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

研究成果: 雜誌貢獻 › 文章 › 同行評審

17 引文斯高帕斯（Scopus）

摘要

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.

原文	英語
頁（從 - 到）	318-322
頁數	5
期刊	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
卷	64
發行號	4
DOIs	https://doi.org/10.1107/S1744309108007197
出版狀態	已發佈 - 3月 29 2008
對外發佈	是

ASJC Scopus subject areas

生物物理學
結構生物學
生物化學
遺傳學
凝聚態物理學

UN SDG

此研究成果有助於以下永續發展目標

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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, 卷 64, 編號 4, 頁 318-322. https://doi.org/10.1107/S1744309108007197

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AU - Miyazaki, Naoyuki

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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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N2 - 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.

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

摘要

ASJC Scopus subject areas

UN SDG

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