Skip to Main content Skip to Navigation
New interface
Journal articles

NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice

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.
Document type :
Journal articles
Complete list of metadata

Cited literature [51 references]  Display  Hide  Download
Contributor : Xavier MONTAGUTELLI Connect in order to contact the contributor
Submitted on : Friday, September 25, 2020 - 1:50:44 PM
Last modification on : Wednesday, September 28, 2022 - 4:20:12 PM
Long-term archiving on: : Thursday, December 3, 2020 - 5:52:25 PM


Distributed under a Creative Commons Attribution 4.0 International License




Psylvia Léger, Eliana Nachman, Karsten Richter, Carole Tamietti, Jana Koch, et al.. NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice. Nature Communications, 2020, 11 (1), pp.3281. ⟨10.1038/s41467-020-17101-y⟩. ⟨pasteur-02949167⟩



Record views


Files downloads