Crystallization and preliminary X-ray diffraction analysis of recombinant hepatitis e virus-like particle

Che Yen Wang; Naoyuki Miyazaki; Tetsuo Yamashita; Akifumi Higashiura; Atsushi Nakagawa; Tian Cheng Li; Naokazu Takeda; Li Xing; Erik Hjalmarsson; Claes Friberg; Der Ming Liou; Yen Jen Sung; Tomitake Tsukihara; Yoshiharu Matsuura; Tatsuo Miyamura; R. Holland Cheng

doi:10.1107/S1744309108007197

Crystallization and preliminary X-ray diffraction analysis of recombinant hepatitis e virus-like particle

Che Yen Wang, Naoyuki Miyazaki, Tetsuo Yamashita, Akifumi Higashiura, Atsushi Nakagawa, Tian Cheng Li, Naokazu Takeda, Li Xing, Erik Hjalmarsson, Claes Friberg, Der Ming Liou, Yen Jen Sung, Tomitake Tsukihara, Yoshiharu Matsuura, Tatsuo Miyamura, R. Holland Cheng

Research output: Contribution to journal › Article › peer-review

17 Citations (Scopus)

Abstract

Hepatitis E virus (HEV) accounts for the majority of enterically transmitted hepatitis infections worldwide. Currently, there is no specific treatment for or vaccine against HEV. The major structural protein is derived from open reading frame (ORF) 2 of the viral genome. A potential oral vaccine is provided by the virus-like particles formed by a protein construct of partial ORF3 protein (residue 70-123) fused to the N-terminus of the ORF2 protein (residues 112-608). Single crystals obtained by the hanging-drop vapour-diffusion method at 293 K diffract X-rays to 8.3 Å resolution. The crystals belong to space group P2₁2₁2₁, with unit-cell parameters a = 337, b = 343, c = 346 Å, α = β = γ = 90°, and contain one particle per asymmetric unit.

Original language	English
Pages (from-to)	318-322
Number of pages	5
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	64
Issue number	4
DOIs	https://doi.org/10.1107/S1744309108007197
Publication status	Published - Mar 29 2008
Externally published	Yes

Keywords

Electron microscopy
Hepatitis E virus
Vaccines
Virus-like particle

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1107/S1744309108007197

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Wang, C. Y., Miyazaki, N., Yamashita, T., Higashiura, A., Nakagawa, A., Li, T. C., Takeda, N., Xing, L., Hjalmarsson, E., Friberg, C., Liou, D. M., Sung, Y. J., Tsukihara, T., Matsuura, Y., Miyamura, T., & Cheng, R. H. (2008). Crystallization and preliminary X-ray diffraction analysis of recombinant hepatitis e virus-like particle. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(4), 318-322. https://doi.org/10.1107/S1744309108007197

Wang, CY, Miyazaki, N, Yamashita, T, Higashiura, A, Nakagawa, A, Li, TC, Takeda, N, Xing, L, Hjalmarsson, E, Friberg, C, Liou, DM, Sung, YJ, Tsukihara, T, Matsuura, Y, Miyamura, T & Cheng, RH 2008, 'Crystallization and preliminary X-ray diffraction analysis of recombinant hepatitis e virus-like particle', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 64, no. 4, pp. 318-322. https://doi.org/10.1107/S1744309108007197

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abstract = "Hepatitis E virus (HEV) accounts for the majority of enterically transmitted hepatitis infections worldwide. Currently, there is no specific treatment for or vaccine against HEV. The major structural protein is derived from open reading frame (ORF) 2 of the viral genome. A potential oral vaccine is provided by the virus-like particles formed by a protein construct of partial ORF3 protein (residue 70-123) fused to the N-terminus of the ORF2 protein (residues 112-608). Single crystals obtained by the hanging-drop vapour-diffusion method at 293 K diffract X-rays to 8.3 {\AA} resolution. The crystals belong to space group P212121, with unit-cell parameters a = 337, b = 343, c = 346 {\AA}, α = β = γ = 90°, and contain one particle per asymmetric unit.",

keywords = "Electron microscopy, Hepatitis E virus, Vaccines, Virus-like particle",

author = "Wang, {Che Yen} and Naoyuki Miyazaki and Tetsuo Yamashita and Akifumi Higashiura and Atsushi Nakagawa and Li, {Tian Cheng} and Naokazu Takeda and Li Xing and Erik Hjalmarsson and Claes Friberg and Liou, {Der Ming} and Sung, {Yen Jen} and Tomitake Tsukihara and Yoshiharu Matsuura and Tatsuo Miyamura and Cheng, {R. Holland}",

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AU - Wang, Che Yen

AU - Miyazaki, Naoyuki

AU - Yamashita, Tetsuo

AU - Higashiura, Akifumi

AU - Nakagawa, Atsushi

AU - Li, Tian Cheng

AU - Takeda, Naokazu

AU - Xing, Li

AU - Hjalmarsson, Erik

AU - Friberg, Claes

AU - Liou, Der Ming

AU - Sung, Yen Jen

AU - Tsukihara, Tomitake

AU - Matsuura, Yoshiharu

AU - Miyamura, Tatsuo

AU - Cheng, R. Holland

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AB - Hepatitis E virus (HEV) accounts for the majority of enterically transmitted hepatitis infections worldwide. Currently, there is no specific treatment for or vaccine against HEV. The major structural protein is derived from open reading frame (ORF) 2 of the viral genome. A potential oral vaccine is provided by the virus-like particles formed by a protein construct of partial ORF3 protein (residue 70-123) fused to the N-terminus of the ORF2 protein (residues 112-608). Single crystals obtained by the hanging-drop vapour-diffusion method at 293 K diffract X-rays to 8.3 Å resolution. The crystals belong to space group P212121, with unit-cell parameters a = 337, b = 343, c = 346 Å, α = β = γ = 90°, and contain one particle per asymmetric unit.

KW - Electron microscopy

KW - Hepatitis E virus

KW - Vaccines

KW - Virus-like particle

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Crystallization and preliminary X-ray diffraction analysis of recombinant hepatitis e virus-like particle

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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