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.
https://hal-pasteur.archives-ouvertes.fr/pasteur-02949167 Contributor : Xavier MONTAGUTELLIConnect in order to contact the contributor Submitted on : Friday, September 25, 2020 - 1:50:44 PM Last modification on : Tuesday, May 31, 2022 - 11:34:02 AM Long-term archiving on: : Thursday, December 3, 2020 - 5:52:25 PM
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, Nature Publishing Group, 2020, 11 (1), pp.3281. ⟨10.1038/s41467-020-17101-y⟩. ⟨pasteur-02949167⟩