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

Sci Rep. 2019 Jan 24;9(1):600. doi: 10.1038/s41598-018-37306-y.

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/NPTAIL). We show that D/NPTAIL harbors a bipartite NLS and designed C-terminal truncated mutants to demonstrate the role of D/NPTAIL for nuclear transport.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus
  • Amino Acid Sequence
  • Cell Nucleus / metabolism*
  • Crystallography, X-Ray
  • HEK293 Cells
  • Humans
  • Nucleoproteins / chemistry*
  • Nucleoproteins / genetics
  • Nucleoproteins / metabolism
  • Orthomyxoviridae / metabolism*
  • Protein Binding
  • Protein Structure, Quaternary
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Sequence Alignment
  • Thogotovirus / metabolism*
  • alpha Karyopherins / metabolism

Substances

  • Nucleoproteins
  • Recombinant Proteins
  • alpha Karyopherins