Structure of an H3N2 influenza virus nucleoprotein
- Resource Type
- Authors
- Haitian Fan; David L.V. Bauer; J.R. Keown; Jonathan M. Grimes; Michael L. Knight; Ervin Fodor
- Source
- Acta Crystallographica. Section F, Structural Biology Communications
- Subject
- Universal interventions
RNA-binding protein
viruses
Biophysics
Biology
H3N2 influenza virus nucleoprotein
Crystallography, X-Ray
medicine.disease_cause
Biochemistry
Protein Structure, Secondary
Virus
Research Communications
03 medical and health sciences
Structural Biology
Influenza, Human
Genetics
medicine
Humans
Amino Acid Sequence
X-ray crystallography
nucleoprotein
030304 developmental biology
0303 health sciences
Influenza A Virus, H3N2 Subtype
030302 biochemistry & molecular biology
virus diseases
Influenza a
Condensed Matter Physics
Virology
Influenza A virus subtype H5N1
Protein Structure, Tertiary
Nucleoprotein
Nucleoproteins
Influenza virus nucleoprotein
influenza
Genomic rna
- Language
- ISSN
- 2053-230X
The influenza virus nucleoprotein binds to the viral RNA genome and is essential for virus replication. Here, the structure of the nucleoprotein from an H3N2 virus is presented at 2.2 Å resolution.
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 Å 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.