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

Psylvia Léger, Eliana Nachman, Karsten Richter, Carole Tamietti, Jana Koch, Robin Burk, Susann Kummer, Qilin Xin, Megan Stanifer, Michèle Bouloy, Steeve Boulant, Hans-Georg Kräusslich, Xavier Montagutelli, Marie Flamand, Carmen Nussbaum-Krammer and Pierre-Yves Lozach ()
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Psylvia Léger: CellNetworks—Cluster of Excellence and Virology, University Hospital Heidelberg
Eliana Nachman: Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance
Karsten Richter: DKFZ
Carole Tamietti: Structural Virology, Institut Pasteur
Jana Koch: CellNetworks—Cluster of Excellence and Virology, University Hospital Heidelberg
Robin Burk: Center for Integrative Infectious Diseases Research (CIID), Virology, University Hospital Heidelberg
Susann Kummer: Center for Integrative Infectious Diseases Research (CIID), Virology, University Hospital Heidelberg
Qilin Xin: University Lyon, INRAE, EPHE, IVPC
Megan Stanifer: Center for Integrative Infectious Diseases Research (CIID), Virology, University Hospital Heidelberg
Michèle Bouloy: Unité de Génétique Moléculaire des Bunyavirus, Institut Pasteur
Steeve Boulant: Center for Integrative Infectious Diseases Research (CIID), Virology, University Hospital Heidelberg
Hans-Georg Kräusslich: Center for Integrative Infectious Diseases Research (CIID), Virology, University Hospital Heidelberg
Xavier Montagutelli: Mouse Genetics Laboratory, Institut Pasteur
Marie Flamand: Structural Virology, Institut Pasteur
Carmen Nussbaum-Krammer: Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance
Pierre-Yves Lozach: CellNetworks—Cluster of Excellence and Virology, University Hospital Heidelberg

Nature Communications, 2020, vol. 11, issue 1, 1-19

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-17101-y

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