5O6A

The cryo-EM structure of Tick-borne encephalitis virus mature particle

Summary for 5O6A

• Entry DOI: 10.2210/pdb5o6a/pdb
• EMDB information: 3752
• Descriptor: Envelope protein, Small envelope protein M, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: tick-borne encephalitis virus, mature particle, cryo-em, virus
• Biological source: Tick-borne encephalitis virus (strain Hypr) (TBEV); More
• Total number of polymer chains: 6
• Total formula weight: 186685.48

Authors

Fuzik, T.,Plevka, P. (deposition date: 2017-06-06, release date: 2018-02-07, Last modification date: 2024-11-20)

Primary citation

Fuzik, T.,Formanova, P.,Ruzek, D.,Yoshii, K.,Niedrig, M.,Plevka, P.
Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody.
Nat Commun, 9:436-436, 2018

PubMed Abstract: Tick-borne encephalitis virus (TBEV) causes 13,000 cases of human meningitis and encephalitis annually. However, the structure of the TBEV virion and its interactions with antibodies are unknown. Here, we present cryo-EM structures of the native TBEV virion and its complex with Fab fragments of neutralizing antibody 19/1786. Flavivirus genome delivery depends on membrane fusion that is triggered at low pH. The virion structure indicates that the repulsive interactions of histidine side chains, which become protonated at low pH, may contribute to the disruption of heterotetramers of the TBEV envelope and membrane proteins and induce detachment of the envelope protein ectodomains from the virus membrane. The Fab fragments bind to 120 out of the 180 envelope glycoproteins of the TBEV virion. Unlike most of the previously studied flavivirus-neutralizing antibodies, the Fab fragments do not lock the E-proteins in the native-like arrangement, but interfere with the process of virus-induced membrane fusion.

PubMed: 29382836
DOI: 10.1038/s41467-018-02882-0

Experimental method

ELECTRON MICROSCOPY (3.9 Å)