tetano
Editor, Senior Moderator
Acta Crystallogr F Struct Biol Commun
. 2021 Jul 1;77(Pt 7):208-214.
doi: 10.1107/S2053230X2100635X. Epub 2021 Jun 29.
Structure of an H3N2 influenza virus nucleoprotein
Michael L Knight[SUP] 1 [/SUP], Haitian Fan[SUP] 1 [/SUP], David L V Bauer[SUP] 2 [/SUP], Jonathan M Grimes[SUP] 3 [/SUP], Ervin Fodor[SUP] 1 [/SUP], Jeremy R Keown[SUP] 3 [/SUP]
Affiliations
Abstract
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.
Keywords: H3N2 influenza virus nucleoprotein; RNA-binding protein; X-ray crystallography; influenza; nucleoprotein.
. 2021 Jul 1;77(Pt 7):208-214.
doi: 10.1107/S2053230X2100635X. Epub 2021 Jun 29.
Structure of an H3N2 influenza virus nucleoprotein
Michael L Knight[SUP] 1 [/SUP], Haitian Fan[SUP] 1 [/SUP], David L V Bauer[SUP] 2 [/SUP], Jonathan M Grimes[SUP] 3 [/SUP], Ervin Fodor[SUP] 1 [/SUP], Jeremy R Keown[SUP] 3 [/SUP]
Affiliations
- PMID: 34196611
- DOI: 10.1107/S2053230X2100635X
Abstract
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.
Keywords: H3N2 influenza virus nucleoprotein; RNA-binding protein; X-ray crystallography; influenza; nucleoprotein.