses · 2025Article
- Emerging role of lipophagy in liver disorders.Molecular and cellular biochemistry · 2024Review
- Apolipoprotein E and viral infection: Risks and Mechanisms.Molecular therapy. Nucleic acids · 2023Review
- Endosomal egress and intercellular transmission of hepatic ApoE-containing lipoproteins and its exploitation by the hepatitis C virus.PLoS pathogens · 2023Article
- Cellular metabolism hijacked by viruses for immunoevasion: potential antiviral targets.Frontiers in immunology · 2023Review
- Apolipoprotein E mediates cell resistance to influenza virus infection.Science advances · 2022Article
- Circumsporozoite Protein ofPharmaceutics · 2022Article
- Human low-density lipoprotein receptor plays an important role in hepatitis B virus infection.PLoS pathogens · 2021Article
- Metabolic complications of hepatitis C virus infection.World journal of gastroenterology · 2021Review
- Molecular Events Occurring in Lipophagy and Its Regulation inFrontiers in microbiology · 2021Review
- Human apolipoprotein E promotes hepatitis B virus infection and production.PLoS pathogens · 2019Article
- The Role of ApoE in HCV Infection and Comorbidity.International journal of molecular sciences · 2019Review
- The Genetic Variability ofGenes · 2019Review
- HCV Pit Stop at the Lipid Droplet: Refuel Lipids and Put on a Lipoprotein Coat before Exit.Cells · 2019Review
- Article
- Regulation of Apolipoprotein E Trafficking by Hepatitis C Virus-Induced Autophagy.Journal of virology · 2018Article
- Relevance of Rab Proteins for the Life Cycle of Hepatitis C Virus.Frontiers in cell and developmental biology · 2018Review
- Hepatitis C Virus (HCV)-Apolipoprotein Interactions and Immune Evasion and Their Impact on HCV Vaccine Design.Frontiers in immunology · 2018Review
17 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
We have recently demonstrated that human apolipoprotein E (apoE) is required for the infectivity and assembly of hepatitis C virus (HCV) (K. S. Chang, J. Jiang, Z. Cai, and G. Luo, J. Virol. 81:13783-13793, 2007; J. Jiang and G. Luo, J. Virol. 83:12680-12691, 2009). In the present study, we have determined the molecular basis underlying the importance of apoE in HCV assembly. Results derived from mammalian two-hybrid studies demonstrate a specific interaction between apoE and HCV nonstructural protein 5A (NS5A). The C-terminal third of apoE per se is sufficient for interaction with NS5A. Progressive deletion mutagenesis analysis identified that the C-terminal α-helix domain of apoE is important for NS5A binding. The N-terminal receptor-binding domain and the C-terminal 20 amino acids of apoE are dispensable for the apoE-NS5A interaction. The NS5A-binding domain of apoE was mapped to the middle of the C-terminal α-helix domain between amino acids 205 and 280. Likewise, deletion mutations disrupting the apoE-NS5A interaction resulted in blockade of HCV production. These findings demonstrate that the specific apoE-NS5A interaction is required for assembly of infectious HCV. Additionally, we have determined that using different major isoforms of apoE (E2, E3, and E4) made no significant difference in the apoE-NS5A interaction. Likewise, these three major isoforms of apoE are equally compatible with infectivity and assembly of infectious HCV, suggesting that apoE isoforms do not differentially modulate the infectivity and/or assembly of HCV in cell culture.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.