ArticleJournal of virology2025
Targeting USP22 to promote K63-linked ubiquitination and degradation of SARS-CoV-2 nucleocapsid protein.
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 3 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
3 citing papers in PubMed.
- The landscape of protein post-translational modifications in the pathogenesis of acute respiratory distress syndrome.Journal of thoracic disease · 2026Review
- Roles of ubiquitin‑specific peptidase 22 in cellular fate: From embryonic survival to tissue repair, inflammation and metabolism (Review).International journal of molecular medicine · 2026Review
- Endosomal maturation leads to nucleocapsid conformation change in seasonal coronaviruses.Nagoya journal of medical science · 2026Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) generally hijacks the cellular machinery of host cells for survival. However, how SARS-CoV-2 employs the host's deubiquitinase to facilitate virus replication remains largely unknown. In this study, we identified the host deubiquitinase USP22 as a crucial regulator of the expression of SARS-CoV-2 nucleocapsid protein (SARS-CoV-2 NP), which is essential for SARS-CoV-2 replication. We demonstrated that SARS-CoV-2 NP proteins undergo ubiquitination-dependent degradation in host cells, while USP22 interacts with SARS-CoV-2 NP and downregulates K63-linked polyubiquitination of SARS-CoV-2 NP, thereby protecting SARS-CoV-2 NP from degradation. Importantly, we further revealed that sulbactam, an antibiotic, can reduce USP22 protein levels, eventually promoting the degradation of SARS-CoV-2 NP
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Registered trials
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