ArticleNature communications2020
NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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
33 citing papers in PubMed, 63 citations in OpenAlex.
- Differential innate immune activation by wild-type and NSs-deficient RVFV strains in human blood monocytes.Emerging microbes & infections · 2026Article
- Pathogenicity of Rift Valley fever virus: Organ-specific clinical outcomes and hidden drivers of virulence - a narrative review.Virulence · 2026Review
- Live-cell 3D-SIM of Rift Valley fever virus NSs filaments reveals a polygon web architecture.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Rift Valley fever virus activates multiple cell death pathways in neurons.Journal of virology · 2026Article
- Review
- NSs: the multifaceted bunyavirus virulence factor.Npj viruses · 2025Review
- Ultrastructural Insight into Rift Valley Fever Virus Pathogenesis in Different Human Cell Types.International journal of molecular sciences · 2025Article
- Review
- RVFV virulence factor NSs triggers the mitochondrial MCL-1-BAK axis to activate pathogenic NLRP3 pyroptosis.PLoS pathogens · 2024Article
- Promising Strategies to Reduce the SARS-CoV-2 Amyloid Deposition in the Brain and Prevent COVID-19-Exacerbated Dementia and Alzheimer's Disease.Pharmaceuticals (Basel, Switzerland) · 2024Review
- 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
- An Introduction to Rift Valley Fever Virus.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Cell-Free Synthesis of Bunyavirales Proteins in View of Their Structural Characterization by Nuclear Magnetic Resonance.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Use of Single-Domain Antibodies Against the NSm Protein for the Detection of Cells Infected by Rift Valley Fever Virus.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Imaging Bunyavirus Infections by Transmission Electron Microscopy: Conventional Sample Preparation vs High-Pressure Freezing and Freeze-Substitution.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Rift Valley fever virus modulates apoptosis and immune response during infection of human astrocytes.Emerging microbes & infections · 2023Article
- Rift Valley Fever Virus-Infection, Pathogenesis and Host Immune Responses.Pathogens (Basel, Switzerland) · 2023Review
- The phenuivirus Toscana virus makes an atypical use of vacuolar acidity to enter host cells.PLoS pathogens · 2023Article
- Perspectives of Next-Generation Live-Attenuated Rift Valley Fever Vaccines for Animal and Human Use.Vaccines · 2023Review
- Host-Pathogen Interactions Influencing Zoonotic Spillover Potential and Transmission in Humans.Viruses · 2023Review
Corrections and comments
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Authors and funding
16 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibrils result from the aggregation of host cell-encoded proteins, many giving rise to specific human illnesses such as Alzheimer's disease. Here we show that the major virulence factor of Rift Valley fever virus, the protein NSs, forms filamentous structures in the brain of mice and affects mortality. NSs assembles into nuclear and cytosolic disulfide bond-dependent fibrillary aggregates in infected cells. NSs structural arrangements exhibit characteristics typical for amyloids, such as an ultrastructure of 12 nm-width fibrils, a strong detergent resistance, and interactions with the amyloid-binding dye Thioflavin-S. The assembly dynamics of viral amyloid-like fibrils can be visualized in real-time. They form spontaneously and grow in an amyloid fashion within 5 hours. Together, our results demonstrate that viruses can encode amyloid-like fibril-forming proteins and have strong implications for future research on amyloid aggregation and toxicity in general.
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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.