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Identification and Characterization of a Novel Epitope of ASFV-Encoded dUTPase by Monoclonal Antibodies

文献类型： 外文期刊

作者： Zhang, Shuai 1 ; Wang, Rui 1 ; Zhu, Xiaojing 1 ; Jin, Jiaxin 1 ; Lu, Wenlong 1 ; Zhao, Xuyang 1 ; Wan, Bo 1 ; Liao, Yifei 3 ; Zhao, Qin 4 ; Netherton, Christopher L. 5 ; Zhuang, Guoqing 1 ; Sun, Aijun 1 ; Zhang, Gaiping 1 ;

作者机构： 1.Henan Agr Univ, Coll Vet Med, Zhengzhou 450046, Peoples R China

2.Henan Agr Univ, Coll Vet Med, Int Joint Res Ctr Natl Anim Immunol, Zhengzhou 450046, Peoples R China

3.Harvard Med Sch, Brigham & Womens Hosp, Dept Med, Div Infect Dis, Boston, MA 02115 USA

4.Northwest A&F Univ, Coll Vet Med, Dept Prevent Vet Med, Xianyang 712100, Peoples R China

5.Pirbright Inst, Ash Rd, Surrey GU24 0NF, England

6.Minist Agr & Rural Afairs, Key Lab Anim Immunol, Zhengzhou 450002, Peoples R China

7.Henan Acad Agr Sci, Henan Prov Key Lab Anim Immunol, Zhengzhou 450002, Peoples R China

关键词： African swine fever virus; African swine fever; dUTPase; epitope; therapeutic drug

期刊名称：VIRUSES-BASEL （ 影响因子：5.818； 五年影响因子：5.811 ）

ISSN：

年卷期： 2021 年 13 卷 11 期

页码：

收录情况： SCI

摘要： Deoxyuridine 5 & PRIME;-triphosphate nucleotidohydrolase (dUTPase) of African swine fever virus (ASFV) is an essential enzyme required for efficient virus replication. Previous crystallography data have indicated that dUTPase (E165R) may serve as a therapeutic target for inhibiting ASFV replication; however, the specificity of the targeting site(s) in ASFV dUTPase remains unclear. In this study, 19 mouse monoclonal antibodies (mAbs) were produced, in which four mAbs showed inhibitory reactivity against E165R recombinant protein. Epitope mapping studies indicated that E165R has three major antigenic regions: 100-120 aa, 120-140 aa, and 140-165 aa. Three mAbs inhibited the dUTPase activity of E165R by binding to the highly conserved 149-RGEGRFGSTG-158 amino acid sequence. Interestingly, 8F6 mAb specifically recognized ASFV dUTPase but not Sus scrofa dUTPase, which may be due to structural differences in the amino acids of F151, R153, and F154 in the motif V region. In summary, we developed anti-E165R-specific mAbs, and identified an important antibody-binding antigenic epitope in the motif V of ASFV dUTPase. Our study provides a comprehensive analysis of mAbs that target the antigenic epitope of ASFV dUTPase, which may contribute to the development of novel antibody-based ASFV therapeutics.

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