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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/43447

Title: Crystallization and X-ray diffraction of virus-like particles from a piscine betanodavirus
Authors: Yu-Chun Luo;Chun-Hsiung Wang;Yi-Min Wu;Wangta Liu;Ming-Wei Lu;Chan-Shing Lin
Contributors: 國立臺灣海洋大學:水產養殖學系
Keywords: Dragon grouper nervous necrosis virus (DGNNV);Betanodavirus;Epinephelus lanceolatus
Date: 2014-07-23
Issue Date: 2017-08-10T03:18:24Z
Publisher: Acta Crystallogr F Struct Biol Commun
Abstract: Abstract:Dragon grouper nervous necrosis virus (DGNNV), a member of the genus Betanodavirus, causes high mortality of larvae and juveniles of the grouper fish Epinephelus lanceolatus. Currently, there is no reported crystal structure of a fish nodavirus. The DGNNV virion capsid is derived from a single open reading frame that encodes a 338-amino-acid protein of approximately 37 kDa. The capsid protein of DGNNV was expressed to form virus-like particles (VLPs) in Escherichia coli. The VLP shape is T = 3 quasi-symmetric with a diameter of ∼38 nm in cryo-electron microscopy images and is highly similar to the native virion. In this report, crystals of DGNNV VLPs were grown to a size of 0.27 mm within two weeks by the hanging-drop vapour-diffusion method at 283 K and diffracted X-rays to ∼7.5 Å resolution. In-house X-ray diffraction data of the DGNNV VLP crystals showed that the crystals belonged to space group R32, with unit-cell parameters a = b = 353.00, c = 800.40 Å, α = β = 90, γ = 120°. 23 268 unique reflections were acquired with an overall R merge of 18.2% and a completeness of 93.2%. Self-rotation function maps confirmed the fivefold, threefold and twofold symmetries of the icosahedron of DGNNV VLPs.
Relation: 70(8), pp.1080-1086
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/43447
Appears in Collections:[水產養殖學系] 期刊論文

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