4PB6
Feline calicivirus VP1 T=1 virus-like particle
Summary for 4PB6
| Entry DOI | 10.2210/pdb4pb6/pdb |
| Descriptor | VP1 (1 entity in total) |
| Functional Keywords | viral capsid protein, virus-like particle, virus |
| Biological source | Feline calicivirus |
| Total number of polymer chains | 20 |
| Total formula weight | 1185952.26 |
| Authors | Burmeister, W.P.,Buisson, M. (deposition date: 2014-04-11, release date: 2015-04-08, Last modification date: 2023-12-20) |
| Primary citation | 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 Cited by 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: 25794153DOI: 10.1371/journal.pone.0119289 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (8 Å) |
Structure validation
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