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@article{1373957,
author = {Kalynych, Sergei and Pálková, Lenka and Plevka, Pavel},
article_location = {WASHINGTON},
article_number = {3},
doi = {http://dx.doi.org/10.1128/JVI.02346-15},
keywords = {ELECTRON-DENSITY; HUMAN RHINOVIRUS-14; PICORNAVIRUS GROUP; COXSACKIEVIRUS A9; CRYSTAL-STRUCTURE; VP1 PROTEIN; NMR SYSTEM; ENTEROVIRUS; RECEPTOR; INFECTIONS},
language = {eng},
issn = {0022-538X},
journal = {JOURNAL OF VIROLOGY},
title = {The Structure of Human Parechovirus 1 Reveals an Association of the RNA Genome with the Capsid},
url = {http://jvi.asm.org/content/90/3/1377},
volume = {90},
year = {2016}
}
TY - JOUR
ID - 1373957
AU - Kalynych, Sergei - Pálková, Lenka - Plevka, Pavel
PY - 2016
TI - The Structure of Human Parechovirus 1 Reveals an Association of the RNA Genome with the Capsid
JF - JOURNAL OF VIROLOGY
VL - 90
IS - 3
SP - 1377-1386
EP - 1377-1386
PB - AMER SOC MICROBIOLOGY
SN - 0022538X
KW - ELECTRON-DENSITY
KW - HUMAN RHINOVIRUS-14
KW - PICORNAVIRUS GROUP
KW - COXSACKIEVIRUS A9
KW - CRYSTAL-STRUCTURE
KW - VP1 PROTEIN
KW - NMR SYSTEM
KW - ENTEROVIRUS
KW - RECEPTOR
KW - INFECTIONS
UR - http://jvi.asm.org/content/90/3/1377
L2 - http://jvi.asm.org/content/90/3/1377
N2 - 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. However, we found that interactions between the HPeV-1 single-stranded RNA genome and subunits VP1 and VP3 in the virion impose a partial icosahedral ordering on the genome. The residues involved in RNA binding are conserved among all parechoviruses, suggesting a putative role of the genome in virion stability or assembly. Therefore, putative small molecules that could disrupt HPeV RNA-capsid protein interactions could be developed into antiviral inhibitors.
ER -
KALYNYCH, Sergei, Lenka PÁLKOVÁ a Pavel PLEVKA. The Structure of Human Parechovirus 1 Reveals an Association of the RNA Genome with the Capsid. \textit{JOURNAL OF VIROLOGY}. WASHINGTON: AMER SOC MICROBIOLOGY, 2016, roč.~90, č.~3, s.~1377-1386. ISSN~0022-538X. Dostupné z: https://dx.doi.org/10.1128/JVI.02346-15.
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