Evidence map›Paper›PMID 41187806›Full record

ArticleJournal of advanced research2026

UDP-glycosyltransferase confers anthranilic diamide resistance in Bemisia tabaci.

Huiwen Tan, Xichao Hu, Jinghao Hu, Wei Xu, Qianwen Wang, Xiaolan Liu, Lei Guo

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Article in Journal of advanced research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

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3citing papers in PubMed
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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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3 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

7 authors.

Huiwen TanCollege of Plant Health and Medicine, Qingdao Agricultural University, Qingdao 266109, PR China.
Xichao HuCollege of Plant Health and Medicine, Qingdao Agricultural University, Qingdao 266109, PR China.
Jinghao HuCollege of Plant Health and Medicine, Qingdao Agricultural University, Qingdao 266109, PR China.
Wei XuFood Futures Institute, Murdoch University, Murdoch WA 6150, Australia.
Qianwen WangInstrumental Analysis Center, Qingdao Agricultural University, Qingdao 266109, PR China.
Xiaolan LiuCollege of Plant Health and Medicine, Qingdao Agricultural University, Qingdao 266109, PR China.
Lei GuoCollege of Plant Health and Medicine, Qingdao Agricultural University, Qingdao 266109, PR China. Electronic address: guoleicau@163.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

introductionUDP-glycosyltransferases (UGTs) are key Phase II detoxification enzymes in insects, playing a crucial role in resistance to a variety of insecticides, including diamides. Cyantraniliprole (CYA) is a systemic diamide insecticide with high toxicity against Bemisia tabaci, a major global agricultural pest transmitting over 200 plant viruses. While B. tabaci has developed medium-level resistance to CYA, the role of UGTs in this resistance remains poorly understood.

objectivesThis study aimed to investigate the role of UGTs in B. tabaci resistance to CYA and further elucidate the underlying mechanisms.

methodsSynergism bioassays and enzymatic activity analyses were conducted to assess the contribution of UGTs to CYA resistance. RNA sequencing and RT-qPCR were employed to identify differentially expressed BtUGT genes associated with resistance. The functions of UGTs and the UDP-glucose (UDPG) biosynthesis pathway in CYA resistance were confirmed through RNA interference and transgenic Drosophila melanogaster lines. The metabolites of CYA in the resistant strain were identified using LC-MS/MS. A cross-resistance study to chlorantraniliprole was performed to further confirm the role of UGTs in the diamide resistance of B. tabaci.

resultsHigher expression of UGTs represents a key metabolic resistance mechanism of B. tabaci to CYA. Specifically, overexpression of BtUGT352B2 and BtUGT352F1, along with the UDP-glucose biosynthesis pathway, contributed significantly to resistance. Four glycoside metabolites of CYA were putatively identified in resistant whiteflies. Significant cross-resistance to chlorantraniliprole confirmed that the UGT-mediated metabolism plays a crucial role in anthranilic diamide resistance in B. tabaci.

conclusionThis research advances our understanding of UGT-mediated insecticide resistance mechanisms and provides valuable insights for the development of more sustainable pest management strategies to combat pesticide resistance.

Indexed as

DiamideGlycosyltransferasesHemipteraInsecticide ResistanceInsecticidesortho-AminobenzoatesAnimalsDrosophila melanogasterInsect ProteinsPyrazoleschlorantranilipolecyantraniliproleDiamideGlycosyltransferasesInsecticidesInsect Proteinsortho-AminobenzoatesPyrazolesDiamide insecticideMetabolic resistancePhase Ⅱ detoxificationUDP-glucose biosynthesisUpregulation expressionWhitefly

Identifiers

PMID41187806
PMCPMC13453716

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.