ArticleNature communications2022
In situ structure and dynamics of an alphacoronavirus spike protein by cryo-ET and cryo-EM.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 56 citations in OpenAlex.
- Virus-like particles vaccine of porcine epidemic diarrhea virus spike 1 protein induces protective immunity challenge in piglets.Biochemistry and biophysics reports · 2026Article
- Single-cell RNA sequencing identifies uterine stromal cells as a previously unrecognized target of an alphacoronavirus underlying reproductive disorders.Journal of virology · 2026Article
- Structure and receptor recognition of type-II feline infectious peritonitis virus spike glycoprotein.The EMBO journal · 2026Article
- Mass Photometry Reveals Distinct ACE2 Binding Stoichiometries across SARS-CoV-2 Omicron Subvariants.The journal of physical chemistry. B · 2026Article
- Spatially and temporally comparative proteomics provide insights into dynamic response patterns to PEDV infection.Communications biology · 2026Article
- Cetacean coronavirus spikes highlight S glycoprotein structural plasticity.PLoS pathogens · 2026Article
- Article
- AI-guided prefusion stabilization of the human coronavirus OC43 spike protein enables universal embecovirus antigen design.PLoS pathogens · 2026Article
- Salvianolic acid A exerts antiviral effects by targeting the S protein, a virulence factor of porcine epidemic diarrhea virus.Journal of virology · 2026Article
- Preclinical Evaluation of a Phage T4-Based Multi-Epitope Nanoparticle Vaccine Against Porcine Epidemic Diarrhea Virus.Transboundary and emerging diseases · 2026Article
- Emergence of a Highly Virulent Porcine Epidemic Diarrhea Virus (PEDV) G2c Subtype in China: Isolation, Genetic and Pathogenic Characterization, and Cross-Neutralizing Antibody Response.Transboundary and emerging diseases · 2026Article
- Engineering a TGEV S-trimer chimera with PEDV D0-NTD generates potent neutralizing antibodies against both viruses.Journal of virology · 2025Article
- N-glycosylation of the PEDV spike protein modulates viral replication and pathogenicity.Veterinary research · 2025Article
- Genetic characterization and pathogenicity analysis of three porcine epidemic diarrhea virus strains isolated from North China.Veterinary research · 2025Article
- A novel genotyping system based on site polymorphism on spike gene reveals the evolutionary pathway of porcine epidemic diarrhea virus.iMetaOmics · 2025Article
- Single-particle cryogenic electron microscopy structure determination for membrane proteins.Current opinion in structural biology · 2025Review
- Molecular characteristics of the immune escape of coronavirus PEDV under the pressure of vaccine immunity.Journal of virology · 2025Article
- Changes in the motifs in the D0 and SD2 domains of the S protein drive the evolution of virulence in enteric coronavirus porcine epidemic diarrhea virus.Journal of virology · 2025Article
- STT3B promotes porcine epidemic diarrhea virus replication by regulating N-glycosylation of PEDV S protein.Journal of virology · 2025Article
- Molecular basis of host recognition of human coronavirus 229E.Nature communications · 2025Article
Corrections and comments
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Authors and funding
15 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Porcine epidemic diarrhea (PED) is a highly contagious swine disease caused by porcine epidemic diarrhea virus (PEDV). PED causes enteric disorders with an exceptionally high fatality in neonates, bringing substantial economic losses in the pork industry. The trimeric spike (S) glycoprotein of PEDV is responsible for virus-host recognition, membrane fusion, and is the main target for vaccine development and antigenic analysis. The atomic structures of the recombinant PEDV S proteins of two different strains have been reported, but they reveal distinct N-terminal domain 0 (D0) architectures that may correspond to different functional states. The existence of the D0 is a unique feature of alphacoronavirus. Here we combined cryo-electron tomography (cryo-ET) and cryo-electron microscopy (cryo-EM) to demonstrate in situ the asynchronous S protein D0 motions on intact viral particles of a highly virulent PEDV Pintung 52 strain. We further determined the cryo-EM structure of the recombinant S protein derived from a porcine cell line, which revealed additional domain motions likely associated with receptor binding. By integrating mass spectrometry and cryo-EM, we delineated the complex compositions and spatial distribution of the PEDV S protein N-glycans, and demonstrated the functional role of a key N-glycan in modulating the D0 conformation.
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