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Title: Crystallization and preliminary X-ray diffraction analysis of recombinant hepatitis E virus-like particle

Abstract

A recombinant virus-like particle that is a potential oral hepatitis E vaccine was crystallized. Diffraction data were collected to 8.3 Å resolution and the X-ray structure was phased with the aid of a low-resolution density map determined using cryo-electron microscopy data. 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 P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 337, b = 343, c = 346 Å, α = β = γ = 90°, and contain one particle per asymmetric unit.

Authors:
 [1];  [1];  [2]; ;  [2]; ;  [3];  [1]; ;  [4];  [5];  [5];  [2];  [6];  [3]
  1. Molecular and Cellular Biology, University of California, Davis, CA 95616 (United States)
  2. Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871 (Japan)
  3. Department of Virology II, National Institute of Infectious Diseases, Tokyo (Japan)
  4. Crystal Research AB, 22370 Lund (Sweden)
  5. Institute of Public Health, National Yang-Ming University, 112 Taipei,Taiwan (China)
  6. Institute for Microbial Diseases, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871 (Japan)
Publication Date:
OSTI Identifier:
22360511
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 64; Journal Issue: Pt 4; Other Information: PMCID: PMC2374242; PMID: 18391436; PUBLISHER-ID: en5297; OAI: oai:pubmedcentral.nih.gov:2374242; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; DENSITY; DIFFUSION; ELECTRON MICROSCOPY; MONOCRYSTALS; POTENTIALS; PROTEINS; RESOLUTION; SPACE GROUPS; X-RAY DIFFRACTION

Citation Formats

Wang, Che-Yen, Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm, Institute of Public Health, National Yang-Ming University, 112 Taipei,Taiwan, Miyazaki, Naoyuki, Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Yamashita, Tetsuo, Institute for Microbial Diseases, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Higashiura, Akifumi, Nakagawa, Atsushi, Li, Tian-Cheng, Takeda, Naokazu, Xing, Li, Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm, Hjalmarsson, Erik, Friberg, Claes, Liou, Der-Ming, Sung, Yen-Jen, Institute of Anatomy and Cell Biology, National Yang-Ming University, 112 Taipei,Taiwan, Tsukihara, Tomitake, Matsuura, Yoshiharu, Miyamura, Tatsuo, Cheng, R. Holland, E-mail: rhch@ucdavis.edu, and Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm. Crystallization and preliminary X-ray diffraction analysis of recombinant hepatitis E virus-like particle. United Kingdom: N. p., 2008. Web. doi:10.1107/S1744309108007197.
Wang, Che-Yen, Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm, Institute of Public Health, National Yang-Ming University, 112 Taipei,Taiwan, Miyazaki, Naoyuki, Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Yamashita, Tetsuo, Institute for Microbial Diseases, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Higashiura, Akifumi, Nakagawa, Atsushi, Li, Tian-Cheng, Takeda, Naokazu, Xing, Li, Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm, Hjalmarsson, Erik, Friberg, Claes, Liou, Der-Ming, Sung, Yen-Jen, Institute of Anatomy and Cell Biology, National Yang-Ming University, 112 Taipei,Taiwan, Tsukihara, Tomitake, Matsuura, Yoshiharu, Miyamura, Tatsuo, Cheng, R. Holland, E-mail: rhch@ucdavis.edu, & Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm. Crystallization and preliminary X-ray diffraction analysis of recombinant hepatitis E virus-like particle. United Kingdom. https://doi.org/10.1107/S1744309108007197
Wang, Che-Yen, Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm, Institute of Public Health, National Yang-Ming University, 112 Taipei,Taiwan, Miyazaki, Naoyuki, Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Yamashita, Tetsuo, Institute for Microbial Diseases, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Higashiura, Akifumi, Nakagawa, Atsushi, Li, Tian-Cheng, Takeda, Naokazu, Xing, Li, Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm, Hjalmarsson, Erik, Friberg, Claes, Liou, Der-Ming, Sung, Yen-Jen, Institute of Anatomy and Cell Biology, National Yang-Ming University, 112 Taipei,Taiwan, Tsukihara, Tomitake, Matsuura, Yoshiharu, Miyamura, Tatsuo, Cheng, R. Holland, E-mail: rhch@ucdavis.edu, and Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm. 2008. "Crystallization and preliminary X-ray diffraction analysis of recombinant hepatitis E virus-like particle". United Kingdom. https://doi.org/10.1107/S1744309108007197.
@article{osti_22360511,
title = {Crystallization and preliminary X-ray diffraction analysis of recombinant hepatitis E virus-like particle},
author = {Wang, Che-Yen and Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm and Institute of Public Health, National Yang-Ming University, 112 Taipei,Taiwan and Miyazaki, Naoyuki and Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm and Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871 and Yamashita, Tetsuo and Institute for Microbial Diseases, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871 and Higashiura, Akifumi and Nakagawa, Atsushi and Li, Tian-Cheng and Takeda, Naokazu and Xing, Li and Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm and Hjalmarsson, Erik and Friberg, Claes and Liou, Der-Ming and Sung, Yen-Jen and Institute of Anatomy and Cell Biology, National Yang-Ming University, 112 Taipei,Taiwan and Tsukihara, Tomitake and Matsuura, Yoshiharu and Miyamura, Tatsuo and Cheng, R. Holland, E-mail: rhch@ucdavis.edu and Karolinska Institute Structural Virology, F68 Karolinska University Hospital, SE-14186 Stockholm},
abstractNote = {A recombinant virus-like particle that is a potential oral hepatitis E vaccine was crystallized. Diffraction data were collected to 8.3 Å resolution and the X-ray structure was phased with the aid of a low-resolution density map determined using cryo-electron microscopy data. 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 P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 337, b = 343, c = 346 Å, α = β = γ = 90°, and contain one particle per asymmetric unit.},
doi = {10.1107/S1744309108007197},
url = {https://www.osti.gov/biblio/22360511}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 4,
volume = 64,
place = {United Kingdom},
year = {Tue Apr 01 00:00:00 EDT 2008},
month = {Tue Apr 01 00:00:00 EDT 2008}
}