Structure of Aichi Virus 1 and Its Empty Particle: Clues to
Kobuvirus Genome Release Mechanism

J 2016

Structure of Aichi Virus 1 and Its Empty Particle: Clues to Kobuvirus Genome Release Mechanism

SABIN, Charles David, Tibor FÜZIK, Karel ŠKUBNÍK, Lenka PÁLKOVÁ, A. Michael LINDBERG et. al.

Základní údaje

Originální název

Structure of Aichi Virus 1 and Its Empty Particle: Clues to Kobuvirus Genome Release Mechanism

Autoři

SABIN, Charles David (250 Francie, domácí), Tibor FÜZIK (703 Slovensko, domácí), Karel ŠKUBNÍK (203 Česká republika, domácí), Lenka PÁLKOVÁ (203 Česká republika, domácí), A. Michael LINDBERG (752 Švédsko) a Pavel PLEVKA (203 Česká republika, garant, domácí)

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

Kód RIV

RIV/00216224:14740/16:00093720

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1128/JVI.01601-16

UT WoS

000389904500030

Klíčová slova anglicky

EM STRUCTURE DETERMINATION; HUMAN ENTEROVIRUS 71; 3-DIMENSIONAL STRUCTURE; CONFORMATIONAL-CHANGES; CRYSTAL-STRUCTURE; ELECTRON-MICROSCOPY; POLIOVIRUS; PICORNAVIRUS; RESOLUTION; RECEPTOR

Štítky

rivok

Změněno: 27. 2. 2017 13:27, Mgr. Eva Špillingová

Anotace

V originále

Aichi virus 1 (AiV-1) is a human pathogen from the Kobuvirus genus of the Picornaviridae family. Worldwide, 80 to 95% of adults have antibodies against the virus. AiV-1 infections are associated with nausea, gastroenteritis, and fever. Unlike most picornaviruses, kobuvirus capsids are composed of only three types of subunits: VP0, VP1, and VP3. We present here the structure of the AiV-1 virion determined to a resolution of 2.1 angstrom using X-ray crystallography. The surface loop puff of VP0 and knob of VP3 in AiV-1 are shorter than those in other picornaviruses. Instead, the 42-residue BC loop of VP0 forms the most prominent surface feature of the AiV-1 virion. We determined the structure of AiV-1 empty particle to a resolution of 4.2 angstrom using cryo-electron microscopy. The empty capsids are expanded relative to the native virus. The N-terminal arms of capsid proteins VP0, which mediate contacts between the pentamers of capsid protein protomers in the native AiV-1 virion, are disordered in the empty capsid. Nevertheless, the empty particles are stable, at least in vitro, and do not contain pores that might serve as channels for genome release. Therefore, extensive and probably reversible local reorganization of AiV-1 capsid is required for its genome release. IMPORTANCE Aichi virus 1 (AiV-1) is a human pathogen that can cause diarrhea, abdominal pain, nausea, vomiting, and fever. AiV-1 is identified in environmental screening studies with higher frequency and greater abundance than other human enteric viruses. Accordingly, 80 to 95% of adults worldwide have suffered from AiV-1 infections. We determined the structure of the AiV-1 virion. Based on the structure, we show that antiviral compounds that were developed against related enteroviruses are unlikely to be effective against AiV-1. The surface of the AiV-1 virion has a unique topology distinct from other related viruses from the Picornaviridae family. We also determined that AiV-1 capsids form compact shells even after genome release. Therefore, AiV-1 genome release requires large localized and probably reversible reorganization of the capsid.

Návaznosti

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

Citovat

SABIN, Charles David, Tibor FÜZIK, Karel ŠKUBNÍK, Lenka PÁLKOVÁ, A. Michael LINDBERG a Pavel PLEVKA. Structure of Aichi Virus 1 and Its Empty Particle: Clues to Kobuvirus Genome Release Mechanism. JOURNAL OF VIROLOGY. WASHINGTON: AMER SOC MICROBIOLOGY, 2016, roč. 90, č. 23, s. 10800-10810. ISSN 0022-538X. Dostupné z: https://dx.doi.org/10.1128/JVI.01601-16.

