Structure of an H3N2 influenza virus nucleoprotein

被引：9

作者：

Knight, Michael L. ^{[1
]}

Fan, Haitian ^{[1
]}

Bauer, David L., V ^{[2
]}

Grimes, Jonathan M. ^{[3
]}

Fodor, Ervin ^{[1
]}

Keown, Jeremy R. ^{[3
]}

机构：

[1] Univ Oxford, Sir William Dunn Sch Pathol, South Parks Rd, Oxford OX1 3RE, England

[2] Francis Crick Inst, RNA Virus Replicat Lab, Midland Rd, London NW1 1AT, England

[3] Univ Oxford, Welcome Ctr Human Genet, Div Struct Biol, Roosevelt Dr, Oxford OX3 7BN, England

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2021年 / 77卷

基金：

英国惠康基金; 英国医学研究理事会; 英国生物技术与生命科学研究理事会;

关键词：

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

D O I：

10.1107/S2053230X2100635X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：208 / 214

页数：7

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