Detailed Information on Publication Record
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.Basic information
Original name
Structure of Aichi Virus 1 and Its Empty Particle: Clues to Kobuvirus Genome Release Mechanism
Authors
SABIN, Charles David (250 France, belonging to the institution), Tibor FÜZIK (703 Slovakia, belonging to the institution), Karel ŠKUBNÍK (203 Czech Republic, belonging to the institution), Lenka PÁLKOVÁ (203 Czech Republic, belonging to the institution), A. Michael LINDBERG (752 Sweden) and Pavel PLEVKA (203 Czech Republic, guarantor, belonging to the institution)
Edition
JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2016, 0022-538X
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 4.663
RIV identification code
RIV/00216224:14740/16:00093720
Organization unit
Central European Institute of Technology
UT WoS
000389904500030
Keywords in English
EM STRUCTURE DETERMINATION; HUMAN ENTEROVIRUS 71; 3-DIMENSIONAL STRUCTURE; CONFORMATIONAL-CHANGES; CRYSTAL-STRUCTURE; ELECTRON-MICROSCOPY; POLIOVIRUS; PICORNAVIRUS; RESOLUTION; RECEPTOR
Tags
Změněno: 27/2/2017 13:27, Mgr. Eva Špillingová
Abstract
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.
Links
| LQ1601, research and development project |
|