ArticleProceedings of the National Academy of Sciences of the United States of America2014
Crystal structure of a nematode-infecting virus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 36 citations in OpenAlex.
- Beyond Pathogenesis: The Nematode Immune Network as the Arbiter of a Host-Virus Truce.Viruses · 2025Review
- Orsay virus variants isolated from wildMicrobiology resource announcements · 2025Article
- Detection of Orsay viral replication intermediates reveals spatial and regulatory links tobioRxiv : the preprint server for biology · 2025Article
- Insights into Virus-Host Interactions: Lessons from Caenorhabditis elegans-Orsay Virus Model.Current medical science · 2025Review
- Orsay virus infection rate declines with age inmicroPublication biology · 2025Article
- Collagen and actin network mediate antiviral immunity against Orsay virus in C. elegans intestinal cells.PLoS pathogens · 2024Article
- Orsay Virus Infection of Caenorhabditis elegans Is Modulated by Zinc and Dependent on Lipids.Journal of virology · 2022Article
- Article
- Orsay Virus CP-δ Adopts a Novel β-Bracelet Structural Fold and Incorporates into Virions as a Head Fiber.Journal of virology · 2020Article
- Cryo-electron Microscopy Structures of Novel Viruses from Mud CrabJournal of virology · 2019Article
- The atomic structures of shrimp nodaviruses reveal new dimeric spike structures and particle polymorphism.Communications biology · 2019Article
- Terminal uridylyltransferases target RNA viruses as part of the innate immune system.Nature structural & molecular biology · 2018Article
- Orsay δ Protein Is Required for Nonlytic Viral Egress.Journal of virology · 2018Article
- Varieties of charge distributions in coat proteins of ssRNA+ viruses.Journal of physics. Condensed matter : an Institute of Physics journal · 2018Article
- Caenorhabditis elegans as an Emerging Model for Virus-Host Interactions.Journal of virology · 2017Review
- Cryo-Electron Microscopy Structure of the Macrobrachium rosenbergii Nodavirus Capsid at 7 Angstroms Resolution.Scientific reports · 2017Article
- The Natural Biotic Environment ofGenetics · 2017Review
- Structure of a pentameric virion-associated fiber with a potential role in Orsay virus entry to host cells.PLoS pathogens · 2017Article
- The Shift of the Intestinal Microbiome in the Innate Immunity-Deficient MutantFrontiers in microbiology · 2017Article
- An expressed, endogenous Nodavirus-like element captured by a retrotransposon in the genome of the plant parasitic nematode Bursaphelenchus xylophilus.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
Abstract
Orsay, the first virus discovered to naturally infect Caenorhabditis elegans or any nematode, has a bipartite, positive-sense RNA genome. Sequence analyses show that Orsay is related to nodaviruses, but molecular characterizations of Orsay reveal several unique features, such as the expression of a capsid-δ fusion protein and the use of an ATG-independent mechanism for translation initiation. Here we report the crystal structure of an Orsay virus-like particle assembled from recombinant capsid protein (CP). Orsay capsid has a T = 3 icosahedral symmetry with 60 trimeric surface spikes. Each CP can be divided into three regions: an N-terminal arm that forms an extended protein interaction network at the capsid interior, an S domain with a jelly-roll, β-barrel fold forming the continuous capsid, and a P domain that forms surface spike projections. The structure of the Orsay S domain is best aligned to T = 3 plant RNA viruses but exhibits substantial differences compared with the insect-infecting alphanodaviruses, which also lack the P domain in their CPs. The Orsay P domain is remotely related to the P1 domain in calicivirus and hepatitis E virus, suggesting a possible evolutionary relationship. Removing the N-terminal arm produced a slightly expanded capsid with fewer nucleic acids packaged, suggesting that the arm is important for capsid stability and genome packaging. Because C. elegans-Orsay serves as a highly tractable model for studying viral pathogenesis, our results should provide a valuable structural framework for further studies of Orsay replication and infection.
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