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

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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Publication Details

Journal
Journal of Virology
Published
2025-11-24
DOI
https://doi.org/10.1128/jvi.01561-25
Citations
1
Primary Topic
Animal Virus Infections Studies
Type
article
Field-Weighted Citation Impact
1.19
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article

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

Yong‐Hui Zheng, Yang Li, Shuqi Xiao, Xuyang Guo et al.
1 citations
Journal of Virology
Animal Virus Infections Studies
1.19
article

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

Yong‐Hui Zheng, Yang Li, Shuqi Xiao, Xuyang Guo, Lele Xu, Zifang Zheng, Zhiwei Li, Haixue Zheng, Yongqi Li, Jianwu Zhang, Yingtong Feng, Zhiqian Ma, Xiaojing Zhao
article en
1 citations

Abstract

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.

Journal of VirologyVol. 99(12)
Gansu Academy of Agricultural Sciences (CN), Lanzhou Veterinary Research Institute (CN), Chinese Academy of Agricultural Sciences (CN), Lanzhou University (CN)
Openalex Percentile: Top 18%
Animal Virus Infections Studies
1.19
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