文献类型：期刊文献

英文题名：Cysteine protease domain of potato virus Y: The potential target for urea derivatives

作者：Bai, Qian Jiang, Junmei Luo, Dan Huang, Yajiao Huang, Min Zhao, Guili Wang, Zhenchao Li, Xiangyang

第一作者：Bai, Qian

通信作者：Li, XY[1];Wang, ZC[2]

机构：[1]Guizhou Univ, Minist Educ, Key Lab Green Pesticide & Agr Bioengn, State Key Lab Breeding Base Green Pesticide & Agr, Guiyang 550025, Peoples R China;[2]Guizhou Inst Technol, Coll Chem Engn, Guiyang, Peoples R China;[3]Guizhou Univ, Coll Pharm, Guiyang, Peoples R China

第一机构：Guizhou Univ, Minist Educ, Key Lab Green Pesticide & Agr Bioengn, State Key Lab Breeding Base Green Pesticide & Agr, Guiyang 550025, Peoples R China

通信机构：corresponding author), Guizhou Univ, Minist Educ, Key Lab Green Pesticide & Agr Bioengn, State Key Lab Breeding Base Green Pesticide & Agr, Guiyang 550025, Peoples R China;corresponding author), Guizhou Univ, Coll Pharm, Guiyang, Peoples R China.

年份：2023

卷号：189

外文期刊名：PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY

收录：;Scopus(收录号：2-s2.0-85144481425);WOS:【SCI-EXPANDED(收录号:WOS:000897706400008)】；

基金：This work was supported in part by the National Key Research and Development Program of China (Grant No. 2021YFD1700101), the National Natural Science Foundation of China (Grant Nos. 31960546 and 32172461), the Talents of Guizhou Science and Technology Cooperation Platform [Grant No. (2021) 5623], the Guizhou Science and Technology Cooperation Foundation [Grant No. ZK (2021) 140], and the Unique Feature Project of Guizhou Provincial Education Department [Grant No. KY (2021) 056].

语种：英文

外文关键词：Potato virus Y; Cysteine protease domain; Urea derivatives; Binding affinity; Molecular docking

摘要：The cysteine protease structural domain (CPD) encoded by the potato virus Y (PVY) accessory component protein helper component-proteinase (HC-Pro) is an auxiliary component of aphid virus transmission and plays an important role in virus infection and replication. Urea derivatives have potential antiviral activities. In this study, the PVY HC-Pro C-terminal truncated recombinant protein (residues 307-465) was expressed and purified. The interactions of PVY CPD with urea derivatives HD1-36 were investigated. Microscale thermophoresis experiments showed that HD6, -19, -21 and - 25 had the strongest binding forces to proteins, with Kd values of 2.16, 1.40, 1.97 and 1.12 mu M, respectively. An experiment verified the microscale thermophoresis results, and the results were as expected, with Kd values of 6.10, 4.78, 5.32, and 4.52 mu M for HD6, -19, -21, and - 25, respectively. Molecular docking studies indicated that the interaction sites between PVY CPD and HD6, -19, -21, and - 25, independently, were aspartic acid 121, asparagine 48, and tyrosine 38, which played important roles in their binding. In vivo experiments verified that HD25 inhibited PVY more than the control agents ningnanmycin and urea. These data have important implications for the design and synthesis of novel urea derivatives.