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Progress on Poxvirus E3 Ubiquitin Ligases and Adaptor Proteins
Poxviruses have evolved a variety of innate immunity evasion mechanisms, some of which involve poxvirus-encoded E3 ubiquitin ligases and adaptor proteins. Based on their functional domains and ubiquitin transfer mechanisms, these poxvirus-encoded E3 ubiquitin ligases and adaptor proteins can be divi...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8695901/ https://www.ncbi.nlm.nih.gov/pubmed/34956175 http://dx.doi.org/10.3389/fimmu.2021.740223 |
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author | Cui, Haoran Zhang, Yaxian Zhang, Leiliang |
author_facet | Cui, Haoran Zhang, Yaxian Zhang, Leiliang |
author_sort | Cui, Haoran |
collection | PubMed |
description | Poxviruses have evolved a variety of innate immunity evasion mechanisms, some of which involve poxvirus-encoded E3 ubiquitin ligases and adaptor proteins. Based on their functional domains and ubiquitin transfer mechanisms, these poxvirus-encoded E3 ubiquitin ligases and adaptor proteins can be divided into five categories: PRANC, ANK/BC, BBK, P28/RING, and MARCH proteins. Although the substrates of many poxvirus E3 ubiquitin ligases remain to be discovered, most of the identified substrates are components of the innate immune system. In this review, we discuss the current research progress on poxvirus-encoded E3 ubiquitin ligases and adaptor proteins to provide mechanistic insights into the interplay between these viruses and their hosts. |
format | Online Article Text |
id | pubmed-8695901 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-86959012021-12-24 Progress on Poxvirus E3 Ubiquitin Ligases and Adaptor Proteins Cui, Haoran Zhang, Yaxian Zhang, Leiliang Front Immunol Immunology Poxviruses have evolved a variety of innate immunity evasion mechanisms, some of which involve poxvirus-encoded E3 ubiquitin ligases and adaptor proteins. Based on their functional domains and ubiquitin transfer mechanisms, these poxvirus-encoded E3 ubiquitin ligases and adaptor proteins can be divided into five categories: PRANC, ANK/BC, BBK, P28/RING, and MARCH proteins. Although the substrates of many poxvirus E3 ubiquitin ligases remain to be discovered, most of the identified substrates are components of the innate immune system. In this review, we discuss the current research progress on poxvirus-encoded E3 ubiquitin ligases and adaptor proteins to provide mechanistic insights into the interplay between these viruses and their hosts. Frontiers Media S.A. 2021-12-09 /pmc/articles/PMC8695901/ /pubmed/34956175 http://dx.doi.org/10.3389/fimmu.2021.740223 Text en Copyright © 2021 Cui, Zhang and Zhang https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Immunology Cui, Haoran Zhang, Yaxian Zhang, Leiliang Progress on Poxvirus E3 Ubiquitin Ligases and Adaptor Proteins |
title | Progress on Poxvirus E3 Ubiquitin Ligases and Adaptor Proteins |
title_full | Progress on Poxvirus E3 Ubiquitin Ligases and Adaptor Proteins |
title_fullStr | Progress on Poxvirus E3 Ubiquitin Ligases and Adaptor Proteins |
title_full_unstemmed | Progress on Poxvirus E3 Ubiquitin Ligases and Adaptor Proteins |
title_short | Progress on Poxvirus E3 Ubiquitin Ligases and Adaptor Proteins |
title_sort | progress on poxvirus e3 ubiquitin ligases and adaptor proteins |
topic | Immunology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8695901/ https://www.ncbi.nlm.nih.gov/pubmed/34956175 http://dx.doi.org/10.3389/fimmu.2021.740223 |
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