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標題: Purification, crystallization and preliminary X-ray analysis of immunogenic viruslike particles formed by infectious bursal disease virus (IBDV) structural protein VP2
作者: Lee, C.C.
Ko, T.P.
Lee, M.S.
Chou, C.C.
Lai, S.Y.
Wang, A.H.J.
Wang, M.Y.
關鍵字: ion affinity-chromatography;maturation process;escherichia-coli;capsid protein;cleavage sites;insect cells;expression;identification;polyprotein;birnavirus
Project: Acta Crystallographica Section D-Biological Crystallography
期刊/報告no:: Acta Crystallographica Section D-Biological Crystallography, Volume 59, Page(s) 1234-1237.
Infectious bursal disease virus (IBDV) causes a highly contagious disease in young chicks and leads to significant economic losses in the poultry industry VP2 protein, which consists of 452 amino-acid residues, is the primary immunogen of IBDV and contains the epitopes responsible for eliciting neutralizing antibodies. When the chimeric VP2 protein (rVP2H) of a local IBDV strain P3009 was expressed alone using the baculovirus system, virus-like particles of approximately 23 nm in diameter formed spontaneously. Highly pure rVP2H particles, obtained using ammonium sulfate precipitation, immobilized metal-ion affinity chromatography and gel-filtration chromatography, were successfully crystallized using the vapour-diffusion method. These crystals, with a maximum dimension of 0.4 mm, diffracted X-rays to 4.5 Angstrom resolution, but data were only collected to 6 Angstrom. Preliminary analysis of the diffraction data showed that the rVP2H crystals belong to the cubic space group P2(1)3, with unit-cell parameter 323.1 Angstrom. The icosahedral symmetry of the particles is clearly seen in the self-rotation function maps, with dyads and triads coincident with the crystallographic axes. Each asymmetric unit contains 1/3 of the particle, or 20 rVP2H subunits, and there are four particles in a unit cell, probably in a tetrahedral arrangement.
ISSN: 0907-4449
DOI: 10.1107/s090744490300859x
Appears in Collections:生物科技學研究所

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