5G52

Crystallographic structure of full particle of Deformed Wing Virus

5G52 の概要

• エントリーDOI: 10.2210/pdb5g52/pdb
• 関連するPDBエントリー: 5G51
• 分子名称: VP1, VP2, VP3, ... (4 entities in total)
• 機能のキーワード: virus, picornavirales, iflaviridae, iflavirus, dwv capsid, p jellyroll, catalytic site protease, lipase esterase recepto
• 由来する生物種: DEFORMED WING VIRUS; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 99936.48

構造登録者

Skubnik, K.,Novacek, J.,Fuzik, T.,Pridal, A.,Paxton, R.,Plevka, P. (登録日: 2016-05-18, 公開日: 2017-03-22, 最終更新日: 2024-05-08)

主引用文献

Skubnik, K.,Novacek, J.,Fuzik, T.,Pridal, A.,Paxton, R.J.,Plevka, P.
Structure of deformed wing virus, a major honey bee pathogen.
Proc. Natl. Acad. Sci. U.S.A., 114:3210-3215, 2017

PubMed Abstract: The worldwide population of western honey bees () is under pressure from habitat loss, environmental stress, and pathogens, particularly viruses that cause lethal epidemics. Deformed wing virus (DWV) from the family , together with its vector, the mite , is likely the major threat to the world's honey bees. However, lack of knowledge of the atomic structures of iflaviruses has hindered the development of effective treatments against them. Here, we present the virion structures of DWV determined to a resolution of 3.1 Å using cryo-electron microscopy and 3.8 Å by X-ray crystallography. The C-terminal extension of capsid protein VP3 folds into a globular protruding (P) domain, exposed on the virion surface. The P domain contains an Asp-His-Ser catalytic triad that is, together with five residues that are spatially close, conserved among iflaviruses. These residues may participate in receptor binding or provide the protease, lipase, or esterase activity required for entry of the virus into a host cell. Furthermore, nucleotides of the DWV RNA genome interact with VP3 subunits. The capsid protein residues involved in the RNA binding are conserved among honey bee iflaviruses, suggesting a putative role of the genome in stabilizing the virion or facilitating capsid assembly. Identifying the RNA-binding and putative catalytic sites within the DWV virion structure enables future analyses of how DWV and other iflaviruses infect insect cells and also opens up possibilities for the development of antiviral treatments.

PubMed: 28270616
DOI: 10.1073/pnas.1615695114

実験手法

X-RAY DIFFRACTION (3.802 Å)