Thonningianin A disrupts pA104R-DNA binding and inhibits African swine fever virus replication
文献类型： 外文期刊
作者： Li, Quan-jie 1 ; Shao, Hui-han 1 ; Zheng, Lin-lin 2 ; Liu, Qian 1 ; Huo, Chen-chao 1 ; Yi, Dong-rong 1 ; Feng, Tao 2 ; Cen, Shan 1 ;
作者机构： 1.Chinese Acad Med Sci & Peking Union Med Coll, Inst Med Biotechnol, Beijing 100050, Peoples R China
2.Lanzhou Univ, Lanzhou Vet Res Inst, Chinese Acad Agr Sci, Coll Vet Med,State Key Lab Anim Dis Control & Prev, Lanzhou 730046, Peoples R China
3.Chinese Acad Med Sci, Peking Union Med Coll, CAMS Key Lab Antiviral Drug Res, Beijing 100730, Peoples R China
关键词： pA104R; thonningianin A; DNA-binding protein; ASFV; EMSA; structure-based virtual screening
期刊名称：EMERGING MICROBES & INFECTIONS （ 影响因子：7.5； 五年影响因子：7.2 ）
ISSN：
年卷期： 2025 年 14 卷 1 期
页码：
收录情况： SCI
摘要： African swine fever is a highly lethal disease caused by the African swine fever virus (ASFV), posing a significant threat to the global pig industry, wherease no approved treatments are currently available. The ASFV DNA-binding protein, pA104R, plays a critical role in viral genome packaging and replication, making it a key target for drug discovery. Through structure-based virtual screening, we identified a polyphenolic compound, thonningianin A, which disrupts the pA104R-DNA binding and significantly inhibits ASFV replication. Mechanistic study revealed that thonningianin A binds to the DNA-binding region of pA104R, forming strong hydrogen bonds with H100 and occupying the vital DNA-binding residues K92, R94, and K97. In addition, we resolved the high-resolution (1.8 & Aring;) structure of pA104R (PDB ID 9JS5), providing valuable insights for future drug screening. Together, these results demonstrate that thonningianin A holds great potential for the development of anti-ASFV drug, as a herb extract with favourable pharmacokinetic properties and safety.
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