5LWI

Israeli acute paralysis virus heated to 63 degree - empty particle

5LWI の概要

• エントリーDOI: 10.2210/pdb5lwi/pdb
• EMDBエントリー: 4115
• 分子名称: VP1, VP2, Structural polyprotein (3 entities in total)
• 機能のキーワード: iapv, dicistroviridae, empty particle, virus
• 由来する生物種: Israeli acute paralysis virus; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 83520.03

構造登録者

Mullapudi, E.,Fuzik, T.,Pridal, A.,Plevka, P. (登録日: 2016-09-16, 公開日: 2016-11-30, 最終更新日: 2024-05-15)

主引用文献

Mullapudi, E.,Fuzik, T.,Pridal, A.,Plevka, P.
Cryo-electron Microscopy Study of the Genome Release of the Dicistrovirus Israeli Acute Bee Paralysis Virus.
J. Virol., 91:-, 2017

PubMed Abstract: Viruses of the family Dicistroviridae can cause substantial economic damage by infecting agriculturally important insects. Israeli acute bee paralysis virus (IAPV) causes honeybee colony collapse disorder in the United States. High-resolution molecular details of the genome delivery mechanism of dicistroviruses are unknown. Here we present a cryo-electron microscopy analysis of IAPV virions induced to release their genomes in vitro We determined structures of full IAPV virions primed to release their genomes to a resolution of 3.3 Å and of empty capsids to a resolution of 3.9 Å. We show that IAPV does not form expanded A particles before genome release as in the case of related enteroviruses of the family Picornaviridae The structural changes observed in the empty IAPV particles include detachment of the VP4 minor capsid proteins from the inner face of the capsid and partial loss of the structure of the N-terminal arms of the VP2 capsid proteins. Unlike the case for many picornaviruses, the empty particles of IAPV are not expanded relative to the native virions and do not contain pores in their capsids that might serve as channels for genome release. Therefore, rearrangement of a unique region of the capsid is probably required for IAPV genome release.

PubMed: 27928006
DOI: 10.1128/JVI.02060-16

実験手法

ELECTRON MICROSCOPY (3.2 Å)