A UDP-glycosyltransferase gene PcUGT202A9 was associated with abamectin resistance in Panonychus citri (McGregor)

Binbin Shao; Shijiang Yu; Shuqi Wang; Sichen Li; Lili Ding; Mingyue Li; Luyan Cheng; Qi Pan; Lin Cong; Chun Ran

doi:10.1016/j.ijbiomac.2024.132228

A UDP-glycosyltransferase gene PcUGT202A9 was associated with abamectin resistance in Panonychus citri (McGregor)

Int J Biol Macromol. 2024 May 10;270(Pt 2):132228. doi: 10.1016/j.ijbiomac.2024.132228. Online ahead of print.

Authors

Binbin Shao¹, Shijiang Yu¹, Shuqi Wang¹, Sichen Li¹, Lili Ding¹, Mingyue Li¹, Luyan Cheng², Qi Pan¹, Lin Cong³, Chun Ran⁴

Affiliations

¹ Citrus Research Institute, Southwest University, National Engineering Research Center for Citrus, Chongqing 400712, China.
² Chongqing Institute for Food and Drug Control, Key Laboratory of Condiment Supervision Technology for State Market Regulation, Chongqing 401121, China.
³ Citrus Research Institute, Southwest University, National Engineering Research Center for Citrus, Chongqing 400712, China. Electronic address: conglin@cric.cn.
⁴ Citrus Research Institute, Southwest University, National Engineering Research Center for Citrus, Chongqing 400712, China. Electronic address: ranchun@cric.cn.

PMID: 38734355
DOI: 10.1016/j.ijbiomac.2024.132228

Abstract

Panonychus citri (McGregor) strains have developed a high level of resistance to abamectin, but the underlying molecular mechanism is unknown. Uridine diphosphate (UDP)-glycosyltransferases (UGTs) are critical for the removal of a variety of exogenous and endogenous substances. In this study, an enzyme activity assay revealed that UGTs potentially contribute to P. citri abamectin resistance. Spatiotemporal expression profiles showed that only PcUGT202A9 was significantly overexpressed in the abamectin-resistant strain (AbR) at all developmental stages. Moreover, UGT activity decreased significantly, whereas abamectin susceptibility increased significantly, in AbR after PcUGT202A9 was silenced. Three-dimensional modeling and molecular docking analyses revealed that PcUGT202A9 can bind stably to abamectin. Recombinant PcUGT202A9 activity was detected when α-naphthol was used, but the enzymatic activity was inhibited by abamectin (50 % inhibitory concentration: 803.3 ± 14.20 μmol/L). High-performance liquid chromatography and mass spectrometry analyses indicated that recombinant PcUGT202A9 can effectively degrade abamectin and catalyze the conjugation of UDP-glucose to abamectin. These results imply PcUGT202A9 contributes to P. citri abamectin resistance.

Keywords: Abamectin resistance; Panonychus citri; UDP-glycosyltransferases.