Cargando…
NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice
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...
Autores principales: | , , , , , , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7329897/ https://www.ncbi.nlm.nih.gov/pubmed/32612175 http://dx.doi.org/10.1038/s41467-020-17101-y |
_version_ | 1783552996587601920 |
---|---|
author | Léger, Psylvia Nachman, Eliana Richter, Karsten Tamietti, Carole Koch, Jana Burk, Robin Kummer, Susann Xin, Qilin Stanifer, Megan Bouloy, Michèle Boulant, Steeve Kräusslich, Hans-Georg Montagutelli, Xavier Flamand, Marie Nussbaum-Krammer, Carmen Lozach, Pierre-Yves |
author_facet | Léger, Psylvia Nachman, Eliana Richter, Karsten Tamietti, Carole Koch, Jana Burk, Robin Kummer, Susann Xin, Qilin Stanifer, Megan Bouloy, Michèle Boulant, Steeve Kräusslich, Hans-Georg Montagutelli, Xavier Flamand, Marie Nussbaum-Krammer, Carmen Lozach, Pierre-Yves |
author_sort | Léger, Psylvia |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7329897 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-73298972020-07-06 NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice Léger, Psylvia Nachman, Eliana Richter, Karsten Tamietti, Carole Koch, Jana Burk, Robin Kummer, Susann Xin, Qilin Stanifer, Megan Bouloy, Michèle Boulant, Steeve Kräusslich, Hans-Georg Montagutelli, Xavier Flamand, Marie Nussbaum-Krammer, Carmen Lozach, Pierre-Yves Nat Commun Article 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. Nature Publishing Group UK 2020-07-01 /pmc/articles/PMC7329897/ /pubmed/32612175 http://dx.doi.org/10.1038/s41467-020-17101-y Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Léger, Psylvia Nachman, Eliana Richter, Karsten Tamietti, Carole Koch, Jana Burk, Robin Kummer, Susann Xin, Qilin Stanifer, Megan Bouloy, Michèle Boulant, Steeve Kräusslich, Hans-Georg Montagutelli, Xavier Flamand, Marie Nussbaum-Krammer, Carmen Lozach, Pierre-Yves NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice |
title | NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice |
title_full | NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice |
title_fullStr | NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice |
title_full_unstemmed | NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice |
title_short | NSs amyloid formation is associated with the virulence of Rift Valley fever virus in mice |
title_sort | nss amyloid formation is associated with the virulence of rift valley fever virus in mice |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7329897/ https://www.ncbi.nlm.nih.gov/pubmed/32612175 http://dx.doi.org/10.1038/s41467-020-17101-y |
work_keys_str_mv | AT legerpsylvia nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT nachmaneliana nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT richterkarsten nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT tamietticarole nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT kochjana nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT burkrobin nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT kummersusann nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT xinqilin nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT stanifermegan nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT bouloymichele nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT boulantsteeve nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT krausslichhansgeorg nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT montagutellixavier nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT flamandmarie nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT nussbaumkrammercarmen nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice AT lozachpierreyves nssamyloidformationisassociatedwiththevirulenceofriftvalleyfevervirusinmice |