A high number of mutations in insect acetylcholinesterase may provide insecticide resistance

Many insect pest species have developed insecticide resistance through modifications of acetylcholinesterase. Seven mutations, issued from one nucleotide change, have been associated with resistance in natural populations of Drosophila and housefly (A. Mutero, M. Pralavorio, J. M, Bride, and D. Fournier, Resistance-associated point mutations in insecticide insensitive acetylcholinesterase, Proc. Nail. Acad Sci. USA 91, 5922 (1994); A. L. Devonshire, F. J. Byrne, G. D. Moores, and M. S. Williamson, Biochemical and molecular characterisation of insecticide- insensitive acetylcholinesterases in resistant insects, in "Structure and function of cholinesterases and related proteins- (B. P. Doctor, P. Taylor, D. M. Quinn, R. L. Rotundo, and M, K. Gentry, Eds.), pp. 491-496, Plenum Press, New York, 1998). In order to study the number of mutations which can lead to resistance, we first analyzed the effects of a set of amino acid replacements in the Drosophila acetylcholinesterase on inhibition by several carbamate and organophosphate insecticides. It appeared that most of the mutations led to a reduced sensitivity to insecticides. Second, we investigated the effect of mutations on substrate hydrolysis. We found that most of the variants retained sufficient levels of substrate hydrolysis. These data suggest that more mutations in acetylcholinesterase may be involved in organophosphate and carbamate resistance in addition to the previously known seven mutations.

Saved in:
Bibliographic Details
Main Authors: Villatte, F., Ziliani, Philippe, Marcel, Véronique, Menozzi, Philippe, Fournier, Didier
Format: article biblioteca
Language:eng
Subjects:H10 - Ravageurs des plantes, Drosophila, insecticide, résistance aux pesticides, mutation provoquée, acétylcholinestérase, acide aminé, http://aims.fao.org/aos/agrovoc/c_2390, http://aims.fao.org/aos/agrovoc/c_3887, http://aims.fao.org/aos/agrovoc/c_25427, http://aims.fao.org/aos/agrovoc/c_3842, http://aims.fao.org/aos/agrovoc/c_85, http://aims.fao.org/aos/agrovoc/c_342,
Online Access:http://agritrop.cirad.fr/487534/
http://agritrop.cirad.fr/487534/1/487534.pdf
Tags: Add Tag
No Tags, Be the first to tag this record!
id dig-cirad-fr-487534
record_format koha
spelling dig-cirad-fr-4875342024-01-28T10:06:22Z http://agritrop.cirad.fr/487534/ http://agritrop.cirad.fr/487534/ A high number of mutations in insect acetylcholinesterase may provide insecticide resistance. Villatte F., Ziliani Philippe, Marcel Véronique, Menozzi Philippe, Fournier Didier. 2000. Pesticide Biochemistry and Physiology, 67 (2) : 95-102.https://doi.org/10.1006/pest.2000.2478 <https://doi.org/10.1006/pest.2000.2478> A high number of mutations in insect acetylcholinesterase may provide insecticide resistance Villatte, F. Ziliani, Philippe Marcel, Véronique Menozzi, Philippe Fournier, Didier eng 2000 Pesticide Biochemistry and Physiology H10 - Ravageurs des plantes Drosophila insecticide résistance aux pesticides mutation provoquée acétylcholinestérase acide aminé http://aims.fao.org/aos/agrovoc/c_2390 http://aims.fao.org/aos/agrovoc/c_3887 http://aims.fao.org/aos/agrovoc/c_25427 http://aims.fao.org/aos/agrovoc/c_3842 http://aims.fao.org/aos/agrovoc/c_85 http://aims.fao.org/aos/agrovoc/c_342 Many insect pest species have developed insecticide resistance through modifications of acetylcholinesterase. Seven mutations, issued from one nucleotide change, have been associated with