The Structure of Human Parechovirus 1 Reveals an Association of the RNA Genome with the Capsid

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F16%3A00093714" target="_blank" >RIV/00216224:14740/16:00093714 - isvavai.cz</a>

Výsledek na webu

<a href="http://jvi.asm.org/content/90/3/1377" target="_blank" >http://jvi.asm.org/content/90/3/1377</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1128/JVI.02346-15" target="_blank" >10.1128/JVI.02346-15</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The Structure of Human Parechovirus 1 Reveals an Association of the RNA Genome with the Capsid

Popis výsledku v původním jazyce

Parechoviruses are human pathogens that cause diseases ranging from gastrointestinal disorders to encephalitis. Unlike those of most picornaviruses, parechovirus capsids are composed of only three subunits: VP0, VP1, and VP3. Here, we present the structure of a human parechovirus 1 (HPeV-1) virion determined to a resolution of 3.1 angstrom. We found that interactions among pentamers in the HPeV-1 capsid are mediated by the N termini of VP0s, which correspond to the capsid protein VP4 and the N-terminal part of the capsid protein VP2 of other picornaviruses. In order to facilitate delivery of the virus genome into the cytoplasm, the N termini of VP0s have to be released from contacts between pentamers and exposed at the particle surface, resulting in capsid disruption. A hydrophobic pocket, which can be targeted by capsid-binding antiviral compounds in many other picornaviruses, is not present in HPeV-1.

Název v anglickém jazyce

The Structure of Human Parechovirus 1 Reveals an Association of the RNA Genome with the Capsid

Popis výsledku anglicky

Parechoviruses are human pathogens that cause diseases ranging from gastrointestinal disorders to encephalitis. Unlike those of most picornaviruses, parechovirus capsids are composed of only three subunits: VP0, VP1, and VP3. Here, we present the structure of a human parechovirus 1 (HPeV-1) virion determined to a resolution of 3.1 angstrom. We found that interactions among pentamers in the HPeV-1 capsid are mediated by the N termini of VP0s, which correspond to the capsid protein VP4 and the N-terminal part of the capsid protein VP2 of other picornaviruses. In order to facilitate delivery of the virus genome into the cytoplasm, the N termini of VP0s have to be released from contacts between pentamers and exposed at the particle surface, resulting in capsid disruption. A hydrophobic pocket, which can be targeted by capsid-binding antiviral compounds in many other picornaviruses, is not present in HPeV-1.

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

3

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

1377-1386

Kód UT WoS článku

000369150800019

EID výsledku v databázi Scopus

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