ArticleCell host & microbe2024
NRP1 is a receptor for mammalian orthoreovirus engaged by distinct capsid subunits.
Article in Cell host & microbe, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Epstein-Barr virus receptors: classification, functional mechanisms, and pathogenic implications.Journal of virology · 2026Review
- Alpha-Glucosidase ofViruses · 2026Article
- Sialic acid serves as a functional receptor for grass carp reovirus.PLoS pathogens · 2025Article
- SARS-CoV-2 spike protein: structure, viral entry and variants.Nature reviews. Microbiology · 2025Review
- Defining diverse spike-receptor interactions involved in SARS-CoV-2 entry: Mechanisms and therapeutic opportunities.Virology · 2025Review
- Nonviral protein cages as tools to decipher and combat viral threats.Npj viruses · 2025Review
- Article
- The NamBio · 2025Article
- Review
- Establishment of reverse genetics systems for Colorado tick fever virus.PLoS pathogens · 2025Article
- From viral assembly to host interaction: AFM's contributions to virology.Journal of virology · 2025Review
- Strain-specific differences in reovirus infection of murine macrophages segregate with polymorphisms in viral outer-capsid protein σ3.Journal of virology · 2024Article
- Isolation and identification of a novel porcine-related recombinant mammalian orthoreovirus type 3 strain from cattle in Guangxi Province, China.Frontiers in microbiology · 2024Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Mammalian orthoreovirus (reovirus) is a nonenveloped virus that establishes primary infection in the intestine and disseminates to sites of secondary infection, including the CNS. Reovirus entry involves multiple engagement factors, but how the virus disseminates systemically and targets neurons remains unclear. In this study, we identified murine neuropilin 1 (mNRP1) as a receptor for reovirus. mNRP1 binds reovirus with nanomolar affinity using a unique mechanism of virus-receptor interaction, which is coordinated by multiple interactions between distinct reovirus capsid subunits and multiple NRP1 extracellular domains. By exchanging essential capsid protein-encoding gene segments, we determined that the multivalent interaction is mediated by outer-capsid protein σ3 and capsid turret protein λ2. Using capsid mutants incapable of binding NRP1, we found that NRP1 contributes to reovirus dissemination and neurovirulence in mice. Collectively, our results demonstrate that NRP1 is an entry receptor for reovirus and uncover mechanisms by which NRPs promote viral entry and pathogenesis.
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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 Socratic graph.