ArticleProceedings of the National Academy of Sciences of the United States of America2015
A ΩXaV motif in the Rift Valley fever virus NSs protein is essential for degrading p62, forming nuclear filaments and virulence.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 39 citations in OpenAlex.
- From Hepatitis to Encephalitis: Neuroinvasion and Antiviral Development in Rift Valley Fever Virus Infection.Pathogens (Basel, Switzerland) · 2026Review
- Review
- Comparative study of two Rift Valley fever virus field strains originating from Mauritania.PLoS neglected tropical diseases · 2024Article
- Review
- An LIR motif in the Rift Valley fever virus NSs protein is critical for the interaction with LC3 family members and inhibition of autophagy.PLoS pathogens · 2024Article
- Innate immune response against vector-borne bunyavirus infection and viral countermeasures.Frontiers in cellular and infection microbiology · 2024Review
- Structural polymorphism of the PH domain in TFIIH.Bioscience reports · 2023Article
- Natural hosts and animal models for Rift Valley fever phlebovirus.Frontiers in veterinary science · 2023Review
- Dynamic structures of intrinsically disordered proteins related to the general transcription factor TFIIH, nucleosomes, and histone chaperones.Biophysical reviews · 2022Review
- Harnessing Rift Valley fever virus NSs gene for cancer gene therapy.Cancer gene therapy · 2022Article
- Article
- Viral evasion of the integrated stress response through antagonism of eIF2-P binding to eIF2B.Nature communications · 2021Article
- Review
- NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice.Nature communications · 2020Article
- Article
- Review
- The essential and multifunctional TFIIH complex.Protein science : a publication of the Protein Society · 2018Review
- Phosphoproteomic analysis reveals Smad protein family activation following Rift Valley fever virus infection.PloS one · 2018Article
- Alterations in the host transcriptome in vitro following Rift Valley fever virus infection.Scientific reports · 2017Article
- Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Rift Valley fever virus (RVFV) is a single-stranded RNA virus capable of inducing fatal hemorrhagic fever in humans. A key component of RVFV virulence is its ability to form nuclear filaments through interactions between the viral nonstructural protein NSs and the host general transcription factor TFIIH. Here, we identify an interaction between a ΩXaV motif in NSs and the p62 subunit of TFIIH. This motif in NSs is similar to ΩXaV motifs found in nucleotide excision repair (NER) factors and transcription factors known to interact with p62. Structural and biophysical studies demonstrate that NSs binds to p62 in a similar manner as these other factors. Functional studies in RVFV-infected cells show that the ΩXaV motif is required for both nuclear filament formation and degradation of p62. Consistent with the fact that the RVFV can be distinguished from other Bunyaviridae-family viruses due to its ability to form nuclear filaments in infected cells, the motif is absent in the NSs proteins of other Bunyaviridae-family viruses. Taken together, our studies demonstrate that p62 binding to NSs through the ΩXaV motif is essential for degrading p62, forming nuclear filaments and enhancing RVFV virulence. In addition, these results show how the RVFV incorporates a simple motif into the NSs protein that enables it to functionally mimic host cell proteins that bind the p62 subunit of TFIIH.
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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.