@article{1373973,
   author = {Sabin, Charles David and Füzik, Tibor and Škubník, Karel and Pálková, Lenka and Lindberg, A. Michael and Plevka, Pavel},
   article_location = {WASHINGTON},
   article_number = {23},
   doi = {http://dx.doi.org/10.1128/JVI.01601-16},
   keywords = {EM STRUCTURE DETERMINATION; HUMAN ENTEROVIRUS 71; 3-DIMENSIONAL STRUCTURE; CONFORMATIONAL-CHANGES; CRYSTAL-STRUCTURE; ELECTRON-MICROSCOPY; POLIOVIRUS; PICORNAVIRUS; RESOLUTION; RECEPTOR},
   language = {eng},
   issn = {0022-538X},
   journal = {JOURNAL OF VIROLOGY},
   title = {Structure of Aichi Virus 1 and Its Empty Particle: Clues to Kobuvirus Genome Release Mechanism},
   url = {http://jvi.asm.org/content/90/23/10800},
   volume = {90},
   year = {2016}
}

TY  - JOUR
ID  - 1373973
AU  - Sabin, Charles David - Füzik, Tibor - Škubník, Karel - Pálková, Lenka - Lindberg, A. Michael - Plevka, Pavel
PY  - 2016
TI  - Structure of Aichi Virus 1 and Its Empty Particle: Clues to Kobuvirus Genome Release Mechanism
JF  - JOURNAL OF VIROLOGY
VL  - 90
IS  - 23
SP  - 10800-10810
EP  - 10800-10810
PB  - AMER SOC MICROBIOLOGY
SN  - 0022538X
KW  - EM STRUCTURE DETERMINATION
KW  - HUMAN ENTEROVIRUS 71
KW  - 3-DIMENSIONAL STRUCTURE
KW  - CONFORMATIONAL-CHANGES
KW  - CRYSTAL-STRUCTURE
KW  - ELECTRON-MICROSCOPY
KW  - POLIOVIRUS
KW  - PICORNAVIRUS
KW  - RESOLUTION
KW  - RECEPTOR
UR  - http://jvi.asm.org/content/90/23/10800
L2  - http://jvi.asm.org/content/90/23/10800
N2  - Aichi virus 1 (AiV-1) is a human pathogen from the Kobuvirus genus of the Picornaviridae family. Worldwide, 80 to 95% of adults have antibodies against the virus. AiV-1 infections are associated with nausea, gastroenteritis, and fever. Unlike most picornaviruses, kobuvirus capsids are composed of only three types of subunits: VP0, VP1, and VP3. We present here the structure of the AiV-1 virion determined to a resolution of 2.1 angstrom using X-ray crystallography. The surface loop puff of VP0 and knob of VP3 in AiV-1 are shorter than those in other picornaviruses. Instead, the 42-residue BC loop of VP0 forms the most prominent surface feature of the AiV-1 virion. We determined the structure of AiV-1 empty particle to a resolution of 4.2 angstrom using cryo-electron microscopy. The empty capsids are expanded relative to the native virus. The N-terminal arms of capsid proteins VP0, which mediate contacts between the pentamers of capsid protein protomers in the native AiV-1 virion, are disordered in the empty capsid. Nevertheless, the empty particles are stable, at least in vitro, and do not contain pores that might serve as channels for genome release. Therefore, extensive and probably reversible local reorganization of AiV-1 capsid is required for its genome release. IMPORTANCE Aichi virus 1 (AiV-1) is a human pathogen that can cause diarrhea, abdominal pain, nausea, vomiting, and fever. AiV-1 is identified in environmental screening studies with higher frequency and greater abundance than other human enteric viruses. Accordingly, 80 to 95% of adults worldwide have suffered from AiV-1 infections. We determined the structure of the AiV-1 virion. Based on the structure, we show that antiviral compounds that were developed against related enteroviruses are unlikely to be effective against AiV-1. The surface of the AiV-1 virion has a unique topology distinct from other related viruses from the Picornaviridae family. We also determined that AiV-1 capsids form compact shells even after genome release. Therefore, AiV-1 genome release requires large localized and probably reversible reorganization of the capsid.
ER  -

SABIN, Charles David, Tibor FÜZIK, Karel ŠKUBNÍK, Lenka PÁLKOVÁ, A. Michael LINDBERG a Pavel PLEVKA. Structure of Aichi Virus 1 and Its Empty Particle: Clues to Kobuvirus Genome Release Mechanism. \textit{JOURNAL OF VIROLOGY}. WASHINGTON: AMER SOC MICROBIOLOGY, 2016, roč.~90, č.~23, s.~10800-10810. ISSN~0022-538X. Dostupné z: https://dx.doi.org/10.1128/JVI.01601-16.

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