The structure of immature tick-borne encephalitis virus supports the collapse model of flavivirus maturation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F24%3A00587841" target="_blank" >RIV/60077344:_____/24:00587841 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216224:14740/24:00136505 RIV/00027162:_____/24:N0000067

Výsledek na webu

<a href="https://www.science.org/doi/10.1126/sciadv.adl1888" target="_blank" >https://www.science.org/doi/10.1126/sciadv.adl1888</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1126/sciadv.adl1888" target="_blank" >10.1126/sciadv.adl1888</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The structure of immature tick-borne encephalitis virus supports the collapse model of flavivirus maturation

Popis výsledku v původním jazyce

We present structures of three immature tick-borne encephalitis virus (TBEV) isolates. Our atomic models of the major viral components, the E and prM proteins, indicate that the pr domains of prM have a critical role in holding the heterohexameric prM3E3 spikes in a metastable conformation. Destabilization of the prM furin-sensitive loop at acidic pH facilitates its processing. The prM topology and domain assignment in TBEV is similar to the mosquito-borne Binjari virus, but is in contrast to other immature flavivirus models. These results support that prM cleavage, the collapse of E protein ectodomains onto the virion surface, the large movement of the membrane domains of both E and M, and the release of the pr fragment from the particle render the virus mature and infectious. Our work favors the collapse model of flavivirus maturation warranting further studies of immature flaviviruses to determine the sequence of events and mechanistic details driving flavivirus maturation.

Název v anglickém jazyce

The structure of immature tick-borne encephalitis virus supports the collapse model of flavivirus maturation

Popis výsledku anglicky

We present structures of three immature tick-borne encephalitis virus (TBEV) isolates. Our atomic models of the major viral components, the E and prM proteins, indicate that the pr domains of prM have a critical role in holding the heterohexameric prM3E3 spikes in a metastable conformation. Destabilization of the prM furin-sensitive loop at acidic pH facilitates its processing. The prM topology and domain assignment in TBEV is similar to the mosquito-borne Binjari virus, but is in contrast to other immature flavivirus models. These results support that prM cleavage, the collapse of E protein ectodomains onto the virion surface, the large movement of the membrane domains of both E and M, and the release of the pr fragment from the particle render the virus mature and infectious. Our work favors the collapse model of flavivirus maturation warranting further studies of immature flaviviruses to determine the sequence of events and mechanistic details driving flavivirus maturation.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10607 - Virology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

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

Název periodika

Science Advances

ISSN

2375-2548

e-ISSN

2375-2548

Svazek periodika

10

Číslo periodika v rámci svazku

27

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

eadl1888

Kód UT WoS článku

001262993200012

EID výsledku v databázi Scopus

2-s2.0-85197686140