ArticleJournal of virology2010
Murine hepatitis virus nonstructural protein 4 regulates virus-induced membrane modifications and replication complex function.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed.
- Structural insights into SARS-CoV-2 nonstructural protein 4 (nsp4) biogenesis.Protein science : a publication of the Protein Society · 2025Article
- Anticoronavirus Activity of Uridine Glycoconjugates Containing a 1,2,3-Triazole Moiety.Journal of medicinal chemistry · 2025Article
- The glycoprotein quality control factor Malectin promotes coronavirus replication and viral protein biogenesis.bioRxiv : the preprint server for biology · 2025Article
- Deciphering the Genetic Variation: A Comparative Analysis of Parental and Attenuated Strains of the QXL87 Vaccine for Infectious Bronchitis.Animals : an open access journal from MDPI · 2024Article
- Mitochondria in COVID-19: from cellular and molecular perspective.Frontiers in physiology · 2024Review
- Mechanism, structural and functional insights into nidovirus-induced double-membrane vesicles.Frontiers in immunology · 2024Review
- Identification of host dependency factors involved in SARS-CoV-2 replication organelle formation through proteomics and ultrastructural analysis.Journal of virology · 2023Article
- Glycoprotein Non-Metastatic Melanoma Protein B Restricts PRRSV Replication by Inhibiting Autophagosome-Lysosome Fusion.Viruses · 2023Article
- A review on structural, non-structural, and accessory proteins of SARS-CoV-2: Highlighting drug target sites.Immunobiology · 2023Review
- Modelling the Transitioning of SARS-CoV-2 nsp3 and nsp4 Lumenal Regions towards a More Stable State on Complex Formation.International journal of molecular sciences · 2022Article
- Glycosylation of viral proteins: Implication in virus-host interaction and virulence.Virulence · 2022Review
- Two Years into the COVID-19 Pandemic: Lessons Learned.ACS infectious diseases · 2022Review
- Unique mutations in SARS-CoV-2 Omicron subvariants' non-spike proteins: Potential impacts on viral pathogenesis and host immune evasion.Microbial pathogenesis · 2022Review
- Article
- Cellular host factors for SARS-CoV-2 infection.Nature microbiology · 2021Review
- An overview of SARS-COV-2 epidemiology, mutant variants, vaccines, and management strategies.Journal of infection and public health · 2021Review
- Why do SARS-CoV-2 NSPs rush to the ER?Journal of neurology · 2021Review
- Genome composition and genetic characterization of SARS-CoV-2.Saudi journal of biological sciences · 2021Review
- Targeting novel structural and functional features of coronavirus protease nsp5 (3CLThe Journal of general virology · 2021Review
- Naturally Occurring Bioactives as Antivirals: Emphasis on Coronavirus Infection.Frontiers in pharmacology · 2021Review
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Authors and funding
7 authors.
Funding
Abstract
Positive-strand RNA viruses induce modifications of cytoplasmic membranes to form replication complexes. For coronaviruses, replicase nonstructural protein 4 (nsp4) has been proposed to function in the formation and organization of replication complexes. Murine hepatitis virus (MHV) nsp4 is glycosylated at residues Asn176 (N176) and N237 during plasmid expression of nsp4 in cells. To test if MHV nsp4 residues N176 and N237 are glycosylated during virus replication and to determine the effects of N176 and N237 on nsp4 function and MHV replication, alanine substitutions of nsp4 N176, N237, or both were engineered into the MHV-A59 genome. The N176A, N237A, and N176A/N237A mutant viruses were viable, and N176 and N237 were glycosylated during infection of wild-type (wt) and mutant viruses. The nsp4 glycosylation mutants exhibited impaired virus growth and RNA synthesis, with the N237A and N176A/N237A mutant viruses demonstrating more profound defects in virus growth and RNA synthesis. Electron microscopic analysis of ultrastructure from infected cells demonstrated that the nsp4 mutants had aberrant morphology of virus-induced double-membrane vesicles (DMVs) compared to those infected with wt virus. The degree of altered DMV morphology directly correlated with the extent of impairment in viral RNA synthesis and virus growth of the nsp4 mutant viruses. The results indicate that nsp4 plays a critical role in the organization and stability of DMVs. The results also support the conclusion that the structure of DMVs is essential for efficient RNA synthesis and optimal replication of coronaviruses.
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