Monitoring detoxification enzyme levels and resistance of Tetranychus urticae against some METI-group chemicals in Türkiye cotton fields

• Published in: Experimental & applied acarology 2024-06, Vol.93 (1), p.211-227
• Main Authors: Alpkent, Yasin Nazım, Ferizli, Ahmet Güray
• Format: Article
• Language: English
• Subjects: Acaricides; Animal Ecology; Animal Genetics and Genomics; Animal Systematics/Taxonomy/Biogeography; Bioassays; Biomedical and Life Sciences; Carboxylesterase; Cotton; Detoxification; Entomology; Enzymes; Glutathione; Glutathione transferase; Life Sciences; Mutation; Pharmacokinetics; Point mutation; Population (statistical); Population studies; Protein folding; Proteins; Tetranychus urticae
• ISSN: 0168-8162; 1572-9702; 1572-9702
• DOI: 10.1007/s10493-024-00923-6

Acaricides used against Tetranychus urticae Koch, 1836 (Acari: Tetranychidae) in cotton fields cause control failure over time. To determine the resistance status of T. urticae populations to tebufenpyrad and bifenazate, different populations collected from Aydın (AYD), Adana (ADA), Şanlıurfa (SAN), and Diyarbakır (DIY) provinces of Türkiye, between 2019 and 2020, were subjected to diagnostic dose bioassays. Firstly, the spider mites were eliminated with a discriminating dose. Afterwards, LC 50 and LC 90 of the remaining populations were determined and the ten highest resistant populations were selected. The highest phenotypic resistance to bifenazate was observed in AYD4 and DIY2 (LC 50 57.14 mg L − 1 with 85.01-fold and LC 50 30.15 mg L − 1 with 44.86-fold, respectively), while the lowest phenotypic resistance was found in SAN6 (LC 50 1.5 mg L − 1 ; 2.28-fold). Considering the phenotypic resistance to tebufenpyrad, the highest resistance was found in AYD4 population (LC 50 96.81 mg L − 1 ; 12.92-fold), while the lowest - in DIY28 population (LC 50 21.23 mg L − 1 ; 2.83-fold). In pharmacokinetic studies, the ADA16 population was compared with the sensitive German Susceptible Strain population and it was determined that carboxylesterase activity was statistically higher (1.46 ± 0.04 nmol/min/mg protein enzyme activation 2.70-fold). The highest activation of glutathione S -transferase was detected in ADA16 (1.49 ± 0.01 nmol/min/mg protein; 2.32-fold). No mutations were found in PSST (METI 1), the point mutation site for tebufenpyrad, and Cytb (METI 3), the point mutation site for bifenazate. In terms of phenotypic resistance, bifenazate was found to be moderately resistant in two populations (85.01 and 44.86-fold), while tebufenpyrad was moderately resistant in one population (12.92-fold). This study showed that both acaricides are still effective against T. urticae populations.