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TitleStructure determination of feline calicivirus virus-like particles in the context of a pseudo-octahedral arrangement.
Journal, issue, pagesPLoS One, Vol. 10, Issue 3, Page e0119289, Year 2015
Publish dateMar 20, 2015
AuthorsWim P Burmeister / Marlyse Buisson / Leandro F Estrozi / Guy Schoehn / Olivier Billet / Zahia Hannas / Cécile Sigoillot / Hervé Poulet /
PubMed AbstractThe 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 ...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.
External linksPLoS One / PubMed:25794153 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution8 - 14.0 Å
Structure data

EMDB-2823:
Structure determination of feline calicivirus virus-like particles in the context of a pseudo-octahedral arrangement
Method: EM (single particle) / Resolution: 14.0 Å

PDB-4pb6:
Feline calicivirus VP1 T=1 virus-like particle
Method: X-RAY DIFFRACTION / Resolution: 8.0 Å

Source
  • feline calicivirus
KeywordsVIRUS / viral capsid protein / virus-like particle

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