ArticleThe EMBO journal2001
Structure of the reovirus outer capsid and dsRNA-binding protein sigma3 at 1.8 A resolution.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
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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
44 citing papers in PubMed, 82 citations in OpenAlex.
- Review
- The nucleocapsid architecture and structural atlas of the prototype baculovirus define the hallmarks of a new viral realm.Science advances · 2024Article
- NgR1 binding to reovirus reveals an unusual bivalent interaction and a new viral attachment protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Reovirus σ3 Protein Inhibits NF-κB-Dependent Antiviral Signaling.Journal of virology · 2022Article
- The multi-functional reovirus σ3 protein is a virulence factor that suppresses stress granule formation and is associated with myocardial injury.PLoS pathogens · 2021Article
- Crucial mutation in the exoribonuclease domain of nsp14 of PEDV leads to high genetic instability during viral replication.Cell & bioscience · 2021Article
- Structure-Based Deep Mining Reveals First-Time Annotations for 46 Percent of the Dark Annotation Space of the 9,671-Member Superproteome of the Nucleocytoplasmic Large DNA Viruses.Journal of virology · 2020Article
- Article
- Single Amino Acid Differences between Closely Related Reovirus T3D Lab Strains Alter Oncolytic PotencyJournal of virology · 2020Article
- How Many Mammalian Reovirus Proteins are involved in the Control of the Interferon Response?Pathogens (Basel, Switzerland) · 2019Review
- Synthesis and Translation of Viral mRNA in Reovirus-Infected Cells: Progress and Remaining Questions.Viruses · 2018Review
- Nonstructural Protein σ1s Is Required for Optimal Reovirus Protein Expression.Journal of virology · 2018Article
- The TRiC chaperonin controls reovirus replication through outer-capsid folding.Nature microbiology · 2018Article
- Article
- Potential for Improving Potency and Specificity of Reovirus Oncolysis with Next-Generation Reovirus Variants.Viruses · 2015Review
- Double-Stranded RNA Is Detected by Immunofluorescence Analysis in RNA and DNA Virus Infections, Including Those by Negative-Stranded RNA Viruses.Journal of virology · 2015Article
- RhoA/ROCK1 regulates Avian Reovirus S1133-induced switch from autophagy to apoptosis.BMC veterinary research · 2015Article
- Proteolytic disassembly of viral outer capsid proteins is crucial for reovirus-mediated type-I interferon induction in both reovirus-susceptible and reovirus-refractory tumor cells.BioMed research international · 2015Article
- Inhibition of antiviral innate immunity by birnavirus VP3 protein via blockage of viral double-stranded RNA binding to the host cytoplasmic RNA detector MDA5.Journal of virology · 2014Article
- Reovirus receptors, cell entry, and proapoptotic signaling.Advances in experimental medicine and biology · 2013Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The crystallographically determined structure of the reovirus outer capsid protein sigma3 reveals a two-lobed structure organized around a long central helix. The smaller of the two lobes includes a CCHC zinc-binding site. Residues that vary between strains and serotypes lie mainly on one surface of the protein; residues on the opposite surface are conserved. From a fit of this model to a reconstruction of the whole virion from electron cryomicroscopy, we propose that each sigma3 subunit is positioned with the small lobe anchoring it to the protein mu1 on the surface of the virion, and the large lobe, the site of initial cleavages during entry-related proteolytic disassembly, protruding outwards. The surface containing variable residues faces solvent. The crystallographic asymmetric unit contains two sigma3 subunits, tightly associated as a dimer. One broad surface of the dimer has a positively charged surface patch, which extends across the dyad. In infected cells, sigma3 binds dsRNA and inhibits the interferon response. The location and extent of the positively charged surface patch suggest that the dimer is the RNA-binding form of sigma3.
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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.