ArticleThe Journal of biological chemistry2015
Hepatitis C Virus Particle Assembly Involves Phosphorylation of NS5A by the c-Abl Tyrosine Kinase.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- A global map of the Zika virus phosphoproteome reveals host-driven regulation of viral particle release and cytopathogenicity.PLoS pathogens · 2026Article
- Serotype-Specific Biochemical and Immunological Signatures of Dengue Virus Envelope Proteins.Current issues in molecular biology · 2026Article
- An integrated proteomics approach identifies phosphorylation sites on viral and host proteins that regulate West Nile virus infection.Cell reports · 2025Article
- Role of c-ABL in DENV-2 Infection and Actin Remodeling in Vero Cells.International journal of molecular sciences · 2025Article
- ASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infection.The Journal of general virology · 2023Article
- Cellular factors involved in the hepatitis C virus life cycle.World journal of gastroenterology · 2021Review
- Structural Modifications Controlling Membrane Raft Partitioning and Curvature in Human and Viral Proteins.The journal of physical chemistry. B · 2020Article
- Phosphorylated tyrosine 93 of hepatitis C virus nonstructural protein 5A is essential for interaction with host c-Src and efficient viral replication.The Journal of biological chemistry · 2019Article
- Restriction of hepatitis B virus replication by c-Abl-induced proteasomal degradation of the viral polymerase.Science advances · 2019Article
- Coronavirus S protein-induced fusion is blocked prior to hemifusion by Abl kinase inhibitors.The Journal of general virology · 2018Article
- Dual inhibitors of hepatitis C virus and hepatocellular carcinoma: design, synthesis and docking studies.Future science OA · 2018Article
- STAT1 is essential for the inhibition of hepatitis C virus replication by interferon-λ but not by interferon-α.Scientific reports · 2016Article
- Multifunctional Abl kinases in health and disease.Journal of cell science · 2016Review
- Phosphorylation of Single Stranded RNA Virus Proteins and Potential for Novel Therapeutic Strategies.Viruses · 2015Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hepatitis C virus (HCV) nonstructural protein 5A (NS5A) is thought to regulate the replication of viral RNA and the assembly of virus particles in a serine/threonine phosphorylation-dependent manner. However, the host kinases that phosphorylate NS5A have not been fully identified. Here, we show that HCV particle assembly involves the phosphorylation of NS5A by the c-Abl tyrosine kinase. Pharmacological inhibition or knockdown of c-Abl reduces the production of infectious HCV (J6/JFH1) particles in Huh-7.5 cells without markedly affecting viral RNA translation and replication. NS5A is tyrosine-phosphorylated in HCV-infected cells, and this phosphorylation is also reduced by the knockdown of c-Abl. Mutational analysis reveals that NS5A tyrosine phosphorylation is dependent, at least in part, on Tyr(330) (Tyr(2306) in polyprotein numbering). Mutation of this residue to phenylalanine reduces the production of infectious HCV particles but does not affect the replication of the JFH1 subgenomic replicon. These findings suggest that c-Abl promotes HCV particle assembly by phosphorylating NS5A at Tyr(330).
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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.