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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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Detalles Bibliográficos
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
Descripción
Sumario: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.