4PB6

Feline calicivirus VP1 T=1 virus-like particle

4PB6 の概要

• エントリーDOI: 10.2210/pdb4pb6/pdb
• 分子名称: VP1 (1 entity in total)
• 機能のキーワード: viral capsid protein, virus-like particle, virus
• 由来する生物種: Feline calicivirus
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 1185952.26

構造登録者

Burmeister, W.P.,Buisson, M. (登録日: 2014-04-11, 公開日: 2015-04-08, 最終更新日: 2023-12-20)

主引用文献

Burmeister, W.P.,Buisson, M.,Estrozi, L.F.,Schoehn, G.,Billet, O.,Hannas, Z.,Sigoillot, C.,Poulet, H.
Structure determination of feline calicivirus virus-like particles in the context of a pseudo-octahedral arrangement.
Plos One, 10:e0119289-e0119289, 2015

PubMed Abstract: The vesivirus feline calicivirus (FCV) is a positive strand RNA virus encapsidated by an icosahedral T=3 shell formed by the viral VP1 protein. Upon its expression in the insect cell - baculovirus system in the context of vaccine development, two types of virus-like particles (VLPs) were formed, a majority built of 60 subunits (T=1) and a minority probably built of 180 subunits (T=3). The structure of the small particles was determined by x-ray crystallography at 0.8 nm resolution helped by cryo-electron microscopy in order to understand their formation. Cubic crystals belonged to space group P213. Their self-rotation function showed the presence of an octahedral pseudo-symmetry similar to the one described previously by Agerbandje and co-workers for human parvovirus VLPs. The crystal structure could be solved starting from the published VP1 structure in the context of the T=3 viral capsid. In contrast to viral capsids, where the capsomers are interlocked by the exchange of the N-terminal arm (NTA) domain, this domain is disordered in the T=1 capsid of the VLPs. Furthermore it is prone to proteolytic cleavage. The relative orientation of P (protrusion) and S (shell) domains is alerted so as to fit VP1 to the smaller T=1 particle whereas the intermolecular contacts around 2-fold, 3-fold and 5-fold axes are conserved. By consequence the surface of the VLP is very similar compared to the viral capsid and suggests a similar antigenicity. The knowledge of the structure of the VLPs will help to improve their stability, in respect to a use for vaccination.

PubMed: 25794153
DOI: 10.1371/journal.pone.0119289

実験手法

X-RAY DIFFRACTION (8 Å)