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Identifier 000410173
Title Λειτουργική έκφραση και χαρακτηρισμός ενζύμων αποτοξικοποίησης (Cytochrome P450) εντόμων- εχθρών καλλιεργειών και φορέων ασθενειών στη ζύμη
Alternative Title Functional expression and characterization of Cytochrome P450 detoxification enzymes from insect pests and vectors of disease in yeast
Author Αναγνώστου, Δημήτριος Α.
Thesis advisor Βόντας, Ιωάννης
Abstract Tetranychus urticae is a major agricultural pest. Field populations of T. urticae are controlled basically with the use of insecticides and acaricides but due to their ability to develop resistance, their control becomes very difficult. So there is a great need to elucidate the molecular mechanisms underlying this process. A multiresistant population was isolated from a greenhouse in Marathon which showed high resistance to almost all known categories of insecticides and acaricides. From DNA microarray experiments it was found a series of detoxification enzymes (P450 monooxygenases, estereses and GSTs) that are overexpressed in this population in comparison with a susceptible population. In this study, attempt was made to functionally express and characterize three P450 enzymes (CYP392D2, CYP392D8 and CYP392D10) in the heterologous expression system Saccharomyces cerevisiae. CYP392D2 expressed in an active form since this enzyme metabolized in vitro the model substrate 7-ethoxycoumarin. However, none of the insecticides and acaricides that were tried in metabolic experiments, is not a substrate of this enzyme. CYP4G16PA and PD1 (2 possible isoforms) and CYP4G17 of Anopheles gambiae are P450 proteins with possible role in the hydrocarbon biosynthesis pathway of epicuticular hydrocarbons and it was found that these proteins are overexpressed in resistant mosquito populations. CYP4G16PA has decarbonylase catalytic activity and catalyses in vitro the conversion of aldehydes in hydrocarbons. In immunofluorescence experiments CYP4G16PA localized in plasma membrane of oenocytes of adult mosquitoes while CYP4G17 localized at the same cells in the endoplasmic reticulum (ER). In the present study, an effort has been made to express and immunolocalize these proteins in yeast cells. CYP4G16 PD1 localized in the plasma membrane of yeast cells. The antibody that was used against CYP4G17, except from CYP4G17 also recognizes two endogenous protein of yeast, so this antibody couldn’t be used in immunofluorescent experiments.
Language Greek
Subject Anopheles gambiae
Tetranychus urticae
Ένζυμα αποτοξικοποιήσης
Κυτοχρωμικές P450s
Issue date 2017-07-21
Collection   Faculty/Department--Faculty of Sciences and Engineering--Department of Biology--Post-graduate theses
  Type of Work--Graduate theses
Permanent Link https://elocus.lib.uoc.gr//dlib/8/4/4/metadata-dlib-1499335258-389987-3817.tkl Bookmark and Share
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