4Z92

crystal structure of parechovirus-1 virion

4Z92 の概要

• エントリーDOI: 10.2210/pdb4z92/pdb
• 分子名称: capsid subunit VP1, Capsid subunit VP3, capsid subunit VP0, ... (4 entities in total)
• 機能のキーワード: parechovirus, picornavirus, virion, pathogen, virus
• 由来する生物種: Human parechovirus 1 (strain Harris) (HPeV-1); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 88219.17

構造登録者

Kalynych, S.,Palkova, L.,Plevka, P. (登録日: 2015-04-09, 公開日: 2015-11-18, 最終更新日: 2024-01-10)

主引用文献

Kalynych, S.,Palkova, L.,Plevka, P.
The Structure of Human Parechovirus 1 Reveals an Association of the RNA Genome with the Capsid.
J.Virol., 90:1377-1386, 2015

PubMed 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 Å. 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.

PubMed: 26581987
DOI: 10.1128/JVI.02346-15

実験手法

X-RAY DIFFRACTION (3.1 Å)