ArticleVeterinary research2025
Porcine reproductive and respiratory syndrome virus NSP5 exploited UBE2L6 to promote viral replication via antagonising host RLRs and ISGylation.
Article in Veterinary research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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Who cites it
4 citing papers in PubMed.
- Autophagy and ubiquitination in important swine viral infections: Host defense and viral antagonism.Virulence · 2026Review
- RNF187 inhibits porcine reproductive and respiratory syndrome virus replication by recruiting the autophagy receptor NDP52 to degrade nsp12.Veterinary research · 2026Article
- Porcine Reproductive and Respiratory Syndrome Virus NSP8 Suppresses NF-κB Signaling by Hijacking Host UBE2K and IKKα.Viruses · 2026Article
- PRRSV suppresses ER-phagy through Nsp2- and Nsp5-mediated degradation of FAM134B.Frontiers in cellular and infection microbiology · 2026Article
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Authors and funding
9 authors.
Funding
Abstract
Porcine reproductive and respiratory syndrome virus (PRRSV) inhibits the host innate immune response to promote its replication. The ubiquitin-proteasome system (UPS) and ISGylation both play roles in modulating host innate immunity. Within this process, ISG15-conjugating enzyme E2L6 (UBE2L6) functions as an E2 ubiquitin/ISG15-conjugating enzyme, which is crucial for the enzymatic cascades of UPS and ISGylation. However, the role of UBE2L6 during PRRSV infection remains unclear. Here, we report that UBE2L6 was up-regulated at both the transcript and protein levels during PRRSV infection. Overexpression of UBE2L6 facilitated PRRSV replication, whereas knockdown of UBE2L6 reduced viral replication. Mechanistically, UBE2L6 promoted the degradation of RIG-I and MDA5 protein expression via the ubiquitin-proteasome pathway and decreased ISGylation levels during PRRSV infection, thereby inhibiting the expression of type I interferons and interferon-stimulated genes (ISGs). In addition, UBE2L6 interacted with PRRSV NSP5 and stabilised the NSP5 protein. Together, PRRSV NSP5 and UBE2L6 further facilitated the degradation of RIG-I and MDA5 via the K48-linked ubiquitination pathway, ultimately facilitating PRRSV replication. Notably, UBE2L6 had minimal impact on RIG-I and MDA5 expression in the absence of PRRSV infection. In summary, UBE2L6 regulated host innate immunity and viral replication through its ubiquitination and ubiquitination-like functions. These findings provide novel insights into how PRRSV NSP5 exploits the host UPS to inhibit the innate immune response and deepen our understanding of the mechanism of host-virus interaction.
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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 OpenQuestion graph.