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Acequinocyl resistance in Tetranychus urticae Koch (Acari: Tetranychidae): inheritance, synergists, cross-resistance and biochemical resistance mechanisms

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dc.creator SARITAŞ, Elif
dc.creator Salman, SİBEL
dc.date 2013-12-31T22:00:00Z
dc.date.accessioned 2020-10-06T09:24:17Z
dc.date.available 2020-10-06T09:24:17Z
dc.identifier 0a7af7dd-119a-42e0-b8f0-ca49124c8cff
dc.identifier 10.1080/01647954.2014.944932
dc.identifier https://avesis.sdu.edu.tr/publication/details/0a7af7dd-119a-42e0-b8f0-ca49124c8cff/oai
dc.identifier.uri http://acikerisim.sdu.edu.tr/xmlui/handle/123456789/52871
dc.description Acequinocyl is the only commercialized acaricide of the naphthoquinone analogue group. To develop strategies to minimize resistance, a laboratory-selected acequinocyl-resistant strain of the two-spotted spider mite Tetranychus urticae was used to determine the inheritance, toxicological, biochemical and cross-resistance data. The LC50 and LC60 values of acequinocyl were determined on T. urticae using a leaf-disc method and spraying tower. A laboratory selection population designated ACE6 had a122.0-fold resistance to acequinocyl following six selection cycles. A selected strain showing 112.0-fold resistance was named ACE6 population. This population developed low resistance to etoxazole and spirodiclofen and moderate cross-resistance to hexythiazox, milbemectin and bifenazate. Monooxygenase enzyme inhibitor piperonyl butoxide, the esterase enzyme inhibitor S-benzyl O, O-diisopropyl phosphorothioate and the glutathione S-transferase (GST) enzyme inhibitor diethyl maleate synergized resistance values were 1.0-, 2.5- and. < 1-fold, respectively. Crossing experiments revealed that acequinocyl resistance in the ACE6 population was intermediately dominant and monogenic. In addition, the detoxifying enzyme activities were increased 3.03-fold for esterase,. < 1-fold for GST and 1.00-fold for cytochrome P450 monooxygenase in the ACE6 population. The results suggest that esterase enzyme may play a role in acequinocyl resistance, while the GST and P450 enzymes do not appear to have any significant involvement.
dc.language eng
dc.rights info:eu-repo/semantics/closedAccess
dc.title Acequinocyl resistance in Tetranychus urticae Koch (Acari: Tetranychidae): inheritance, synergists, cross-resistance and biochemical resistance mechanisms
dc.type info:eu-repo/semantics/article


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