ArticleJournal of virology2013
SUMOylation affects the interferon blocking activity of the influenza A nonstructural protein NS1 without affecting its stability or cellular localization.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 46 citations in OpenAlex.
- CBX4 facilitates EV71 replication by SUMOylation and stabilizing 3D polymerase.Frontiers in microbiology · 2026Article
- The roles of post-translational modifications in the pathogenesis of RNA viruses: allies or adversaries?Frontiers in microbiology · 2026Review
- Chronic Diseases and Influenza Vaccines.Vaccines · 2025Review
- Nonstructural Protein 1 of Influenza A (NS1A) Demonstrates Strain-Specific dsRNA Binding Capabilities.ACS infectious diseases · 2025Article
- The applications of live attenuated influenza a virus with modified NS1 gene.Molecular therapy. Nucleic acids · 2025Review
- A Vivo-Morpholino-Based Approach to Block Paralog-Specific SUMOylation.Methods in molecular biology (Clifton, N.J.) · 2025Article
- SUMOylation of SARS-CoV-2 spike protein is a key target for broad-spectrum antiviral therapy.Theranostics · 2025Article
- Antiviral responses versus virus-induced cellular shutoff: a game of thrones between influenza A virus NS1 and SARS-CoV-2 Nsp1.Frontiers in cellular and infection microbiology · 2024Review
- Paradoxes of Cellular SUMOylation Regulation: A Role of Biomolecular Condensates?Pharmacological reviews · 2023Review
- SUMO Proteomics Analyses Identify Protein Inhibitor of Activated STAT-Mediated Regulatory Networks Involved in Cell Cycle and Cell Proliferation.Journal of proteome research · 2023Article
- Generation of a high yield vaccine backbone for influenza B virus in embryonated chicken eggs.NPJ vaccines · 2023Article
- Multiple-Site SUMOylation of FMDV 3C Protease and Its Negative Role in Viral Replication.Journal of virology · 2022Article
- PIAS1-mediated SUMOylation of influenza A virus PB2 restricts viral replication and virulence.PLoS pathogens · 2022Article
- Article
- Review
- The influenza A virus host shutoff factor PA-X is rapidly turned over in a strain-specific manner.Journal of virology · 2021Article
- Viral RNA-binding ability conferred by SUMOylation at PB1 K612 of influenza A virus is essential for viral pathogenesis and transmission.PLoS pathogens · 2021Article
- MASS SPECTROMETRY IN VIROLOGICAL SCIENCES.Mass spectrometry reviews · 2020Review
- Structure and Sequence Determinants Governing the Interactions of RNAs with Influenza A Virus Non-Structural Protein NS1.Viruses · 2020Article
- The Central Role of Non-Structural Protein 1 (NS1) in Influenza Biology and Infection.International journal of molecular sciences · 2020Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Our pioneering studies on the interplay between the small ubiquitin-like modifier (SUMO) and influenza A virus identified the nonstructural protein NS1 as the first known SUMO target of influenza virus and one of the most abundantly SUMOylated influenza virus proteins. Here, we further characterize the role of SUMOylation for the A/Puerto Rico/8/1934 (PR8) NS1 protein, demonstrating that NS1 is SUMOylated not only by SUMO1 but also by SUMO2/3 and mapping the main SUMOylation sites in NS1 to residues K219 and K70. Furthermore, by using SUMOylatable and non-SUMOylatable forms of NS1 and an NS1-specific artificial SUMO ligase (ASL) that increases NS1 SUMOylation ~4-fold, we demonstrate that SUMOylation does not affect the stability or cellular localization of PR8 NS1. However, NS1's ability to be SUMOylated appears to affect virus multiplication, as indicated by the delayed growth of a virus expressing the non-SUMOylatable form of NS1 in the interferon (IFN)-competent MDCK cell line. Remarkably, while a non-SUMOylatable form of NS1 exhibited a substantially diminished ability to neutralize IFN production, increasing NS1 SUMOylation beyond its normal levels also exerted a negative effect on its IFN-blocking function. This observation indicates the existence of an optimal level of NS1 SUMOylation that allows NS1 to achieve maximal activity and suggests that the limited amount of SUMOylation normally observed for most SUMO targets may correspond to an optimal level that maximizes the contribution of SUMOylation to protein function. Finally, protein cross-linking data suggest that SUMOylation may affect NS1 function by regulating the abundance of NS1 dimers and trimers in the cell.
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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.