Identification and characterisation of Aedes aegypti aldehyde dehydrogenases involved in pyrethroid metabolism

Background: Pyrethroid insecticides, especially permethrin and deltamethrin, have been used extensively worldwide for mosquito control. However, insecticide resistance can spread through a population very rapidly under strong selection pressure from insecticide use. The upregulation of aldehyde dehy...

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Main Authors: Lumjuan N., Wicheer J., Leelapat P., Choochote W., Somboon P.
Format: Article
Language:English
Published: Public Library of Science 2014
Online Access:http://www.scopus.com/inward/record.url?eid=2-s2.0-84904562081&partnerID=40&md5=438cdf3367fa4948068dfbaebbc80b37
http://cmuir.cmu.ac.th/handle/6653943832/1767
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Institution: Chiang Mai University
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spelling th-cmuir.6653943832-17672014-08-30T02:00:05Z Identification and characterisation of Aedes aegypti aldehyde dehydrogenases involved in pyrethroid metabolism Lumjuan N. Wicheer J. Leelapat P. Choochote W. Somboon P. Background: Pyrethroid insecticides, especially permethrin and deltamethrin, have been used extensively worldwide for mosquito control. However, insecticide resistance can spread through a population very rapidly under strong selection pressure from insecticide use. The upregulation of aldehyde dehydrogenase (ALDH) has been reported upon pyrethroid treatment. In Aedes aegypti, the increase in ALDH activity against the hydrolytic product of pyrethroid has been observed in DDT/permethrin-resistant strains. The objective of this study was to identify the role of individual ALDHs involved in pyrethroid metabolism. Methodology/Principal Findings: Three ALDHs were identified; two of these, ALDH9948 and ALDH14080, were upregulated in terms of both mRNA and protein levels in a DDT/pyrethroid-resistant strain of Ae. aegypti. Recombinant ALDH9948 and ALDH14080 exhibited oxidase activities to catalyse the oxidation of a permethrin intermediate, phenoxybenzyl aldehyde (PBald), to phenoxybenzoic acid (PBacid). Conclusions/Significance: ALDHs have been identified in association with permethrin resistance in Ae. aegypti. Characterisation of recombinant ALDHs confirmed the role of this protein in pyrethroid metabolism. Understanding the biochemical and molecular mechanisms of pyrethroid resistance provides information for improving vector control strategies. © 2014 Lumjuan et al. 2014-08-30T02:00:05Z 2014-08-30T02:00:05Z 2014 Article 19326203 10.1371/journal.pone.0102746 POLNC http://www.scopus.com/inward/record.url?eid=2-s2.0-84904562081&partnerID=40&md5=438cdf3367fa4948068dfbaebbc80b37 http://cmuir.cmu.ac.th/handle/6653943832/1767 English Public Library of Science
institution Chiang Mai University
building Chiang Mai University Library
country Thailand
collection CMU Intellectual Repository
language English
description Background: Pyrethroid insecticides, especially permethrin and deltamethrin, have been used extensively worldwide for mosquito control. However, insecticide resistance can spread through a population very rapidly under strong selection pressure from insecticide use. The upregulation of aldehyde dehydrogenase (ALDH) has been reported upon pyrethroid treatment. In Aedes aegypti, the increase in ALDH activity against the hydrolytic product of pyrethroid has been observed in DDT/permethrin-resistant strains. The objective of this study was to identify the role of individual ALDHs involved in pyrethroid metabolism. Methodology/Principal Findings: Three ALDHs were identified; two of these, ALDH9948 and ALDH14080, were upregulated in terms of both mRNA and protein levels in a DDT/pyrethroid-resistant strain of Ae. aegypti. Recombinant ALDH9948 and ALDH14080 exhibited oxidase activities to catalyse the oxidation of a permethrin intermediate, phenoxybenzyl aldehyde (PBald), to phenoxybenzoic acid (PBacid). Conclusions/Significance: ALDHs have been identified in association with permethrin resistance in Ae. aegypti. Characterisation of recombinant ALDHs confirmed the role of this protein in pyrethroid metabolism. Understanding the biochemical and molecular mechanisms of pyrethroid resistance provides information for improving vector control strategies. © 2014 Lumjuan et al.
format Article
author Lumjuan N.
Wicheer J.
Leelapat P.
Choochote W.
Somboon P.
spellingShingle Lumjuan N.
Wicheer J.
Leelapat P.
Choochote W.
Somboon P.
Identification and characterisation of Aedes aegypti aldehyde dehydrogenases involved in pyrethroid metabolism
author_facet Lumjuan N.
Wicheer J.
Leelapat P.
Choochote W.
Somboon P.
author_sort Lumjuan N.
title Identification and characterisation of Aedes aegypti aldehyde dehydrogenases involved in pyrethroid metabolism
title_short Identification and characterisation of Aedes aegypti aldehyde dehydrogenases involved in pyrethroid metabolism
title_full Identification and characterisation of Aedes aegypti aldehyde dehydrogenases involved in pyrethroid metabolism
title_fullStr Identification and characterisation of Aedes aegypti aldehyde dehydrogenases involved in pyrethroid metabolism
title_full_unstemmed Identification and characterisation of Aedes aegypti aldehyde dehydrogenases involved in pyrethroid metabolism
title_sort identification and characterisation of aedes aegypti aldehyde dehydrogenases involved in pyrethroid metabolism
publisher Public Library of Science
publishDate 2014
url http://www.scopus.com/inward/record.url?eid=2-s2.0-84904562081&partnerID=40&md5=438cdf3367fa4948068dfbaebbc80b37
http://cmuir.cmu.ac.th/handle/6653943832/1767
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