ArticleJournal of virology2026
E3 ubiquitin ligase NEDD4 inhibits PEDV infection through ubiquitination and degradation of the viral primase NSP8.
Article in Journal of virology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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
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Who cites it
2 citing papers in PubMed.
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Authors and funding
16 authors.
Funding
Abstract
Porcine epidemic diarrhea virus (PEDV), a highly lethal alpha coronavirus, primarily infects piglet intestines, yet the role of the intestinal homeostasis regulator NEDD4-a HECT-family E3 ubiquitin ligase-in PEDV infection was previously unknown. This study reveals that NEDD4 inhibits PEDV infection by mediating K63-linked ubiquitination of the viral primase NSP8, targeting a conserved lysine (K170) within an NEDD4-recognized SPP motif. The C2 domain of NEDD4 is critical for this antiviral activity, as deletion of its RDDFLGQVDVPLYPLPT exon abolishes PEDV suppression and disrupts NSP8 binding, with AlphaFold3 structural modeling showing this deletion induces conformational changes at the C2-WW interdomain junction. PEDV infection upregulates NEDD4 expression
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Registered trials
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