tetano
Editor, Senior Moderator
Sci Rep. 2019 Jan 24;9(1):600. doi: 10.1038/s41598-018-37306-y.
[h=1]The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NP[SUB]CORE[/SUB], with or without a NP[SUB]TAIL[/SUB] for nuclear transport.[/h] Donchet A[SUP]1[/SUP], Oliva J[SUP]2[/SUP], Labaronne A[SUP]1[/SUP], Tengo L[SUP]1[/SUP], Miloudi M[SUP]1[/SUP], C A Gerard F[SUP]1[/SUP], Mas C[SUP]3[/SUP], Schoehn G[SUP]1[/SUP], W H Ruigrok R[SUP]1[/SUP], Ducatez M[SUP]2[/SUP], Cr?pin T[SUP]4[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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 ? 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[SUB]TAIL[/SUB]). We show that D/NP[SUB]TAIL[/SUB] harbors a bipartite NLS and designed C-terminal truncated mutants to demonstrate the role of D/NP[SUB]TAIL[/SUB] for nuclear transport.
PMID: 30679709 DOI: 10.1038/s41598-018-37306-y
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[h=1]The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NP[SUB]CORE[/SUB], with or without a NP[SUB]TAIL[/SUB] for nuclear transport.[/h] Donchet A[SUP]1[/SUP], Oliva J[SUP]2[/SUP], Labaronne A[SUP]1[/SUP], Tengo L[SUP]1[/SUP], Miloudi M[SUP]1[/SUP], C A Gerard F[SUP]1[/SUP], Mas C[SUP]3[/SUP], Schoehn G[SUP]1[/SUP], W H Ruigrok R[SUP]1[/SUP], Ducatez M[SUP]2[/SUP], Cr?pin T[SUP]4[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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 ? 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[SUB]TAIL[/SUB]). We show that D/NP[SUB]TAIL[/SUB] harbors a bipartite NLS and designed C-terminal truncated mutants to demonstrate the role of D/NP[SUB]TAIL[/SUB] for nuclear transport.
PMID: 30679709 DOI: 10.1038/s41598-018-37306-y
Free full text