7PE2

Cryo-EM structure of BMV-derived VLP expressed in E. coli (eVLP)

これはPDB形式変換不可エントリーです。

7PE2 の概要

• エントリーDOI: 10.2210/pdb7pe2/pdb
• EMDBエントリー: 13345
• 分子名称: Coat protein (2 entities in total)
• 機能のキーワード: bmv, brome mosaic virus, capsid proteins, virus like particle
• 由来する生物種: Brome mosaic virus (BMV)
• タンパク質・核酸の鎖数: 180
• 化学式量合計: 3702364.74

構造登録者

Ruszkowski, M.,Strugala, A.,Indyka, P.,Urbanowicz, A. (登録日: 2021-08-09, 公開日: 2022-03-02, 最終更新日: 2024-07-17)

主引用文献

Ruszkowski, M.,Strugala, A.,Indyka, P.,Tresset, G.,Figlerowicz, M.,Urbanowicz, A.
Cryo-EM reconstructions of BMV-derived virus-like particles reveal assembly defects in the icosahedral lattice structure.
Nanoscale, 14:3224-3233, 2022

PubMed Abstract: The increasing interest in virus-like particles (VLPs) has been reflected by the growing number of studies on their assembly and application. However, the formation of complete VLPs is a complex phenomenon, making it difficult to rationally design VLPs with desired features . In this paper, we describe VLPs assembled from the recombinant capsid protein of brome mosaic virus (BMV). The analysis of VLPs was performed by Cryo-EM reconstructions and allowed us to visualize a few classes of VLPs, giving insight into the VLP self-assembly process. Apart from the mature icosahedral VLP practically identical with native virions, we describe putative VLP intermediates displaying non-icosahedral arrangements of capsomers, proposed to occur before the final disorder-order transition stage of icosahedral VLP assembly. Some of the described VLP classes show a lack of protein shell continuity, possibly resulting from too strong interaction with the cargo (in this case tRNA) with the capsid protein. We believe that our results are a useful prerequisite for the rational design of VLPs in the future and lead the way to the effective production of modified VLPs.

PubMed: 35156989
DOI: 10.1039/d1nr05650f

実験手法

ELECTRON MICROSCOPY (3.2 Å)