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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00027162%3A_____%2F18%3AN0000228" target="_blank" >RIV/00027162:_____/18:N0000228 - isvavai.cz</a>

Alternative codes found

RIV/60077344:_____/18:00498599 RIV/00216224:14740/18:00101775

Result on the web

<a href="https://www.nature.com/articles/s41467-018-02882-0" target="_blank" >https://www.nature.com/articles/s41467-018-02882-0</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41467-018-02882-0" target="_blank" >10.1038/s41467-018-02882-0</a>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10607 - Virology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2018

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Nature Communications

ISSN

2041-1723

e-ISSN

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Volume of the periodical

9

Issue of the periodical within the volume

January

Country of publishing house

GB - UNITED KINGDOM

Number of pages

11

Pages from-to

436

UT code for WoS article

000423510600013

EID of the result in the Scopus database

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