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Characterization of self-assembled virus-like particles of dromedary camel hepatitis e virus generated by recombinant baculoviruses
Dromedary camel hepatitis E virus (DcHEV), a novel hepatitis E virus, has been identified in dromedary camels in Dubai, United Arab Emirates. The antigenicity, pathogenicity and epidemiology of this virus have been unclear. Here we first used a recombinant baculovirus expression system to express th...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier B.V.
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114528/ https://www.ncbi.nlm.nih.gov/pubmed/26160190 http://dx.doi.org/10.1016/j.virusres.2015.06.022 |
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author | Zhou, Xianfeng Kataoka, Michiyo Liu, Zheng Takeda, Naokazu Wakita, Takaji Li, Tian-Cheng |
author_facet | Zhou, Xianfeng Kataoka, Michiyo Liu, Zheng Takeda, Naokazu Wakita, Takaji Li, Tian-Cheng |
author_sort | Zhou, Xianfeng |
collection | PubMed |
description | Dromedary camel hepatitis E virus (DcHEV), a novel hepatitis E virus, has been identified in dromedary camels in Dubai, United Arab Emirates. The antigenicity, pathogenicity and epidemiology of this virus have been unclear. Here we first used a recombinant baculovirus expression system to express the 13 and 111 N-terminus amino-acid-truncated DcHEV ORF2 protein in insect Tn5 cells, and we obtained two types of virus-like particles (VLPs) with densities of 1.300 g/cm(3) and 1.285 g/cm(3), respectively. The small VLPs (Dc4sVLPs) were estimated to be 24 nm in diameter, and were assembled by a protein with the molecular mass 53 kDa. The large VLPs (Dc3nVLPs and Dc4nVLPs) were 35 nm in diameter, and were assembled by a 64-kDa protein. An antigenic analysis demonstrated that DcHEV was cross-reactive with G1, G3–G6, ferret and rat HEVs, and DcHEV showed a stronger cross-reactivity to G1 G3–G6 HEV than it did to rat and ferret HEV. In addition, the antibody against DcHEV-LPs neutralized G1 and G3 HEV in a cell culture system, suggesting that the serotypes of these HEVs are identical. We also found that the amino acid residue Met-358 affects the small DcHEV-LPs assembly. |
format | Online Article Text |
id | pubmed-7114528 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71145282020-04-02 Characterization of self-assembled virus-like particles of dromedary camel hepatitis e virus generated by recombinant baculoviruses Zhou, Xianfeng Kataoka, Michiyo Liu, Zheng Takeda, Naokazu Wakita, Takaji Li, Tian-Cheng Virus Res Article Dromedary camel hepatitis E virus (DcHEV), a novel hepatitis E virus, has been identified in dromedary camels in Dubai, United Arab Emirates. The antigenicity, pathogenicity and epidemiology of this virus have been unclear. Here we first used a recombinant baculovirus expression system to express the 13 and 111 N-terminus amino-acid-truncated DcHEV ORF2 protein in insect Tn5 cells, and we obtained two types of virus-like particles (VLPs) with densities of 1.300 g/cm(3) and 1.285 g/cm(3), respectively. The small VLPs (Dc4sVLPs) were estimated to be 24 nm in diameter, and were assembled by a protein with the molecular mass 53 kDa. The large VLPs (Dc3nVLPs and Dc4nVLPs) were 35 nm in diameter, and were assembled by a 64-kDa protein. An antigenic analysis demonstrated that DcHEV was cross-reactive with G1, G3–G6, ferret and rat HEVs, and DcHEV showed a stronger cross-reactivity to G1 G3–G6 HEV than it did to rat and ferret HEV. In addition, the antibody against DcHEV-LPs neutralized G1 and G3 HEV in a cell culture system, suggesting that the serotypes of these HEVs are identical. We also found that the amino acid residue Met-358 affects the small DcHEV-LPs assembly. Elsevier B.V. 2015-12-02 2015-07-06 /pmc/articles/PMC7114528/ /pubmed/26160190 http://dx.doi.org/10.1016/j.virusres.2015.06.022 Text en Copyright © 2015 Elsevier B.V. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Zhou, Xianfeng Kataoka, Michiyo Liu, Zheng Takeda, Naokazu Wakita, Takaji Li, Tian-Cheng Characterization of self-assembled virus-like particles of dromedary camel hepatitis e virus generated by recombinant baculoviruses |
title | Characterization of self-assembled virus-like particles of dromedary camel hepatitis e virus generated by recombinant baculoviruses |
title_full | Characterization of self-assembled virus-like particles of dromedary camel hepatitis e virus generated by recombinant baculoviruses |
title_fullStr | Characterization of self-assembled virus-like particles of dromedary camel hepatitis e virus generated by recombinant baculoviruses |
title_full_unstemmed | Characterization of self-assembled virus-like particles of dromedary camel hepatitis e virus generated by recombinant baculoviruses |
title_short | Characterization of self-assembled virus-like particles of dromedary camel hepatitis e virus generated by recombinant baculoviruses |
title_sort | characterization of self-assembled virus-like particles of dromedary camel hepatitis e virus generated by recombinant baculoviruses |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114528/ https://www.ncbi.nlm.nih.gov/pubmed/26160190 http://dx.doi.org/10.1016/j.virusres.2015.06.022 |
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