کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5510592 | 1539267 | 2017 | 17 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Multiple resistance to pirimiphos-methyl and bifenthrin in Tribolium castaneum involves the activity of lipases, esterases, and laccase2
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کلمات کلیدی
GSTXREJHEPYRORGPyrethroidEcdysone response elementMAFLACSSPECPBCyPNC2LIPsOrganophosphate - ارگانوفسفاتArtificial selection - انتخاب مصنوعیEcRE - اکرانColorado potato beetle - سوسک سیب زمینی کلرادوRed flour beetle - سوسک قرمز آردCytochrome P450 - سیتوکروم پی۴۵۰Interaction network - شبکه تعاملlethal concentration - غلظت کشندهLaccases - لاک هاLipases - لیپازهاSEM - مدل معادلات ساختاری / میکروسکوپ الکترونی روبشیPesticide resistance - مقاومت به آفت کش هاEnzymatic inhibition - مهار آنزیمیscanning electron microscope - میکروسکوپ الکترونی اسکنJuvenile hormone esterase - هورمون استرس نوجوانانJuvenile hormone - هورمون جوانیribosomal protein - پروتئین ریبوزومیglutathione-S-transferase - گلوتاتیون S-ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Several recent studies have elucidated the molecular mechanisms that confer insecticide resistance on insect pests. However, little is known about multiple resistance in red flour beetle (Tribolium castaneum) at molecular level. The multiple resistance is characterized as resistance to different classes of insecticides that have different target sites, and is mediated by several enzymatic systems. In this study, we investigated the biochemical and molecular mechanisms involved in multiple resistance of T. castaneum to bifenthrin (pyrethroid [Pyr]) and pirimiphos-methyl (organophosphate [Org]). We used artificial selection, biochemical and in silico approaches including structural computational biology. After five generations of artificial selection in the presence of bifenthrin (F5Pyr) or pirimiphos-methyl (F5Org), we found high levels of multiple resistance. The hierarchical enzymatic cluster revealed a pool of esterases (E), lipases (LIPs) and laccase2 (LAC2) potentially contributing to the resistance in different ways throughout development, after one or more generations in the presence of insecticides. The enzyme-insecticide interaction network indicated that E2, E3, LIP3, and LAC2 are enzymes potentially required for multiple resistance phenotype. Kinetic analysis of esterases from F5Pyr and F5Org showed that pirimiphos-methyl and specially bifenthrin promote enzyme inhibition, indicating that esterases mediate resistance by sequestering bifenthrin and pirimiphos-methyl. Our computational data were in accordance with kinetic results, indicating that bifenthrin has higher affinity at the active site of esterase than pirimiphos-methyl. We also report the capability of these insecticides to modify the development in T. castaneum. Our study provide insights into the biochemical mechanisms employed by T. castaneum to acquire multiple resistance.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology - Volume 195, May 2017, Pages 27-43
Journal: Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology - Volume 195, May 2017, Pages 27-43
نویسندگان
Alison Henrique Ferreira Julio, Adriana Aparecida Sinópolis Gigliolli, Kátia Aparecida Kern Cardoso, Sandro Daniel Drosdoski, Rodrigo Amaral Kulza, Flávio Augusto Vicente Seixas, Maria Claudia Colla Ruvolo-Takasusuki, Cristina Giatti Marques de Souza,