ArticleJournal of virology1997
The internal open reading frame within the nucleocapsid gene of mouse hepatitis virus encodes a structural protein that is not essential for viral replication.
Article in Journal of virology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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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.
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Who cites it
69 citing papers in PubMed, 104 citations in OpenAlex.
- Definition of the components required for selective packaging of coronavirus genomic RNA.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Betacoronavirus internal protein: role in immune evasion and viral pathogenesis.Journal of virology · 2025Review
- The SARS-CoV-2 nucleocapsid protein interferes with the full enzymatic activation of UPF1 and its interaction with UPF2.Nucleic acids research · 2025Article
- Mouse hepatitis virus JHMV I protein is required for maximal virulence.Journal of virology · 2024Article
- Hydrophobic Alpha-Helical Short Peptides in Overlapping Reading Frames of the Coronavirus Genome.Pathogens (Basel, Switzerland) · 2022Article
- One microRNA has the potential to target whole viral mRNAs in a given human coronavirus.Frontiers in microbiology · 2022Review
- Spike Glycoprotein Is Central to Coronavirus Pathogenesis-Parallel Between m-CoV and SARS-CoV-2.Annals of neurosciences · 2021Review
- Recent Progress in Torovirus Molecular Biology.Viruses · 2021Review
- Coronavirus, the King Who Wanted More Than a Crown: From Common to the Highly Pathogenic SARS-CoV-2, Is the Key in the Accessory Genes?Frontiers in microbiology · 2021Review
- Naturally Occurring Bioactives as Antivirals: Emphasis on Coronavirus Infection.Frontiers in pharmacology · 2021Review
- Middle East Respiratory Syndrome Coronavirus ORF8b Accessory Protein Suppresses Type I IFN Expression by Impeding HSP70-Dependent Activation of IRF3 Kinase IKKε.Journal of immunology (Baltimore, Md. : 1950) · 2020Article
- Review
- Porcine Deltacoronavirus Accessory Protein NS7a Antagonizes IFN-β Production by Competing With TRAF3 and IRF3 for Binding to IKKε.Frontiers in cellular and infection microbiology · 2020Article
- Genetic manipulation of porcine deltacoronavirus reveals insights into NS6 and NS7 functions: a novel strategy for vaccine design.Emerging microbes & infections · 2020Article
- Transcriptional and Translational Landscape of Equine Torovirus.Journal of virology · 2018Article
- Porcine Deltacoronavirus Accessory Protein NS6 Antagonizes Interferon Beta Production by Interfering with the Binding of RIG-I/MDA5 to Double-Stranded RNA.Journal of virology · 2018Article
- Article
- Expanded subgenomic mRNA transcriptome and coding capacity of a nidovirus.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- High-Resolution Analysis of Coronavirus Gene Expression by RNA Sequencing and Ribosome Profiling.PLoS pathogens · 2016Article
- Viral and Cellular mRNA Translation in Coronavirus-Infected Cells.Advances in virus research · 2016Review
9 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
5 authors at 1 institution in 1 country.
Funding
Abstract
The coronavirus mouse hepatitis virus (MHV) contains a large open reading frame embedded entirely within the 5' half of its nucleocapsid (N) gene. This internal gene (designated I) is in the +1 reading frame with respect to the N gene, and it encodes a mostly hydrophobic 23-kDa polypeptide. We have found that this protein is expressed in MHV-infected cells and that it is a previously unrecognized structural protein of the virion. To analyze the potential biological importance of the I gene, we disrupted its expression by site-directed mutagenesis using targeted RNA recombination. The start codon for I was replaced by a threonine codon, and a stop codon was introduced at a short interval downstream. Both alterations created silent changes in the N reading frame. In vitro translation studies showed that these mutations completely abolished synthesis of I protein, and immunological analysis of infected cell lysates confirmed this conclusion. The MHV I mutant was viable and grew to high titer. However, the I mutant had a reduced plaque size in comparison with its isogenic wild-type counterpart, suggesting that expression of I confers some minor growth advantage to the virus. The engineered mutations were stable during the course of experimental infection in mice, and the I mutant showed no significant differences from wild type in its ability to replicate in the brains or livers of infected animals. These results demonstrate that I protein is not essential for the replication of MHV either in tissue culture or in its natural host.
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