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Griffithsin binds to the glycosylated proteins (E and prM) of Japanese encephalitis virus and inhibit its infection
Griffithsin (GRFT) is a broad-spectrum antiviral protein against several glycosylated viruses. In our previous publication, we have shown that GRFT exerted antiviral activity against Japanese encephalitis virus (JEV) infection. Herein, we further elucidated the mechanism by which GRFT inhibits JEV i...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier B.V.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114533/ https://www.ncbi.nlm.nih.gov/pubmed/26820432 http://dx.doi.org/10.1016/j.virusres.2016.01.016 |
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author | Ishag, Hassan Z.A. Li, Chen Wang, Fengjuan Mao, Xiang |
author_facet | Ishag, Hassan Z.A. Li, Chen Wang, Fengjuan Mao, Xiang |
author_sort | Ishag, Hassan Z.A. |
collection | PubMed |
description | Griffithsin (GRFT) is a broad-spectrum antiviral protein against several glycosylated viruses. In our previous publication, we have shown that GRFT exerted antiviral activity against Japanese encephalitis virus (JEV) infection. Herein, we further elucidated the mechanism by which GRFT inhibits JEV infection in BHK-21 cells. In vitro experiments using Pull-down assay and Co-immunoprecipitation (CO-IP) assay showed that GRFT binds to the JEV glycosylated viral proteins, specifically the enveloped (E) and premature (prM) glycoproteins. The binding of GRFT to the JEV was competitively inhibited by increasing concentrations of mannose; in turns abolished anti-JEV activity of GRFT. We suggested that, the binding of GRFT to the glycosylated viral proteins may contribute to its anti-JEV activity. Collectively, our data indicated a possible mechanism by which GRFT exerted its anti-JEV activity. This observation suggests GRFT's potentials in the development of therapeutics against JEV or other flavivirus infection. |
format | Online Article Text |
id | pubmed-7114533 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71145332020-04-02 Griffithsin binds to the glycosylated proteins (E and prM) of Japanese encephalitis virus and inhibit its infection Ishag, Hassan Z.A. Li, Chen Wang, Fengjuan Mao, Xiang Virus Res Article Griffithsin (GRFT) is a broad-spectrum antiviral protein against several glycosylated viruses. In our previous publication, we have shown that GRFT exerted antiviral activity against Japanese encephalitis virus (JEV) infection. Herein, we further elucidated the mechanism by which GRFT inhibits JEV infection in BHK-21 cells. In vitro experiments using Pull-down assay and Co-immunoprecipitation (CO-IP) assay showed that GRFT binds to the JEV glycosylated viral proteins, specifically the enveloped (E) and premature (prM) glycoproteins. The binding of GRFT to the JEV was competitively inhibited by increasing concentrations of mannose; in turns abolished anti-JEV activity of GRFT. We suggested that, the binding of GRFT to the glycosylated viral proteins may contribute to its anti-JEV activity. Collectively, our data indicated a possible mechanism by which GRFT exerted its anti-JEV activity. This observation suggests GRFT's potentials in the development of therapeutics against JEV or other flavivirus infection. Elsevier B.V. 2016-04-02 2016-01-25 /pmc/articles/PMC7114533/ /pubmed/26820432 http://dx.doi.org/10.1016/j.virusres.2016.01.016 Text en Copyright © 2016 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 Ishag, Hassan Z.A. Li, Chen Wang, Fengjuan Mao, Xiang Griffithsin binds to the glycosylated proteins (E and prM) of Japanese encephalitis virus and inhibit its infection |
title | Griffithsin binds to the glycosylated proteins (E and prM) of Japanese encephalitis virus and inhibit its infection |
title_full | Griffithsin binds to the glycosylated proteins (E and prM) of Japanese encephalitis virus and inhibit its infection |
title_fullStr | Griffithsin binds to the glycosylated proteins (E and prM) of Japanese encephalitis virus and inhibit its infection |
title_full_unstemmed | Griffithsin binds to the glycosylated proteins (E and prM) of Japanese encephalitis virus and inhibit its infection |
title_short | Griffithsin binds to the glycosylated proteins (E and prM) of Japanese encephalitis virus and inhibit its infection |
title_sort | griffithsin binds to the glycosylated proteins (e and prm) of japanese encephalitis virus and inhibit its infection |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114533/ https://www.ncbi.nlm.nih.gov/pubmed/26820432 http://dx.doi.org/10.1016/j.virusres.2016.01.016 |
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