ArticleJournal of virology2011
The SUMOylation of matrix protein M1 modulates the assembly and morphogenesis of influenza A virus.
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 61 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
61 citing papers in PubMed, 86 citations in OpenAlex.
- Evolutionary Rate Variation at Predicted PTM Sites Reveals Localized Host-Associated Patterns in Influenza A Virus.Genome biology and evolution · 2026Article
- Post-Translational Modifications in Respiratory Virus Infection: Recent Insights into the Development of In Vitro Models.International journal of molecular sciences · 2025Review
- Matrix protein 1 (M1) of influenza A virus: structural and functional insights.Emerging microbes & infections · 2025Review
- H5N1 2.3.4.4b: a review of mammalian adaptations and risk of pandemic emergence.The Journal of general virology · 2025Review
- Human ANP32A/B are SUMOylated and utilized by avian influenza virus NS2 protein to overcome species-specific restriction.Nature communications · 2024Article
- Article
- Paradoxes of Cellular SUMOylation Regulation: A Role of Biomolecular Condensates?Pharmacological reviews · 2023Review
- Article
- Multiple-Site SUMOylation of FMDV 3C Protease and Its Negative Role in Viral Replication.Journal of virology · 2022Article
- PSMD12-Mediated M1 Ubiquitination of Influenza A Virus at K102 Regulates Viral Replication.Journal of virology · 2022Article
- PIAS1-mediated SUMOylation of influenza A virus PB2 restricts viral replication and virulence.PLoS pathogens · 2022Article
- SUMOylation in Viral Replication and Antiviral Defense.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Review
- SUMOylation of Matrix Protein M1 and Filamentous Morphology Collectively Contribute to the Replication and Virulence of Highly Pathogenic H5N1 Avian Influenza Viruses in Mammals.Journal of virology · 2022Article
- Article
- Review
- Review
- Viral RNA-binding ability conferred by SUMOylation at PB1 K612 of influenza A virus is essential for viral pathogenesis and transmission.PLoS pathogens · 2021Article
- Role of Host-Mediated Post-Translational Modifications (PTMs) in RNA Virus Pathogenesis.International journal of molecular sciences · 2020Review
- Influenza virus neuraminidase regulates host CD8Communications biology · 2020Article
- Article
1 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
No grant is acknowledged in the PubMed record.
Abstract
SUMOylation is an important posttranslational modification for regulation of cellular functions and viral replication. Here, we report that protein SUMOylation regulates the replication of influenza A virus at the steps of viral maturation and assembly. Knocking down the SUMO-conjugating enzyme Ubc9 resulted in the reduction of virus production. Dissection of the virus life cycle revealed that SUMOylation is involved in the processes of virus maturation and assembly. The viral matrix protein M1 is SUMOylated at K242. A virus carrying the SUMO-defective M1 produced a lower titer of virus, while its viral proteins and viral RNA (vRNA) accumulated in the cells. Furthermore, the mechanistic studies showed that the SUMOylation of M1 is required for the interaction between M1 and viral RNP (vRNP) to form the M1-vRNP complex. The lack of M1 SUMOylation prevented the nuclear export of vRNP and subsequent viral morphogenesis. Taken together, our findings elucidate that the maturation and assembly of influenza A virus is controlled by the SUMO modification of M1 protein. Therefore, we suggest that M1 can serve as a target for developing a new generation of drugs for flu therapy.
Indexed as
Identifiers
What OpenQuestion holds
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.