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Truncated glycoprotein E of varicella-zoster virus is an ideal immunogen for Escherichia coli-based vaccine design
Varicella-zoster virus (VZV) is a highly infectious agent responsible for both varicella and herpes zoster disease. Despite high efficacy, there remain safety and accessibility concerns with the licensed vaccines. Here, we sought to produce a VZV gE immunogen using an E. coli expression system. We f...
Autores principales: | , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Science China Press
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9930067/ https://www.ncbi.nlm.nih.gov/pubmed/36790656 http://dx.doi.org/10.1007/s11427-022-2264-1 |
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author | Chen, Tingting Sun, Jie Zhang, Sibo Li, Tingting Liu, Liqin Xue, Wenhui Zhou, Lizhi Liang, Siting Yu, Zhili Zheng, Qingbing Yu, Hai Cheng, Tong Zhang, Jun Gu, Ying Li, Shaowei Xia, Ningshao |
author_facet | Chen, Tingting Sun, Jie Zhang, Sibo Li, Tingting Liu, Liqin Xue, Wenhui Zhou, Lizhi Liang, Siting Yu, Zhili Zheng, Qingbing Yu, Hai Cheng, Tong Zhang, Jun Gu, Ying Li, Shaowei Xia, Ningshao |
author_sort | Chen, Tingting |
collection | PubMed |
description | Varicella-zoster virus (VZV) is a highly infectious agent responsible for both varicella and herpes zoster disease. Despite high efficacy, there remain safety and accessibility concerns with the licensed vaccines. Here, we sought to produce a VZV gE immunogen using an E. coli expression system. We found that the soluble expression and yield of gE protein could be enhanced via C-terminal truncations to the protein, thereby facilitating a robust and scalable purification process for the purpose of vaccine manufacturing. The lead truncated gE (aa 31–358), hereafter referred to as tgE, was a homogenous monomer in solution and showed excellent antigenicity. Finally, we assessed and compared the immunogenicity of tgE with commercial vOka LAV and Shingrix vaccine. We found that aluminum-adjuvanted tgE was immunogenic as compared with vOka LAV. When adjuvanted with AS01(B), a two-dose immunization of tgE showed comparable or better potency in antibody responses and cell-mediated immunity with those of the Shingrix vaccine at the same dosage, especially in terms of the proportion of IFN-γ-expressing CD4(+) T cells. In conclusion, this method of E. coli-mediate tgE expression offers a cost-effective and scalable strategy to generate an ideal VZV gE immunogen for the development of both varicella and zoster vaccines. |
format | Online Article Text |
id | pubmed-9930067 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Science China Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-99300672023-02-15 Truncated glycoprotein E of varicella-zoster virus is an ideal immunogen for Escherichia coli-based vaccine design Chen, Tingting Sun, Jie Zhang, Sibo Li, Tingting Liu, Liqin Xue, Wenhui Zhou, Lizhi Liang, Siting Yu, Zhili Zheng, Qingbing Yu, Hai Cheng, Tong Zhang, Jun Gu, Ying Li, Shaowei Xia, Ningshao Sci China Life Sci Research Paper Varicella-zoster virus (VZV) is a highly infectious agent responsible for both varicella and herpes zoster disease. Despite high efficacy, there remain safety and accessibility concerns with the licensed vaccines. Here, we sought to produce a VZV gE immunogen using an E. coli expression system. We found that the soluble expression and yield of gE protein could be enhanced via C-terminal truncations to the protein, thereby facilitating a robust and scalable purification process for the purpose of vaccine manufacturing. The lead truncated gE (aa 31–358), hereafter referred to as tgE, was a homogenous monomer in solution and showed excellent antigenicity. Finally, we assessed and compared the immunogenicity of tgE with commercial vOka LAV and Shingrix vaccine. We found that aluminum-adjuvanted tgE was immunogenic as compared with vOka LAV. When adjuvanted with AS01(B), a two-dose immunization of tgE showed comparable or better potency in antibody responses and cell-mediated immunity with those of the Shingrix vaccine at the same dosage, especially in terms of the proportion of IFN-γ-expressing CD4(+) T cells. In conclusion, this method of E. coli-mediate tgE expression offers a cost-effective and scalable strategy to generate an ideal VZV gE immunogen for the development of both varicella and zoster vaccines. Science China Press 2023-02-09 2023 /pmc/articles/PMC9930067/ /pubmed/36790656 http://dx.doi.org/10.1007/s11427-022-2264-1 Text en © Science China Press 2023 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Research Paper Chen, Tingting Sun, Jie Zhang, Sibo Li, Tingting Liu, Liqin Xue, Wenhui Zhou, Lizhi Liang, Siting Yu, Zhili Zheng, Qingbing Yu, Hai Cheng, Tong Zhang, Jun Gu, Ying Li, Shaowei Xia, Ningshao Truncated glycoprotein E of varicella-zoster virus is an ideal immunogen for Escherichia coli-based vaccine design |
title | Truncated glycoprotein E of varicella-zoster virus is an ideal immunogen for Escherichia coli-based vaccine design |
title_full | Truncated glycoprotein E of varicella-zoster virus is an ideal immunogen for Escherichia coli-based vaccine design |
title_fullStr | Truncated glycoprotein E of varicella-zoster virus is an ideal immunogen for Escherichia coli-based vaccine design |
title_full_unstemmed | Truncated glycoprotein E of varicella-zoster virus is an ideal immunogen for Escherichia coli-based vaccine design |
title_short | Truncated glycoprotein E of varicella-zoster virus is an ideal immunogen for Escherichia coli-based vaccine design |
title_sort | truncated glycoprotein e of varicella-zoster virus is an ideal immunogen for escherichia coli-based vaccine design |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9930067/ https://www.ncbi.nlm.nih.gov/pubmed/36790656 http://dx.doi.org/10.1007/s11427-022-2264-1 |
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