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7Z51

Tick-borne encephalitis virus Kuutsalo-14

Summary for 7Z51
Entry DOI10.2210/pdb7z51/pdb
EMDB information14512
DescriptorEnvelope protein E, Small envelope protein M, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordsvirion, membrane protein, glycoprotein, virus
Biological sourceTick-borne encephalitis virus (WESTERN SUBTYPE)
More
Total number of polymer chains6
Total formula weight191870.36
Authors
Pulkkinen, L.I.A.,Barrass, S.V.,Anastasina, M.,Butcher, S.J. (deposition date: 2022-03-07, release date: 2022-04-20, Last modification date: 2024-10-23)
Primary citationPulkkinen, L.I.A.,Barrass, S.V.,Domanska, A.,Overby, A.K.,Anastasina, M.,Butcher, S.J.
Molecular Organisation of Tick-Borne Encephalitis Virus.
Viruses, 14:-, 2022
Cited by
PubMed Abstract: Tick-borne encephalitis virus (TBEV) is a pathogenic, enveloped, positive-stranded RNA virus in the family . 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 Å 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.
PubMed: 35458522
DOI: 10.3390/v14040792
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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