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The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NPCORE, with or without a NPTAIL for nuclear transport

2019; Nature Portfolio; Volume: 9; Issue: 1 Linguagem: Inglês

10.1038/s41598-018-37306-y

2045-2322

Amélie Donchet, Justine Oliva, Alice Labaronne, Laura Tengo, Myriam Miloudi, Francine C. A. Gérard, Caroline Mas, Guy Schoehn, Rob W. H. Ruigrok, Mariette Ducatez, Thibaut Crépin,

RNA Research and Splicing

Abstract 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.