Structures and Functional Diversities of ASFV Proteins

被引:89
作者
Wang, Guoguo
Xie, Mengjia
Wu, Wei
Chen, Zhongzhou [1 ]
机构
[1] China Agr Univ, State Key Lab Agrobiotechnol, Beijing 100193, Peoples R China
来源
VIRUSES-BASEL | 2021年 / 13卷 / 11期
基金
中国国家自然科学基金;
关键词
African swine fever virus; ASFV; structures; survival; AP endonuclease; dUTPases; pS273R; p72; AsfvPolX; AsfvLIG; SWINE-FEVER VIRUS; DNA-POLYMERASE-X; REPLICATION; TRANSMISSION; POLYPROTEIN; INHIBITION; MECHANISM; SEQUENCE; DUTPASE; FAMILY;
D O I
10.3390/v13112124
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
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页数:11
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