resistance in natural populations of Drosophila and housefly (A. Mutero, M. Pralavorio, J. M, Bride, and D. Fournier, Resistance-associated point mutations in insecticide insensitive acetylcholinesterase, Proc. Nail. Acad Sci. USA 91, 5922 (1994); A. L. Devonshire, F. J. Byrne, G. D. Moores, and M. S. Williamson, Biochemical and molecular characterisation of insecticide- insensitive acetylcholinesterases in resistant insects, in "Structure and function of cholinesterases and related proteins- (B. P. Doctor, P. Taylor, D. M. Quinn, R. L. Rotundo, and M, K. Gentry, Eds.), pp. 491-496, Plenum Press, New York, 1998). In order to study the number of mutations which can lead to resistance, we first analyzed the effects of a set of amino acid replacements in the Drosophila acetylcholinesterase on inhibition by several carbamate and organophosphate insecticides. It appeared that most of the mutations led to a reduced sensitivity to insecticides. Second, we investigated the effect of mutations on substrate hydrolysis. We found that most of the variants retained sufficient levels of substrate hydrolysis. These data suggest that more mutations in acetylcholinesterase may be involved in organophosphate and carbamate resistance in addition to the previously known seven mutations. article info:eu-repo/semantics/article Journal Article info:eu-repo/semantics/publishedVersion http://agritrop.cirad.fr/487534/1/487534.pdf text Cirad license info:eu-repo/semantics/restrictedAccess https://agritrop.cirad.fr/mention_legale.html https://doi.org/10.1006/pest.2000.2478 10.1006/pest.2000.2478 http://catalogue-bibliotheques.cirad.fr/cgi-bin/koha/opac-detail.pl?biblionumber=170679 info:eu-repo/semantics/altIdentifier/doi/10.1006/pest.2000.2478 info:eu-repo/semantics/altIdentifier/purl/https://doi.org/10.1006/pest.2000.2478
institution CIRAD FR
collection DSpace
country Francia
countrycode FR
component Bibliográfico
access En linea
databasecode dig-cirad-fr
tag biblioteca
region Europa del Oeste
libraryname Biblioteca del CIRAD Francia
language eng
topic H10 - Ravageurs des plantes
Drosophila
insecticide
résistance aux pesticides
mutation provoquée
acétylcholinestérase
acide aminé
http://aims.fao.org/aos/agrovoc/c_2390
http://aims.fao.org/aos/agrovoc/c_3887
http://aims.fao.org/aos/agrovoc/c_25427
http://aims.fao.org/aos/agrovoc/c_3842
http://aims.fao.org/aos/agrovoc/c_85
http://aims.fao.org/aos/agrovoc/c_342
H10 - Ravageurs des plantes
Drosophila
insecticide
résistance aux pesticides
mutation provoquée
acétylcholinestérase
acide aminé
http://aims.fao.org/aos/agrovoc/c_2390
http://aims.fao.org/aos/agrovoc/c_3887
http://aims.fao.org/aos/agrovoc/c_25427
http://aims.fao.org/aos/agrovoc/c_3842
http://aims.fao.org/aos/agrovoc/c_85
http://aims.fao.org/aos/agrovoc/c_342
spellingShingle H10 - Ravageurs des plantes
Drosophila
insecticide
résistance aux pesticides
mutation provoquée
acétylcholinestérase
acide aminé
http://aims.fao.org/aos/agrovoc/c_2390
http://aims.fao.org/aos/agrovoc/c_3887
http://aims.fao.org/aos/agrovoc/c_25427
http://aims.fao.org/aos/agrovoc/c_3842
http://aims.fao.org/aos/agrovoc/c_85
http://aims.fao.org/aos/agrovoc/c_342
H10 - Ravageurs des plantes
Drosophila
insecticide
résistance aux pesticides
mutation provoquée
acétylcholinestérase
acide aminé
http://aims.fao.org/aos/agrovoc/c_2390
http://aims.fao.org/aos/agrovoc/c_3887
http://aims.fao.org/aos/agrovoc/c_25427
http://aims.fao.org/aos/agrovoc/c_3842
http://aims.fao.org/aos/agrovoc/c_85
http://aims.fao.org/aos/agrovoc/c_342
Villatte, F.
