ArticleJournal of virology2011
The acidic domain of hepatitis C virus NS4A contributes to RNA replication and virus particle assembly.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 50 citations in OpenAlex.
- Packaging defects in pestiviral NS4A can be compensated by mutations in NS2 and NS3.Journal of virology · 2023Article
- Characterization of a multipurpose NS3 surface patch coordinating HCV replicase assembly and virion morphogenesis.PLoS pathogens · 2022Article
- TheJournal of virology · 2022Article
- Micro-PET imaging of hepatitis C virus NS3/4A protease activity using a protease-activatable retention probe.Frontiers in microbiology · 2022Article
- Hepatitis C Viral Replication Complex.Viruses · 2021Review
- Determination of Critical Requirements for Classical Swine Fever Virus NS2-3-Independent Virion Formation.Journal of virology · 2019Article
- The acidic domain of the hepatitis C virus NS4A protein is required for viral assembly and envelopment through interactions with the viral E1 glycoprotein.PLoS pathogens · 2019Article
- Tylophorine Analogs Allosterically Regulates Heat Shock Cognate Protein 70 And Inhibits Hepatitis C Virus Replication.Scientific reports · 2017Article
- IRE1α promotes viral infection by conferring resistance to apoptosis.Science signaling · 2017Article
- A positive-strand RNA virus uses alternative protein-protein interactions within a viral protease/cofactor complex to switch between RNA replication and virion morphogenesis.PLoS pathogens · 2017Article
- The Hepatitis C Virus-Induced Membranous Web and Associated Nuclear Transport Machinery Limit Access of Pattern Recognition Receptors to Viral Replication Sites.PLoS pathogens · 2016Article
- Polyprotein-Driven Formation of Two Interdependent Sets of Complexes Supporting Hepatitis C Virus Genome Replication.Journal of virology · 2015Article
- Phylogenetic and 2D/3D Analysis of HCV 1a NS4A Gene/Protein in Pakistani Isolates.Hepatitis monthly · 2015Article
- Dynamic Interaction of Stress Granules, DDX3X, and IKK-α Mediates Multiple Functions in Hepatitis C Virus Infection.Journal of virology · 2015Article
- Hepatitis C virus RNA replication depends on specific cis- and trans-acting activities of viral nonstructural proteins.PLoS pathogens · 2015Article
- HCV core protein and virus assembly: what we know without structures.Immunologic research · 2014Review
- Picornavirus morphogenesis.Microbiology and molecular biology reviews : MMBR · 2014Review
- The linker region of NS3 plays a critical role in the replication and infectivity of hepatitis C virus.Journal of virology · 2014Article
- Incorporation of hepatitis C virus E1 and E2 glycoproteins: the keystones on a peculiar virion.Viruses · 2014Review
- Genetic complementation of hepatitis C virus nonstructural protein functions associated with replication exhibits requirements that differ from those for virion assembly.Journal of virology · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Hepatitis C virus NS3-4A is a membrane-bound enzyme complex that exhibits serine protease, RNA helicase, and RNA-stimulated ATPase activities. This enzyme complex is essential for viral genome replication and has been recently implicated in virus particle assembly. To help clarify the role of NS4A in these processes, we conducted alanine scanning mutagenesis on the C-terminal acidic domain of NS4A in the context of a chimeric genotype 2a reporter virus. Of 13 mutants tested, two (Y45A and F48A) had severe defects in replication, while seven (K41A, L44A, D49A, E50A, M51A, E52A, and E53A) efficiently replicated but had severe defects in virus particle assembly. Multiple strategies were used to identify second-site mutations that suppressed these NS4A defects. The replication defect of NS4A F48A was partially suppressed by mutation of NS4B I7F, indicating that a genetic interaction between NS4A and NS4B contributes to RNA replication. Furthermore, the virus assembly defect of NS4A K41A was suppressed by NS3 Q221L, a mutation previously implicated in overcoming other virus assembly defects. We therefore examined the known enzymatic activities of wild-type or mutant forms of NS3-4A but did not detect specific defects in the mutants. Taken together, our data reveal interactions between NS4A and NS4B that control genome replication and between NS3 and NS4A that control virus assembly.
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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.