Structural insights into the CP312R protein of the African swine fever virus

被引：7

作者：

Chen, Lifei ^{[1
,2
]}

Chen, Leiqing ^{[1
,2
]}

Chen, Huan ^{[3
]}

Zhang, Hong ^{[1
,2
]}

Dong, PanPan ^{[1
,2
]}

Sun, Lifang ^{[1
,2
]}

Huang, Xiaojing ^{[1
,2
]}

Lin, Pingdong ^{[1
,2
]}

Wu, Linjiao ^{[1
,2
]}

Jing, Dingding ^{[1
,2
]}

Qian, Yingjuan ^{[3
]}

Wu, Yunkun ^{[1
,2
]}

机构：

[1] Fujian Normal Univ, Coll Life Sci, Prov Univ Key Lab Cellular Stress Response & Meta, Fuzhou 350117, Peoples R China

[2] Fujian Normal Univ, Coll Life Sci, Fujian Key Lab Dev & Neural Biol, Fuzhou 350117, Peoples R China

[3] Nanjing Agr Univ, Coll Vet Med, MOE Joint Int Res Lab Anim Hlth & Food Safety, Nanjing, Jiangsu, Peoples R China

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2022年 / 624卷

基金：

中国国家自然科学基金;

关键词：

African swine fever virus; CP312R; Crystal structure; Single-stranded DNA binding Protein; OB-Fold; DNA-BINDING;

D O I：

10.1016/j.bbrc.2022.07.091

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

African swine fever (ASF) is a lethal hemorrhagic disease that affects domestic pigs and wild boars. There is no medication available for ASF to date. The ability to mount antigen-specific responses to viral vectored CP312R makes it a crucial potential target for designing vaccines or drugs. This study determined the crystal structure of ASFV CP312R at 2.32 A and found it to be a monomer with a single-stranded DNA binding core domain with a clear five-strands b-barrel OB-fold architecture. Electrophoretic mobility shift assay and size-exclusion chromatography characterization assay further confirmed the single-stranded DNA (ssDNA)-binding property of ASFV CP312R. This study revealed the structure and preliminary ssDNA interaction mechanisms of ASFV CP312R, providing new clues for developing new antiviral strategies. (C) 2022 Elsevier Inc. All rights reserved.

引用

页码：68 / 74

页数：7

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