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Structures and Functional Diversities of ASFV Proteins
African swine fever virus (ASFV), the causative pathogen of the recent ASF epidemic, is a highly contagious double-stranded DNA virus. Its genome is in the range of 170~193 kbp and encodes 68 structural proteins and over 100 non-structural proteins. Its high pathogenicity strains cause nearly 100% m...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8619059/ https://www.ncbi.nlm.nih.gov/pubmed/34834930 http://dx.doi.org/10.3390/v13112124 |
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author | Wang, Guoguo Xie, Mengjia Wu, Wei Chen, Zhongzhou |
author_facet | Wang, Guoguo Xie, Mengjia Wu, Wei Chen, Zhongzhou |
author_sort | Wang, Guoguo |
collection | PubMed |
description | African swine fever virus (ASFV), the causative pathogen of the recent ASF epidemic, is a highly contagious double-stranded DNA virus. Its genome is in the range of 170~193 kbp and encodes 68 structural proteins and over 100 non-structural proteins. Its high pathogenicity strains cause nearly 100% mortality in swine. Consisting of four layers of protein shells and an inner genome, its structure is obviously more complicated than many other viruses, and its multi-layered structures play different kinds of roles in ASFV replication and survival. Each layer possesses many proteins, but very few of the proteins have been investigated at a structural level. Here, we concluded all the ASFV proteins whose structures were unveiled, and explained their functions from the view of structures. Those structures include ASFV AP endonuclease, dUTPases (E165R), pS273R protease, core shell proteins p15 and p35, non-structural proteins pA151R, pNP868R (RNA guanylyltransferase), major capsid protein p72 (gene B646L), Bcl-2-like protein A179L, histone-like protein pA104R, sulfhydryl oxidase pB119L, polymerase X and ligase. These novel structural features, diverse functions, and complex molecular mechanisms promote ASFV to escape the host immune system easily and make this large virus difficult to control. |
format | Online Article Text |
id | pubmed-8619059 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-86190592021-11-27 Structures and Functional Diversities of ASFV Proteins Wang, Guoguo Xie, Mengjia Wu, Wei Chen, Zhongzhou Viruses Review African swine fever virus (ASFV), the causative pathogen of the recent ASF epidemic, is a highly contagious double-stranded DNA virus. Its genome is in the range of 170~193 kbp and encodes 68 structural proteins and over 100 non-structural proteins. Its high pathogenicity strains cause nearly 100% mortality in swine. Consisting of four layers of protein shells and an inner genome, its structure is obviously more complicated than many other viruses, and its multi-layered structures play different kinds of roles in ASFV replication and survival. Each layer possesses many proteins, but very few of the proteins have been investigated at a structural level. Here, we concluded all the ASFV proteins whose structures were unveiled, and explained their functions from the view of structures. Those structures include ASFV AP endonuclease, dUTPases (E165R), pS273R protease, core shell proteins p15 and p35, non-structural proteins pA151R, pNP868R (RNA guanylyltransferase), major capsid protein p72 (gene B646L), Bcl-2-like protein A179L, histone-like protein pA104R, sulfhydryl oxidase pB119L, polymerase X and ligase. These novel structural features, diverse functions, and complex molecular mechanisms promote ASFV to escape the host immune system easily and make this large virus difficult to control. MDPI 2021-10-21 /pmc/articles/PMC8619059/ /pubmed/34834930 http://dx.doi.org/10.3390/v13112124 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Wang, Guoguo Xie, Mengjia Wu, Wei Chen, Zhongzhou Structures and Functional Diversities of ASFV Proteins |
title | Structures and Functional Diversities of ASFV Proteins |
title_full | Structures and Functional Diversities of ASFV Proteins |
title_fullStr | Structures and Functional Diversities of ASFV Proteins |
title_full_unstemmed | Structures and Functional Diversities of ASFV Proteins |
title_short | Structures and Functional Diversities of ASFV Proteins |
title_sort | structures and functional diversities of asfv proteins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8619059/ https://www.ncbi.nlm.nih.gov/pubmed/34834930 http://dx.doi.org/10.3390/v13112124 |
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