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Molecular Organisation of Tick-Borne Encephalitis Virus
Lauri I A Pulkkinen1,2, Sarah V Barrass1,2, Aušra Domanska1,2
1Faculty of Biological and Environmental Sciences, Molecular and Integrative Bioscience Research Programme, University of Helsinki, 00014 Helsinki, Finland.
Viruses
|April 23, 2022
Summary
This study reveals the cryo-electron microscopy structure of tick-borne encephalitis virus (TBEV), detailing its M protein conformational changes and lipid interactions crucial for viral assembly and stability.
Area of Science:
- Virology
- Structural Biology
- Molecular Microbiology
Background:
- Tick-borne encephalitis virus (TBEV) is a significant flavivirus pathogen.
- Structural data on tick-borne flaviviruses are limited compared to mosquito-borne counterparts.
- Understanding TBEV virion structure is key to comprehending its pathogenesis.
Purpose of the Study:
- To determine the high-resolution cryo-electron microscopy (cryo-EM) structure of the TBEV virion.
- To elucidate the molecular mechanisms underlying TBEV architecture and stability.
- To identify key interactions, including M protein dynamics and lipid binding, important for TBEV assembly.
Main Methods:
- Cryo-electron microscopy (cryo-EM) at 3.3 Å resolution.
- Analysis of viral protein (M and E proteins) structures and interactions.
- Identification and characterization of lipid molecules within the virion.
Main Results:
- A detailed 3.3 Å cryo-EM structure of the TBEV Kuutsalo-14 isolate was obtained.
- Conformational switching in M protein peripheral and transmembrane helices was observed, explaining protein packing.
- Highly conserved M protein interaction residues in TBEV were identified, potentially compensating for fewer E protein hydrogen bonds.
- Two lipids bound within the E protein were visualized, similar to those in other flaviviruses, and are implicated in virus assembly.
Conclusions:
- The TBEV structure provides insights into tick-borne flavivirus architecture.
- M protein conformational flexibility and specific interactions are critical for virion stability.
- Lipid interactions within the E protein play a role in TBEV assembly, offering potential targets for antiviral strategies.
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