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The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NP(CORE), with or without a NP(TAIL) for nuclear transport

This paper focuses on the nucleoprotein (NP) of the newly identified member of the Orthomyxoviridae family, Influenza D virus. To date several X-ray structures of NP of Influenza A (A/NP) and B (B/NP) viruses and of infectious salmon anemia (ISA/NP) virus have been solved. Here we purified, characte...

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Autores principales: Donchet, Amélie, Oliva, Justine, Labaronne, Alice, Tengo, Laura, Miloudi, Myriam, C.A. Gerard, Francine, Mas, Caroline, Schoehn, Guy, W.H. Ruigrok, Rob, Ducatez, Mariette, Crépin, Thibaut
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6346101/
https://www.ncbi.nlm.nih.gov/pubmed/30679709
http://dx.doi.org/10.1038/s41598-018-37306-y
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author Donchet, Amélie
Oliva, Justine
Labaronne, Alice
Tengo, Laura
Miloudi, Myriam
C.A. Gerard, Francine
Mas, Caroline
Schoehn, Guy
W.H. Ruigrok, Rob
Ducatez, Mariette
Crépin, Thibaut
author_facet Donchet, Amélie
Oliva, Justine
Labaronne, Alice
Tengo, Laura
Miloudi, Myriam
C.A. Gerard, Francine
Mas, Caroline
Schoehn, Guy
W.H. Ruigrok, Rob
Ducatez, Mariette
Crépin, Thibaut
author_sort Donchet, Amélie
collection PubMed
description This paper focuses on the nucleoprotein (NP) of the newly identified member of the Orthomyxoviridae family, Influenza D virus. To date several X-ray structures of NP of Influenza A (A/NP) and B (B/NP) viruses and of infectious salmon anemia (ISA/NP) virus have been solved. Here we purified, characterized and solved the X-ray structure of the tetrameric D/NP at 2.4 Å resolution. The crystal structure of its core is similar to NP of other Influenza viruses. However, unlike A/NP and B/NP which possess a flexible amino-terminal tail containing nuclear localization signals (NLS) for their nuclear import, D/NP possesses a carboxy-terminal tail (D/NP(TAIL)). We show that D/NP(TAIL) harbors a bipartite NLS and designed C-terminal truncated mutants to demonstrate the role of D/NP(TAIL) for nuclear transport.
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spelling pubmed-63461012019-01-29 The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NP(CORE), with or without a NP(TAIL) for nuclear transport Donchet, Amélie Oliva, Justine Labaronne, Alice Tengo, Laura Miloudi, Myriam C.A. Gerard, Francine Mas, Caroline Schoehn, Guy W.H. Ruigrok, Rob Ducatez, Mariette Crépin, Thibaut Sci Rep Article This paper focuses on the nucleoprotein (NP) of the newly identified member of the Orthomyxoviridae family, Influenza D virus. To date several X-ray structures of NP of Influenza A (A/NP) and B (B/NP) viruses and of infectious salmon anemia (ISA/NP) virus have been solved. Here we purified, characterized and solved the X-ray structure of the tetrameric D/NP at 2.4 Å resolution. The crystal structure of its core is similar to NP of other Influenza viruses. However, unlike A/NP and B/NP which possess a flexible amino-terminal tail containing nuclear localization signals (NLS) for their nuclear import, D/NP possesses a carboxy-terminal tail (D/NP(TAIL)). We show that D/NP(TAIL) harbors a bipartite NLS and designed C-terminal truncated mutants to demonstrate the role of D/NP(TAIL) for nuclear transport. Nature Publishing Group UK 2019-01-24 /pmc/articles/PMC6346101/ /pubmed/30679709 http://dx.doi.org/10.1038/s41598-018-37306-y Text en © The Author(s) 2019 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
Donchet, Amélie
Oliva, Justine
Labaronne, Alice
Tengo, Laura
Miloudi, Myriam
C.A. Gerard, Francine
Mas, Caroline
Schoehn, Guy
W.H. Ruigrok, Rob
Ducatez, Mariette
Crépin, Thibaut
The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NP(CORE), with or without a NP(TAIL) for nuclear transport
title The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NP(CORE), with or without a NP(TAIL) for nuclear transport
title_full The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NP(CORE), with or without a NP(TAIL) for nuclear transport
title_fullStr The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NP(CORE), with or without a NP(TAIL) for nuclear transport
title_full_unstemmed The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NP(CORE), with or without a NP(TAIL) for nuclear transport
title_short The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NP(CORE), with or without a NP(TAIL) for nuclear transport
title_sort structure of the nucleoprotein of influenza d shows that all orthomyxoviridae nucleoproteins have a similar np(core), with or without a np(tail) for nuclear transport
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6346101/
https://www.ncbi.nlm.nih.gov/pubmed/30679709
http://dx.doi.org/10.1038/s41598-018-37306-y
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