Molecular Organisation of Tick-Borne Encephalitis Virus

被引:30
作者
Pulkkinen, Lauri I. A. [1 ,2 ]
Barrass, Sarah, V [1 ,2 ]
Domanska, Ausra [1 ,2 ]
Overby, Anna K. [3 ,4 ]
Anastasina, Maria [1 ,2 ]
Butcher, Sarah J. [1 ,2 ]
机构
[1] Univ Helsinki, Fac Biol & Environm Sci, Mol & Integrat Biosci Res Programme, Helsinki 00014, Finland
[2] Univ Helsinki, Helsinki Inst Life Sci, Inst Biotechnol, Helsinki 00014, Finland
[3] Umea Univ, Fac Med, Dept Clin Microbiol, S-90185 Umea, Sweden
[4] Umea Univ, Lab Mol Infect Med Sweden MIMS, S-90185 Umea, Sweden
来源
VIRUSES-BASEL | 2022年 / 14卷 / 04期
基金
芬兰科学院; 瑞典研究理事会;
关键词
tick-borne encephalitis virus; cryo-electron microscopy; TBEV; envelope protein; membrane protein; lipid factor; glycoprotein; quasi-equivalence; LAMININ-BINDING PROTEIN; CATION-PI INTERACTIONS; ENVELOPE GLYCOPROTEIN; MEMBRANE CURVATURE; GLYCOSYLATION; SEQUENCE; CARBOHYDRATE; RESOLUTION; SECRETION; IMMATURE;
D O I
10.3390/v14040792
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Tick-borne encephalitis virus (TBEV) is a pathogenic, enveloped, positive-stranded RNA virus in the family Flaviviridae. Structural studies of flavivirus virions have primarily focused on mosquito-borne species, with only one cryo-electron microscopy (cryo-EM) structure of a tick-borne species published. Here, we present a 3.3 angstrom cryo-EM structure of the TBEV virion of the Kuutsalo-14 isolate, confirming the overall organisation of the virus. We observe conformational switching of the peripheral and transmembrane helices of M protein, which can explain the quasi-equivalent packing of the viral proteins and highlights their importance in stabilising membrane protein arrangement in the virion. The residues responsible for M protein interactions are highly conserved in TBEV but not in the structurally studied Hypr strain, nor in mosquito-borne flaviviruses. These interactions may compensate for the lower number of hydrogen bonds between E proteins in TBEV compared to the mosquito-borne flaviviruses. The structure reveals two lipids bound in the E protein which are important for virus assembly. The lipid pockets are comparable to those recently described in mosquito-borne Zika, Spondweni, Dengue, and Usutu viruses. Our results thus advance the understanding of tick-borne flavivirus architecture and virion-stabilising interactions.
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页数:17
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