ArticleVeterinary research2025
N-glycosylation of the PEDV spike protein modulates viral replication and pathogenicity.
Article in Veterinary research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Overcoming Antigenic Drift in PEDV: Broadly Protective Antigen Design and sIgA-Driven Lactogenic Immunity.Veterinary sciences · 2026Review
- Development of an automated chemiluminescence immunoassay for detection of IgA antibodies against porcine epidemic diarrhea virus spike.BMC veterinary research · 2026Article
- Development of a Cellular Membrane Nanovesicle-Based Vaccine Against Porcine Epidemic Diarrhea Virus.Cells · 2026Article
- Genetic Diversity, Recombination, and Pathogenicity of Porcine Epidemic Diarrhea Virus Strains Circulating in China During 2023-2024.Transboundary and emerging diseases · 2026Article
- Precise mapping of two conserved minimal epitopes on the nucleocapsid protein of porcine epidemic diarrhea virus.Frontiers in microbiology · 2026Article
- The glycosylation variant at residue 381 of the spike protein contributes to virulence shifts in porcine epidemic diarrhea virus during both natural field transmission and laboratory cell passaging with poor cross-protection.Journal of virology · 2025Article
- G2c-Lineage Dominance and S1 Epitope-Glycan Drift of Porcine Epidemic Diarrhea Virus in Guangdong Province, China, 2022-2024.Veterinary sciences · 2025Article
- Prevalence and S gene characterization of porcine epidemic diarrhea virus in Sichuan province, China (2023-2024).Frontiers in veterinary science · 2025Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Porcine epidemic diarrhea virus (PEDV), a highly virulent enteric coronavirus, induces severe watery diarrhea and mortality in suckling piglets. The spike (S) protein, a critical mediator of viral entry, undergoes extensive N-linked glycosylation. To elucidate the functional significance of these post-translational modifications, we employed a reverse genetics system to generate 19 recombinant PEDV strains with single-site mutations at predicted N-glycosylation sites. In vitro experiments revealed that mutations at residues N118, N216, N726, N1232, and N1249 significantly attenuated viral replication and reduced plaque size. Our data demonstrated that these mutations impaired viral attachment and internalization. Importantly, in vivo pathogenicity assays in piglets indicated that the N1232Q and N1249Q mutants presented minimal faecal viral shedding and no clinical symptoms, suggesting their potential as live attenuated vaccine candidates. These findings underscore the critical role of S protein glycosylation in PEDV infectivity and virulence, providing a molecular basis for rational vaccine design.
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