ArticlePLoS pathogens2014
New insights into rotavirus entry machinery: stabilization of rotavirus spike conformation is independent of trypsin cleavage.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- Structural determinants of rotavirus proteolytic activation.PLoS pathogens · 2025Article
- Tapping into Metabolomics for Understanding Host and Rotavirus Group A Interactome.Life (Basel, Switzerland) · 2025Article
- Rotavirus-specific neutralization assay enables evaluation of mucosal immune responses.Frontiers in immunology · 2025Article
- The recruitment of TRiC chaperonin in rotavirus viroplasms correlates with virus replication.mBio · 2024Article
- VP4 Mutation Boosts Replication of Recombinant Human/Simian Rotavirus in Cell Culture.Viruses · 2024Article
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- Acute rotavirus infection is associated with the induction of circulating memory CD4Scientific reports · 2023Article
- Epidemiological study of unusual rotavirus strains and molecular characterization of emerging P[14] strains isolated from children with acute gastroenteritis during a 15-year period.Archives of virology · 2023Article
- Characterization of the rotavirus assembly pathway in situ using cryoelectron tomography.Cell host & microbe · 2023Article
- Using Species a Rotavirus Reverse Genetics to Engineer Chimeric Viruses Expressing SARS-CoV-2 Spike Epitopes.Journal of virology · 2022Article
- Detection and molecular characteristics of bovine rotavirus A in dairy calves in China.Journal of veterinary science · 2021Article
- Recent advances in rotavirus reverse genetics and its utilization in basic research and vaccine development.Archives of virology · 2021Review
- Article
- Mechanisms of Cell Entry by dsRNA Viruses: Insights for Efficient Delivery of dsRNA and Tools for Improved RNAi-Based Pest Control.Frontiers in physiology · 2021Review
- Coding-Gene Coevolution Analysis of Rotavirus Proteins: A Bioinformatics and Statistical Approach.Genes · 2019Article
- Asymmetric analysis reveals novel virus capsid features.Biophysical reviews · 2019Review
- Rotavirus infection beyond the gut.Infection and drug resistance · 2019Review
- Article
- Inflammatory and oxidative stress in rotavirus infection.World journal of virology · 2016Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The infectivity of rotavirus, the main causative agent of childhood diarrhea, is dependent on activation of the extracellular viral particles by trypsin-like proteases in the host intestinal lumen. This step entails proteolytic cleavage of the VP4 spike protein into its mature products, VP8* and VP5*. Previous cryo-electron microscopy (cryo-EM) analysis of trypsin-activated particles showed well-resolved spikes, although no density was identified for the spikes in uncleaved particles; these data suggested that trypsin activation triggers important conformational changes that give rise to the rigid, entry-competent spike. The nature of these structural changes is not well understood, due to lack of data relative to the uncleaved spike structure. Here we used cryo-EM and cryo-electron tomography (cryo-ET) to characterize the structure of the uncleaved virion in two model rotavirus strains. Cryo-EM three-dimensional reconstruction of uncleaved virions showed spikes with a structure compatible with the atomic model of the cleaved spike, and indistinguishable from that of digested particles. Cryo-ET and subvolume average, combined with classification methods, resolved the presence of non-icosahedral structures, providing a model for the complete structure of the uncleaved spike. Despite the similar rigid structure observed for uncleaved and cleaved particles, trypsin activation is necessary for successful infection. These observations suggest that the spike precursor protein must be proteolytically processed, not to achieve a rigid conformation, but to allow the conformational changes that drive virus entry.
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