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

Result code in 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>
Result on the web
<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>

Result language
angličtina
Original language name
The Structure of Human Parechovirus 1 Reveals an Association of the RNA Genome with the Capsid
Original language description
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.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EE - Microbiology, virology
OECD FORD branch
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Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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