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

<h4>Background</h4>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 upregulati...

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Autores principales:	Nongkran Lumjuan, Jureeporn Wicheer, Posri Leelapat, Wej Choochote, Pradya Somboon
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/303aace116194cbc829521d652a75dbf
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spelling	oai:doaj.org-article:303aace116194cbc829521d652a75dbf2021-11-25T06:07:51ZIdentification and characterisation of Aedes aegypti aldehyde dehydrogenases involved in pyrethroid metabolism.1932-620310.1371/journal.pone.0102746https://doaj.org/article/303aace116194cbc829521d652a75dbf2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25047125/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>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.<h4>Methodology/principal findings</h4>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).<h4>Conclusions/significance</h4>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.Nongkran LumjuanJureeporn WicheerPosri LeelapatWej ChoochotePradya SomboonPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 7, p e102746 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nongkran Lumjuan Jureeporn Wicheer Posri Leelapat Wej Choochote Pradya Somboon Identification and characterisation of Aedes aegypti aldehyde dehydrogenases involved in pyrethroid metabolism.
description	<h4>Background</h4>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.<h4>Methodology/principal findings</h4>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).<h4>Conclusions/significance</h4>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.
format	article
author	Nongkran Lumjuan Jureeporn Wicheer Posri Leelapat Wej Choochote Pradya Somboon
author_facet	Nongkran Lumjuan Jureeporn Wicheer Posri Leelapat Wej Choochote Pradya Somboon
author_sort	Nongkran Lumjuan
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 (PLoS)
publishDate	2014
url	https://doaj.org/article/303aace116194cbc829521d652a75dbf
work_keys_str_mv	AT nongkranlumjuan identificationandcharacterisationofaedesaegyptialdehydedehydrogenasesinvolvedinpyrethroidmetabolism AT jureepornwicheer identificationandcharacterisationofaedesaegyptialdehydedehydrogenasesinvolvedinpyrethroidmetabolism AT posrileelapat identificationandcharacterisationofaedesaegyptialdehydedehydrogenasesinvolvedinpyrethroidmetabolism AT wejchoochote identificationandcharacterisationofaedesaegyptialdehydedehydrogenasesinvolvedinpyrethroidmetabolism AT pradyasomboon identificationandcharacterisationofaedesaegyptialdehydedehydrogenasesinvolvedinpyrethroidmetabolism
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Identification and characterisation of Aedes aegypti aldehyde dehydrogenases involved in pyrethroid metabolism.

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