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...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-10-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/13/11/2124 |
| _version_ | 1797508203845517312 |
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| author | Guoguo Wang Mengjia Xie Wei Wu Zhongzhou Chen |
| author_facet | Guoguo Wang Mengjia Xie Wei Wu Zhongzhou Chen |
| author_sort | Guoguo Wang |
| collection | DOAJ |
| 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 <i>B646L</i>), 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. |
| first_indexed | 2024-03-10T04:59:04Z |
| format | Article |
| id | doaj.art-53001910f27a456dbbbfe9a7ea628bea |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-10T04:59:04Z |
| publishDate | 2021-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-53001910f27a456dbbbfe9a7ea628bea2023-11-23T01:55:12ZengMDPI AGViruses1999-49152021-10-011311212410.3390/v13112124Structures and Functional Diversities of ASFV ProteinsGuoguo Wang0Mengjia Xie1Wei Wu2Zhongzhou Chen3State Key Laboratory of Agrobiotechnology and Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Biological Sciences, China Agricultural University, Beijing 100193, ChinaState Key Laboratory of Agrobiotechnology and Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Biological Sciences, China Agricultural University, Beijing 100193, ChinaState Key Laboratory of Agrobiotechnology and Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Biological Sciences, China Agricultural University, Beijing 100193, ChinaState Key Laboratory of Agrobiotechnology and Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Biological Sciences, China Agricultural University, Beijing 100193, ChinaAfrican 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 <i>B646L</i>), 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.https://www.mdpi.com/1999-4915/13/11/2124African swine fever virusASFVstructuressurvivalAP endonucleasedUTPases |
| spellingShingle | Guoguo Wang Mengjia Xie Wei Wu Zhongzhou Chen Structures and Functional Diversities of ASFV Proteins Viruses African swine fever virus ASFV structures survival AP endonuclease dUTPases |
| 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 | African swine fever virus ASFV structures survival AP endonuclease dUTPases |
| url | https://www.mdpi.com/1999-4915/13/11/2124 |
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