ArticleVirology journal2024
Pseudorabies virus UL38 attenuates the cGAS-STING signaling pathway by recruiting Tollip to promote STING for autophagy degradation.
Article in Virology journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The trial behind it
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Who cites it
10 citing papers in PubMed.
- The cGAS-STING/MITA pathway in innate antiviral immunity and beyond.Cell insight · 2026Review
- Boosting the immune response and protective efficacy of inactivated PRV vaccine using cGAMP as a mucosal adjuvant.BMC veterinary research · 2026Article
- STING agonists as antiviral agents.FEBS letters · 2026Review
- Fish TOLLIP manipulates ATG5 for autophagic degradation of STING to attenuate antiviral interferon responses.PLoS pathogens · 2025Article
- Tollip deficiency enhances mitophagy and reduces STING activation in influenza A virus-infected mice.Journal of immunology (Baltimore, Md. : 1950) · 2025Article
- Rosmarinic Acid inhibits Pseudorabies Virus (PRV) infection by activating the cGAS-STING signaling pathway.BMC microbiology · 2025Article
- Grass carp reovirus VP4 manipulates TOLLIP to degrade STING for inhibition of IFN production.Journal of virology · 2025Article
- Review
- Alphaherpesvirus in Pets and Livestock.Microorganisms · 2025Review
- Evasion of the Antiviral Innate Immunity by PRV.International journal of molecular sciences · 2024Review
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Natural immunity is the first defense line of the host immune system, which plays a significant role in combating foreign pathogenic microorganisms. The IFN-β (interferon-beta) signaling pathway, being a typical example of innate immunity, plays a vital function. This study aimed to elucidate the function of pseudorabies virus (PRV) UL38 protein (unique long region 38) in suppressing the activation of the IFN-β signaling pathway. The findings from our study indicate that the PRV UL38 protein effectively hampers the activation of IFN-β by poly (dA: dT) (poly(deoxyadenylic-deoxythymidylic)) and 2'3'-cGAMP (2'-3'-cyclic GMP-AMP). Furthermore, UL38 exhibits spatial co-localization with STING (stimulator of interferon genes) and effectively hinders STING dimerization. Subsequently, STING was downgraded to suppress the production of IFN-β and ISGs (interferon stimulated genes). Immunoprecipitation analysis revealed that the interaction between UL38 and STING, which subsequently initiated the degradation of STING via selective autophagy mediated by TOLLIP (toll interacting protein). To summarize, this research elucidates the function of UL38 in counteracting the cGAS (cGAMP synthase)-STING-induced IFN-β pathway. The PRV UL38 protein may attenuate the activation of IFN-β as a means of regulating the virus's persistence in the host.
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Registered trials
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 Socratic graph.