Structure and Genome Release Mechanism of the Human Cardiovirus Saffold Virus 3

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F16%3A00093713" target="_blank" >RIV/00216224:14740/16:00093713 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00027162:_____/16:N0000151

Výsledek na webu

<a href="http://jvi.asm.org/content/90/17/7628" target="_blank" >http://jvi.asm.org/content/90/17/7628</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1128/JVI.00746-16" target="_blank" >10.1128/JVI.00746-16</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structure and Genome Release Mechanism of the Human Cardiovirus Saffold Virus 3

Popis výsledku v původním jazyce

In order to initiate an infection, viruses need to deliver their genomes into cells. This involves uncoating the genome and transporting it to the cytoplasm. The process of genome delivery is not well understood for nonenveloped viruses. We address this gap in our current knowledge by studying the uncoating of the nonenveloped human cardiovirus Saffold virus 3 (SAFV-3) of the family Picornaviridae. SAFVs cause diseases ranging from gastrointestinal disorders to meningitis. We present a structure of a native SAFV-3 virion determined to 2.5 angstrom by X-ray crystallography and an 11-angstrom-resolution cryo-electron microscopy reconstruction of an "altered" particle that is primed for genome release. The altered particles are expanded relative to the native virus and contain pores in the capsid that might serve as channels for the release of VP4 subunits, N termini of VP1, and the RNA genome.

Název v anglickém jazyce

Structure and Genome Release Mechanism of the Human Cardiovirus Saffold Virus 3

Popis výsledku anglicky

In order to initiate an infection, viruses need to deliver their genomes into cells. This involves uncoating the genome and transporting it to the cytoplasm. The process of genome delivery is not well understood for nonenveloped viruses. We address this gap in our current knowledge by studying the uncoating of the nonenveloped human cardiovirus Saffold virus 3 (SAFV-3) of the family Picornaviridae. SAFVs cause diseases ranging from gastrointestinal disorders to meningitis. We present a structure of a native SAFV-3 virion determined to 2.5 angstrom by X-ray crystallography and an 11-angstrom-resolution cryo-electron microscopy reconstruction of an "altered" particle that is primed for genome release. The altered particles are expanded relative to the native virus and contain pores in the capsid that might serve as channels for the release of VP4 subunits, N termini of VP1, and the RNA genome.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

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Návaznosti

R - Projekt Ramcoveho programu EK

Rok uplatnění

2016

Kód důvěrnosti údajů

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

Název periodika

JOURNAL OF VIROLOGY

ISSN

0022-538X

e-ISSN

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Svazek periodika

90

Číslo periodika v rámci svazku

17

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

7628-7639

Kód UT WoS článku

000382306800004

EID výsledku v databázi Scopus

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