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Domain I and II from newly emerging goose tembusu virus envelope protein functions as a dominant-negative inhibitor of virus infectivity
Flavivirus envelope protein locates at the outermost surface of viral particle and mediates virus entry and fusion infection, and domains I and II of E protein play an important role in this process. In this study, we have expressed and purified goose tembusu virus (GTV) E protein domains I and II (...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Ltd.
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7172782/ https://www.ncbi.nlm.nih.gov/pubmed/25481678 http://dx.doi.org/10.1016/j.rvsc.2014.11.003 |
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author | Zhao, Dongmin Huang, Xinmei Liu, Yuzhuo Han, Kaikai Zhang, Jingfeng Yang, Jing Xie, Xingxing Li, Yin |
author_facet | Zhao, Dongmin Huang, Xinmei Liu, Yuzhuo Han, Kaikai Zhang, Jingfeng Yang, Jing Xie, Xingxing Li, Yin |
author_sort | Zhao, Dongmin |
collection | PubMed |
description | Flavivirus envelope protein locates at the outermost surface of viral particle and mediates virus entry and fusion infection, and domains I and II of E protein play an important role in this process. In this study, we have expressed and purified goose tembusu virus (GTV) E protein domains I and II (DI/II) from E. coli, and tested conceptual approach that purified protein serves as anti-viral reagent. We found that DI/II inhibited GTV JS804 infection in BHK-21 cells in a dose-dependent manner, and this inhibition activity was achieved by binding to cell membrane specifically. Moreover, JS804 treated with DI/II specific anti-serum decreased its infectivity to BHK-21 cells. Taken together, this is first to show that the purified DI/II domain of tembusu virus expressed in E. coli was able to interfere with virus infection, which opens an avenue to develop novel anti-viral regents to prevent and eventually eradicate GTV infection. |
format | Online Article Text |
id | pubmed-7172782 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Elsevier Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71727822020-04-22 Domain I and II from newly emerging goose tembusu virus envelope protein functions as a dominant-negative inhibitor of virus infectivity Zhao, Dongmin Huang, Xinmei Liu, Yuzhuo Han, Kaikai Zhang, Jingfeng Yang, Jing Xie, Xingxing Li, Yin Res Vet Sci Article Flavivirus envelope protein locates at the outermost surface of viral particle and mediates virus entry and fusion infection, and domains I and II of E protein play an important role in this process. In this study, we have expressed and purified goose tembusu virus (GTV) E protein domains I and II (DI/II) from E. coli, and tested conceptual approach that purified protein serves as anti-viral reagent. We found that DI/II inhibited GTV JS804 infection in BHK-21 cells in a dose-dependent manner, and this inhibition activity was achieved by binding to cell membrane specifically. Moreover, JS804 treated with DI/II specific anti-serum decreased its infectivity to BHK-21 cells. Taken together, this is first to show that the purified DI/II domain of tembusu virus expressed in E. coli was able to interfere with virus infection, which opens an avenue to develop novel anti-viral regents to prevent and eventually eradicate GTV infection. Elsevier Ltd. 2015-02 2014-11-18 /pmc/articles/PMC7172782/ /pubmed/25481678 http://dx.doi.org/10.1016/j.rvsc.2014.11.003 Text en Copyright © 2014 Elsevier Ltd. 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 Zhao, Dongmin Huang, Xinmei Liu, Yuzhuo Han, Kaikai Zhang, Jingfeng Yang, Jing Xie, Xingxing Li, Yin Domain I and II from newly emerging goose tembusu virus envelope protein functions as a dominant-negative inhibitor of virus infectivity |
title | Domain I and II from newly emerging goose tembusu virus envelope protein functions as a dominant-negative inhibitor of virus infectivity |
title_full | Domain I and II from newly emerging goose tembusu virus envelope protein functions as a dominant-negative inhibitor of virus infectivity |
title_fullStr | Domain I and II from newly emerging goose tembusu virus envelope protein functions as a dominant-negative inhibitor of virus infectivity |
title_full_unstemmed | Domain I and II from newly emerging goose tembusu virus envelope protein functions as a dominant-negative inhibitor of virus infectivity |
title_short | Domain I and II from newly emerging goose tembusu virus envelope protein functions as a dominant-negative inhibitor of virus infectivity |
title_sort | domain i and ii from newly emerging goose tembusu virus envelope protein functions as a dominant-negative inhibitor of virus infectivity |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7172782/ https://www.ncbi.nlm.nih.gov/pubmed/25481678 http://dx.doi.org/10.1016/j.rvsc.2014.11.003 |
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