4.0 Article

Structure of an H3N2 influenza virus nucleoprotein

Publisher

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X2100635X

Keywords

influenza; H3N2 influenza virus nucleoprotein; X-ray crystallography; nucleoprotein; RNA-binding protein

Funding

  1. Medical Research Council [MR/R009945/1]
  2. Biotechnology and Biological Sciences Research Council (BBSRC) [BB/M011224/1]
  3. Wellcome Investigator Award [200835/Z/16/Z]
  4. Wellcome Trust [200835/Z/16/Z, FC011104]
  5. Francis Crick Institute from Cancer Research UK [FC011104]
  6. UK Medical Research Council [FC011104]
  7. MRC [MR/R009945/1] Funding Source: UKRI
  8. Wellcome Trust [200835/Z/16/Z] Funding Source: Wellcome Trust

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The study presents the structure of the NP from an H3N2 virus, which is highly similar to NPs from other virus subtypes but with key differences, which may enhance understanding of the structural conservation of influenza NPs.
Influenza A viruses of the H1N1 and H3N2 subtypes are responsible for seasonal epidemic events. The influenza nucleoprotein (NP) binds to the viral genomic RNA and is essential for its replication. Efforts are under way to produce therapeutics and vaccines targeting the NP. Despite this, no structure of an NP from an H3N2 virus has previously been determined. Here, the structure of the A/Northern Territory/60/1968 (H3N2) influenza virus NP is presented at 2.2 angstrom resolution. The structure is highly similar to those of the A/WSN/1933 (H1N1) and A/Hong Kong/483/97 (H5N1) NPs. Nonconserved amino acids are widely dispersed both at the sequence and structural levels. A movement of the 73-90 RNA-binding loop is observed to be the key difference between the structure determined here and previous structures. The data presented here increase the understanding of structural conservation amongst influenza NPs and may aid in the design of universal interventions against influenza.

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