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

J 2016

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

KALYNYCH, Sergei; Lenka PÁLKOVÁ a Pavel PLEVKA

Základní údaje

Originální název

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

Autoři

KALYNYCH, Sergei; Lenka PÁLKOVÁ a Pavel PLEVKA

Vydání

JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2016, 0022-538X

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.663

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14740/16:00093714

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

ELECTRON-DENSITY; HUMAN RHINOVIRUS-14; PICORNAVIRUS GROUP; COXSACKIEVIRUS A9; CRYSTAL-STRUCTURE; VP1 PROTEIN; NMR SYSTEM; ENTEROVIRUS; RECEPTOR; INFECTIONS

Štítky

rivok

Změněno: 27. 2. 2017 11:29, Mgr. Eva Špillingová

Anotace

V originále

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.

Citovat

KALYNYCH, Sergei; Lenka PÁLKOVÁ a Pavel PLEVKA. The Structure of Human Parechovirus 1 Reveals an Association of the RNA Genome with the Capsid. JOURNAL OF VIROLOGY. WASHINGTON: AMER SOC MICROBIOLOGY, 2016, roč. 90, č. 3, s. 1377-1386. ISSN 0022-538X. Dostupné z: https://doi.org/10.1128/JVI.02346-15.

@article{1373957,
   author = {Kalynych, Sergei and Pálková, Lenka and Plevka, Pavel},
   article_location = {WASHINGTON},
   article_number = {3},
   doi = {https://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://doi.org/10.1128/JVI.02346-15.

Přehled o publikaci