ArticleThe Journal of cell biology2025
SARS-CoV-2 NSP3/4 control formation of replication organelle and recruitment of RNA polymerase NSP12.
Article in The Journal of cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Recent advances in functional studies of coronavirus NSP13 helicase and challenges in inhibitor development.Virulence · 2026Review
- VPS33A and VPS18 orchestrate porcine epidemic diarrhea virus replication by modulating autophagic flux.Virulence · 2026Article
- GPNMB promotes double-membrane vesicle accumulation and facilitates structural protein transport during PEDV infection.Virulence · 2026Article
- Conformational Dynamics of Viral Protease Precursors in Maturation, Inhibition, and Drug-Resistance Development.Viruses · 2026Review
- Targeting host lipogenesis with a diarylamide inhibitor disrupts SARS-CoV-2 replication.iScience · 2026Article
- Super-resolution atlas of SARS-CoV-2 infection reveals protease-dependent organelle maturation, dsRNA landscapes, and intracellular structural proteins.Nature communications · 2026Article
- Disruption of ER-mitochondria contact sites by coronavirus replication organelles sustains viral replication via NSP3 stabilization.The EMBO journal · 2026Article
- Heterodimerization of PRRSV replicase membrane proteins nsp2 and nsp3 regulates their cytoplasmic tail binding to viral RdRp domain for sgRNA synthesis.Journal of virology · 2026Article
- The transmembrane segments of SARS-CoV-2 nsp3 govern viral intracellular trafficking.Cell & bioscience · 2026Article
- A pan-viral map of host dependency factors from multi-omics integration and machine learning across influenza A, SARS-CoV-2, Zika, and dengue viruses.Journal of translational medicine · 2026Article
- Chemical modulation of the unfolded protein response reveals an antiviral role for the PERK pathway in human coronavirus 229E infection.RSC chemical biology · 2026Article
- Emerging approaches for characterizing spatial and temporal dynamics of pathogen-induced organelle remodeling.Cell systems · 2026Review
- In Search of the Most Significant Potential G-Quadruplexes in SARS-CoV-2 RNA: Genomic Analysis.Viruses · 2026Article
- SARS-CoV-2 polyprotein expression and the induction of double-membrane vesicles.Journal of virology · 2025Article
- Review
- The SARS-CoV-2 NSP4 T492I mutation promotes double-membrane vesicle formation to facilitate transmission.Virologica Sinica · 2025Article
- Whole-cell response of coronavirus-infected BMDCs through proteomic and transcriptomic analyses.Frontiers in immunology · 2025Article
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Authors and funding
15 authors.
Funding
Abstract
β-coronavirus rearranges the host cellular membranes to form double-membrane vesicles (DMVs) via NSP3/4, which anchor replication-transcription complexes (RTCs), thereby constituting the replication organelles (ROs). However, the impact of specific domains within NSP3/4 on DMV formation and RO assembly remains largely unknown. By using cryogenic-correlated light and electron microscopy (cryo-CLEM), we discovered that the N-terminal and C-terminal domains (NTD and CTD) of SARS-CoV-2 NSP3 are essential for DMV formation. Nevertheless, the CTD of NSP4 is not essential for DMV formation but regulates the DMV numbers. Additionally, the NTD of NSP3 is required for recruiting the RTC component to the cytosolic face of DMVs through direct interaction with NSP12 to assemble ROs. Furthermore, we observed that the size of NSP3/4-induced DMVs is smaller than virus-induced DMVs and established that RTC-mediated synthesis of double-stranded RNA (dsRNA) cargo plays a crucial role in determining DMV size. Collectively, our findings reveal that β-coronaviruses exploit the NSP3/4/12 axis to establish the viral ROs.
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