Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody

FÜZIK, Tibor, P. FORMANOVA, D. RUZEK, K. YOSHII, M. NIEDRIG and Pavel PLEVKA. Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody. Nature Communications. London: Nature Publishing Group, 2018, vol. 9, JAN, p. 436-446. ISSN 2041-1723. Available from: https://dx.doi.org/10.1038/s41467-018-02882-0.

Basic information

Original name

Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody

Authors

FÜZIK, Tibor (703 Slovakia, belonging to the institution), P. FORMANOVA (203 Czech Republic), D. RUZEK (203 Czech Republic), K. YOSHII (392 Japan), M. NIEDRIG (276 Germany) and Pavel PLEVKA (203 Czech Republic, guarantor, belonging to the institution)

Edition

Nature Communications, London, Nature Publishing Group, 2018, 2041-1723

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Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10607 Virology

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 11.878

RIV identification code

RIV/00216224:14740/18:00101775

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1038/s41467-018-02882-0

UT WoS

000423510600013

Keywords in English

WEST-NILE-VIRUS; DENGUE VIRUS; MEMBRANE-FUSION; ENVELOPE GLYCOPROTEIN; ELECTRON-MICROSCOPY; ZIKA VIRUS; CELL ENTRY; ACIDIC PH; MATURATION; PROTEINS

Tags

CF CRYO, CF PROT, rivok

Tags

International impact, Reviewed

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Abstract

V originále

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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Links

GA17-02196S, research and development project	Name: Strukturní studie flavivirů a mechanismu jejich neutralizace protilátkami Investor: Czech Science Foundation, Structural studies of flaviviruses and their neutralization by antibodies
LM2015043, research and development project	Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB) Investor: Ministry of Education, Youth and Sports of the CR
LM2015085, research and development project	Name: CERIT Scientific Cloud (Acronym: CERIT-SC) Investor: Ministry of Education, Youth and Sports of the CR, CERIT Scientific Cloud
LQ1601, research and development project	Name: CEITEC 2020 (Acronym: CEITEC2020) Investor: Ministry of Education, Youth and Sports of the CR
3041, interní kód MU	Name: Structural studies of human and animal pathogens from the order Picornavirales Investor: EMBO (European Molecular Biology Organization)
335855, interní kód MU	Name: Structural studies of human picornaviruses directed towards development of anti-viral compounds (Acronym: PicoDrugs) Investor: European Union, Ideas