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

KALYNYCH, Sergei, Lenka PÁLKOVÁ and 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, vol. 90, No 3, p. 1377-1386. ISSN 0022-538X. Available from: https://dx.doi.org/10.1128/JVI.02346-15.

Basic information

• Original name: The Structure of Human Parechovirus 1 Reveals an Association of the RNA Genome with the Capsid
• Authors: KALYNYCH, Sergei (124 Canada, belonging to the institution), Lenka PÁLKOVÁ (203 Czech Republic, belonging to the institution) and Pavel PLEVKA (203 Czech Republic, guarantor, belonging to the institution).
• Edition: JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2016, 0022-538X.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10600 1.6 Biological sciences
• Country of publisher: United States of America
• Confidentiality degree: is not subject to a state or trade secret
• WWW: URL
• Impact factor: Impact factor: 4.663
• RIV identification code: RIV/00216224:14740/16:00093714
• Organization unit: Central European Institute of Technology
• Doi: http://dx.doi.org/10.1128/JVI.02346-15
• UT WoS: 000369150800019
• Keywords in English: ELECTRON-DENSITY; HUMAN RHINOVIRUS-14; PICORNAVIRUS GROUP; COXSACKIEVIRUS A9; CRYSTAL-STRUCTURE; VP1 PROTEIN; NMR SYSTEM; ENTEROVIRUS; RECEPTOR; INFECTIONS
• Tags: rivok

Abstract

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.