4QPG

Crystal structure of empty hepatitis A virus

4QPG の概要

• エントリーDOI: 10.2210/pdb4qpg/pdb
• 分子名称: Capsid protein VP1, Capsid protein VP0, Capsid protein VP3, ... (5 entities in total)
• 機能のキーワード: evolution, insect picorna-like viruses, icosahedral, domain swap, beta-barrel, virus, picornavirus, pathogen, liver
• 由来する生物種: Human hepatitis A virus; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 76180.11

構造登録者

Wang, X.,Ren, J.,Gao, Q.,Hu, Z.,Sun, Y.,Li, X.,Rowlands, D.J.,Yin, W.,Wang, J.,Stuart, D.I.,Rao, Z.,Fry, E.E. (登録日: 2014-06-23, 公開日: 2014-10-15, 最終更新日: 2023-09-20)

主引用文献

Wang, X.,Ren, J.,Gao, Q.,Hu, Z.,Sun, Y.,Li, X.,Rowlands, D.J.,Yin, W.,Wang, J.,Stuart, D.I.,Rao, Z.,Fry, E.E.
Hepatitis A virus and the origins of picornaviruses.
Nature, 517:85-88, 2015

PubMed Abstract: Hepatitis A virus (HAV) remains enigmatic, despite 1.4 million cases worldwide annually. It differs radically from other picornaviruses, existing in an enveloped form and being unusually stable, both genetically and physically, but has proved difficult to study. Here we report high-resolution X-ray structures for the mature virus and the empty particle. The structures of the two particles are indistinguishable, apart from some disorder on the inside of the empty particle. The full virus contains the small viral protein VP4, whereas the empty particle harbours only the uncleaved precursor, VP0. The smooth particle surface is devoid of depressions that might correspond to receptor-binding sites. Peptide scanning data extend the previously reported VP3 antigenic site, while structure-based predictions suggest further epitopes. HAV contains no pocket factor and can withstand remarkably high temperature and low pH, and empty particles are even more robust than full particles. The virus probably uncoats via a novel mechanism, being assembled differently to other picornaviruses. It utilizes a VP2 'domain swap' characteristic of insect picorna-like viruses, and structure-based phylogenetic analysis places HAV between typical picornaviruses and the insect viruses. The enigmatic properties of HAV may reflect its position as a link between 'modern' picornaviruses and the more 'primitive' precursor insect viruses; for instance, HAV retains the ability to move from cell-to-cell by transcytosis.

PubMed: 25327248
DOI: 10.1038/nature13806

実験手法

X-RAY DIFFRACTION (3.5 Å)