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Peptide inhibitors of tembusu virus infection derived from the envelope protein
The outbreak and spread of Tembusu virus (TMUV) has caused very large losses in the waterfowl-breeding industry since 2010. The viral envelope (E) protein, the principal surface protein of viral particles, plays a vital role in viral entry and fusion. In this study, two peptides derived from domain...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Published by Elsevier B.V.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7204726/ https://www.ncbi.nlm.nih.gov/pubmed/32456819 http://dx.doi.org/10.1016/j.vetmic.2020.108708 |
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author | Zhao, Dongmin Zhang, Lijiao Han, Kaikai Liu, Qingtao Yang, Jing Huang, Xinmei Liu, Yuzhuo Li, Yin Zhao, Peng |
author_facet | Zhao, Dongmin Zhang, Lijiao Han, Kaikai Liu, Qingtao Yang, Jing Huang, Xinmei Liu, Yuzhuo Li, Yin Zhao, Peng |
author_sort | Zhao, Dongmin |
collection | PubMed |
description | The outbreak and spread of Tembusu virus (TMUV) has caused very large losses in the waterfowl-breeding industry since 2010. The viral envelope (E) protein, the principal surface protein of viral particles, plays a vital role in viral entry and fusion. In this study, two peptides derived from domain II (DII) and the stem of the TMUV envelope protein, TP1 and TP2, respectively, were tested for their antiviral activity. TP1 and TP2 inhibited TMUV infection in BHK-21 cells, and their 50% inhibitory concentrations (IC(50)) were 14.19 mg/L and 7.64 mg/L, respectively. Viral inhibition assays in different cell lines of avian origin showed that the inhibitory effects of TP1 and TP2 are not cell type dependent. Moreover, TP2 also exhibited inhibitory activity against Japanese encephalitis virus (JEV) infection. The two peptides inhibited antibody-mediated TMUV infection of duck peripheral blood lymphocytes. Co-immunoprecipitation assays and indirect enzyme-linked immunosorbent assays (ELISAs) indicated that both peptides interact with the surface of the TMUV virion. RNase digestion assays confirmed the release of viral RNA following incubation with TP1, while incubation with TP1 or TP2 interfered with the binding between TMUV and cells. Taken together, these results show that TP1 and TP2 may be developed into antiviral treatments against TMUV infection. |
format | Online Article Text |
id | pubmed-7204726 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Published by Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-72047262020-05-07 Peptide inhibitors of tembusu virus infection derived from the envelope protein Zhao, Dongmin Zhang, Lijiao Han, Kaikai Liu, Qingtao Yang, Jing Huang, Xinmei Liu, Yuzhuo Li, Yin Zhao, Peng Vet Microbiol Article The outbreak and spread of Tembusu virus (TMUV) has caused very large losses in the waterfowl-breeding industry since 2010. The viral envelope (E) protein, the principal surface protein of viral particles, plays a vital role in viral entry and fusion. In this study, two peptides derived from domain II (DII) and the stem of the TMUV envelope protein, TP1 and TP2, respectively, were tested for their antiviral activity. TP1 and TP2 inhibited TMUV infection in BHK-21 cells, and their 50% inhibitory concentrations (IC(50)) were 14.19 mg/L and 7.64 mg/L, respectively. Viral inhibition assays in different cell lines of avian origin showed that the inhibitory effects of TP1 and TP2 are not cell type dependent. Moreover, TP2 also exhibited inhibitory activity against Japanese encephalitis virus (JEV) infection. The two peptides inhibited antibody-mediated TMUV infection of duck peripheral blood lymphocytes. Co-immunoprecipitation assays and indirect enzyme-linked immunosorbent assays (ELISAs) indicated that both peptides interact with the surface of the TMUV virion. RNase digestion assays confirmed the release of viral RNA following incubation with TP1, while incubation with TP1 or TP2 interfered with the binding between TMUV and cells. Taken together, these results show that TP1 and TP2 may be developed into antiviral treatments against TMUV infection. Published by Elsevier B.V. 2020-06 2020-05-07 /pmc/articles/PMC7204726/ /pubmed/32456819 http://dx.doi.org/10.1016/j.vetmic.2020.108708 Text en © 2020 Published by Elsevier B.V. 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 Zhang, Lijiao Han, Kaikai Liu, Qingtao Yang, Jing Huang, Xinmei Liu, Yuzhuo Li, Yin Zhao, Peng Peptide inhibitors of tembusu virus infection derived from the envelope protein |
title | Peptide inhibitors of tembusu virus infection derived from the envelope protein |
title_full | Peptide inhibitors of tembusu virus infection derived from the envelope protein |
title_fullStr | Peptide inhibitors of tembusu virus infection derived from the envelope protein |
title_full_unstemmed | Peptide inhibitors of tembusu virus infection derived from the envelope protein |
title_short | Peptide inhibitors of tembusu virus infection derived from the envelope protein |
title_sort | peptide inhibitors of tembusu virus infection derived from the envelope protein |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7204726/ https://www.ncbi.nlm.nih.gov/pubmed/32456819 http://dx.doi.org/10.1016/j.vetmic.2020.108708 |
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