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Structure and function of capsid protein in flavivirus infection and its applications in the development of vaccines and therapeutics
Flaviviruses are enveloped single positive-stranded RNA viruses. The capsid (C), a structural protein of flavivirus, is dimeric and alpha-helical, with several special structural and functional features. The functions of the C protein go far beyond a structural role in virions. It is not only respon...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8247181/ https://www.ncbi.nlm.nih.gov/pubmed/34193256 http://dx.doi.org/10.1186/s13567-021-00966-2 |
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author | Zhang, Xingcui Zhang, Yanting Jia, Renyong Wang, Mingshu Yin, Zhongqiong Cheng, Anchun |
author_facet | Zhang, Xingcui Zhang, Yanting Jia, Renyong Wang, Mingshu Yin, Zhongqiong Cheng, Anchun |
author_sort | Zhang, Xingcui |
collection | PubMed |
description | Flaviviruses are enveloped single positive-stranded RNA viruses. The capsid (C), a structural protein of flavivirus, is dimeric and alpha-helical, with several special structural and functional features. The functions of the C protein go far beyond a structural role in virions. It is not only responsible for encapsidation to protect the viral RNA but also able to interact with various host proteins to promote virus proliferation. Therefore, the C protein plays an important role in infected host cells and the viral life cycle. Flaviviruses have been shown to affect the health of humans and animals. Thus, there is an urgent need to effectively control flavivirus infections. The structure of the flavivirus virion has been determined, but there is relatively little information about the function of the C protein. Hence, a greater understanding of the role of the C protein in viral infections will help to discover novel antiviral strategies and provide a promising starting point for the further development of flavivirus vaccines or therapeutics. |
format | Online Article Text |
id | pubmed-8247181 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-82471812021-07-06 Structure and function of capsid protein in flavivirus infection and its applications in the development of vaccines and therapeutics Zhang, Xingcui Zhang, Yanting Jia, Renyong Wang, Mingshu Yin, Zhongqiong Cheng, Anchun Vet Res Review Flaviviruses are enveloped single positive-stranded RNA viruses. The capsid (C), a structural protein of flavivirus, is dimeric and alpha-helical, with several special structural and functional features. The functions of the C protein go far beyond a structural role in virions. It is not only responsible for encapsidation to protect the viral RNA but also able to interact with various host proteins to promote virus proliferation. Therefore, the C protein plays an important role in infected host cells and the viral life cycle. Flaviviruses have been shown to affect the health of humans and animals. Thus, there is an urgent need to effectively control flavivirus infections. The structure of the flavivirus virion has been determined, but there is relatively little information about the function of the C protein. Hence, a greater understanding of the role of the C protein in viral infections will help to discover novel antiviral strategies and provide a promising starting point for the further development of flavivirus vaccines or therapeutics. BioMed Central 2021-06-30 2021 /pmc/articles/PMC8247181/ /pubmed/34193256 http://dx.doi.org/10.1186/s13567-021-00966-2 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Review Zhang, Xingcui Zhang, Yanting Jia, Renyong Wang, Mingshu Yin, Zhongqiong Cheng, Anchun Structure and function of capsid protein in flavivirus infection and its applications in the development of vaccines and therapeutics |
title | Structure and function of capsid protein in flavivirus infection and its applications in the development of vaccines and therapeutics |
title_full | Structure and function of capsid protein in flavivirus infection and its applications in the development of vaccines and therapeutics |
title_fullStr | Structure and function of capsid protein in flavivirus infection and its applications in the development of vaccines and therapeutics |
title_full_unstemmed | Structure and function of capsid protein in flavivirus infection and its applications in the development of vaccines and therapeutics |
title_short | Structure and function of capsid protein in flavivirus infection and its applications in the development of vaccines and therapeutics |
title_sort | structure and function of capsid protein in flavivirus infection and its applications in the development of vaccines and therapeutics |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8247181/ https://www.ncbi.nlm.nih.gov/pubmed/34193256 http://dx.doi.org/10.1186/s13567-021-00966-2 |
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