Abstract
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.
Highlights
African swine fever (ASF) is an acute hemorrhagic viral disease caused by the African swine fever virus (ASFV), affecting wild boar and domestic pigs
A great deal of large DNA viruses have been found in the past two decades, and few of them have caused as great an economic impact to society as ASFV [2]
ASFV pB119L belongs to the Erv1p/Alrp family of sulfhydryl oxidases and has been described as a late nonstructural protein required for correct virus assembly, performing its activity by catalyzing the formation of disulfide bonds
Summary
African swine fever (ASF) is an acute hemorrhagic viral disease caused by the African swine fever virus (ASFV), affecting wild boar and domestic pigs. Differed from other Aps, AsfvAP adopts a unique DNA-binding mode [19] It has new structural features, including one narrower nucleotide-binding pocket at the active site, a histidine-rich region R2, and a C16–C20 disulfide bond containing region R1 (Figure 2). These features are important for AsfvAP to adapt to the acidic and oxidative environment [23]. DNA binding is the rate-limiting step of the catalytic efficiency of AsfvPolX [30] In a word, these three enzymes are important in the BER system, which repairs damaged DNA throughout the cell cycle, and are beneficial to the virus survival and evolution
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