ArticleJournal of virology2025
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.
Article in Journal of virology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
- Precise mapping of two conserved minimal epitopes on the nucleocapsid protein of porcine epidemic diarrhea virus.Frontiers in microbiology · 2026Article
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Authors and funding
13 authors.
Funding
Abstract
The virulence and immunogenicity of porcine epidemic diarrhea virus (PEDV) vary during field circulation and cell culture passage (such as when the GI CV777 strain is attenuated through serial passaging). This study revealed that the glycosylation site mutation at position 381 (N381K) of the S protein is associated with these phenomena. Compared with piglets inoculated with P13 virus, piglets inoculated with P100 (N381K) of virulent GX223 exhibited delayed diarrhea, viral shedding, and mortality. Using the virulent rCH/SX/2016-S IMPORTANCE: Porcine epidemic diarrhea virus (PEDV) continues to cause substantial economic losses in the global swine industry, with emerging strains challenging existing vaccine strategies. This study identifies the N381K glycosylation site mutation in the S protein of PEDV as a factor involved in variations in virulence during natural transmission and laboratory adaptation. Crucially, the mutant induces suboptimal neutralizing immunity against the prevalent strain, revealing a mechanism by which classical-strain vaccines may provide limited protection against currently circulating strains. Our findings reveal how a single glycan modification modulates both pathogenicity and immunogenicity, providing critical insights for the development of effective vaccines against circulating PEDV variants.
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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 OpenQuestion graph.