Date of Award

Spring 2021

Document Type

Open Access Dissertation

Department

Chemistry and Biochemistry

First Advisor

Maksymilian Chruszcz

Abstract

Invasive pest species are a major cause of crop loss around the world and adversely affect the agricultural industry. We are focusing on Tetranychus urticae (two-spotted spider mite; TSSM), which is a polyphagous pest that targets more than 1100 plant species. The TSSM alone causes a loss of roughly $1.6 billion per year globally due to acaricide resistance. It is developing resistance to most acaricides due to rapid growth and reproduction. Therefore, new acaricides are needed to combat TSSM resistance and infestation [1]. To address this problem, four enzymes of TSSM, intradiol ring cleavage dioxygenases, a glutathione S-transferase, a β cyanoalanine synthase, and uridine diphosphate glycosyltransferases, are characterized. These enzymes contribute to the detoxification system of TSSM and are potential protein targets to develop new acaricides. Intradiol ring-cleavage dioxygenases are involved in the breakdown and metabolism of toxic aromatic compounds [2]. Glutathione S-transferases conjugate reduced glutathione to xenobiotics for detoxification and have been associated with insecticide resistance [3]. The β cyanoalanine synthase is known for detoxification of cyanide and silencing this gene in TSSM reduces the survival of the mites on cyanogenic plants [4]. Uridine diphosphate glycosyltransferases (UGTs) catalyze the covalent addition of sugar moieties from UDP sugar donors to xenobiotics to facilitate their elimination from cells [5]. UGTs are known for the detoxification of acaricides such as abamectin. Here we have structurally and functionally characterized these proteins, particularly focusing on revealing the crystal structure of enzymes with the intention of exposing unique properties that will allow for the design of new acaricides and control of TSSM.

Rights

© 2021, Leily Daneshian

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