Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-018-02882-0
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Funding
- Czech Infrastructure for Integrative Structural Biology - Ministry of Education, Youth and Sports of the Czech Republic [LM2015043]
- project CEITEC [LQ1601]
- Ministry of Education, Youth and Sports of the Czech Republic
- CESNET [LM2015042]
- CERIT Scientific Cloud [LM2015085]
- Ministry of Education, Youth and Sports from the Large Infrastructures for Research, Experimental Development and Innovations project IT4Innovations National Supercomputing Center [LM2015070]
- European Research Council under the European Union [355855]
- EMBO [IG 3041]
- Czech Science Foundation [17-02196S]
- JSPS KAKENHI [16K1503206, 17H03910]
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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.
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