Ziliani, Philippe
Marcel, Véronique
Menozzi, Philippe
Fournier, Didier
A high number of mutations in insect acetylcholinesterase may provide insecticide resistance
description Many insect pest species have developed insecticide resistance through modifications of acetylcholinesterase. Seven mutations, issued from one nucleotide change, have been associated with resistance in natural populations of Drosophila and housefly (A. Mutero, M. Pralavorio, J. M, Bride, and D. Fournier, Resistance-associated point mutations in insecticide insensitive acetylcholinesterase, Proc. Nail. Acad Sci. USA 91, 5922 (1994); A. L. Devonshire, F. J. Byrne, G. D. Moores, and M. S. Williamson, Biochemical and molecular characterisation of insecticide- insensitive acetylcholinesterases in resistant insects, in "Structure and function of cholinesterases and related proteins- (B. P. Doctor, P. Taylor, D. M. Quinn, R. L. Rotundo, and M, K. Gentry, Eds.), pp. 491-496, Plenum Press, New York, 1998). In order to study the number of mutations which can lead to resistance, we first analyzed the effects of a set of amino acid replacements in the Drosophila acetylcholinesterase on inhibition by several carbamate and organophosphate insecticides. It appeared that most of the mutations led to a reduced sensitivity to insecticides. Second, we investigated the effect of mutations on substrate hydrolysis. We found that most of the variants retained sufficient levels of substrate hydrolysis. These data suggest that more mutations in acetylcholinesterase may be involved in organophosphate and carbamate resistance in addition to the previously known seven mutations.
format article
topic_facet H10 - Ravageurs des plantes
Drosophila
insecticide
résistance aux pesticides
mutation provoquée
acétylcholinestérase
acide aminé
http://aims.fao.org/aos/agrovoc/c_2390
http://aims.fao.org/aos/agrovoc/c_3887
http://aims.fao.org/aos/agrovoc/c_25427
http://aims.fao.org/aos/agrovoc/c_3842
http://aims.fao.org/aos/agrovoc/c_85
http://aims.fao.org/aos/agrovoc/c_342
author Villatte, F.
Ziliani, Philippe
Marcel, Véronique
Menozzi, Philippe
Fournier, Didier
author_facet Villatte, F.
Ziliani, Philippe
Marcel, Véronique
Menozzi, Philippe
Fournier, Didier
author_sort Villatte, F.
title A high number of mutations in insect acetylcholinesterase may provide insecticide resistance
title_short A high number of mutations in insect acetylcholinesterase may provide insecticide resistance
title_full A high number of mutations in insect acetylcholinesterase may provide insecticide resistance
title_fullStr A high number of mutations in insect acetylcholinesterase may provide insecticide resistance
title_full_unstemmed A high number of mutations in insect acetylcholinesterase may provide insecticide resistance
title_sort high number of mutations in insect acetylcholinesterase may provide insecticide resistance
url http://agritrop.cirad.fr/487534/
http://agritrop.cirad.fr/487534/1/487534.pdf
work_keys_str_mv AT villattef ahighnumberofmutationsininsectacetylcholinesterasemayprovideinsecticideresistance
AT zilianiphilippe ahighnumberofmutationsininsectacetylcholinesterasemayprovideinsecticideresistance
AT marcelveronique ahighnumberofmutationsininsectacetylcholinesterasemayprovideinsecticideresistance
AT menozziphilippe ahighnumberofmutationsininsectacetylcholinesterasemayprovideinsecticideresistance
AT fournierdidier ahighnumberofmutationsininsectacetylcholinesterasemayprovideinsecticideresistance
AT villattef highnumberofmutationsininsectacetylcholinesterasemayprovideinsecticideresistance
AT zilianiphilippe highnumberofmutationsininsectacetylcholinesterasemayprovideinsecticideresistance
AT marcelveronique highnumberofmutationsininsectacetylcholinesterasemayprovideinsecticideresistance
AT menozziphilippe highnumberofmutationsininsectacetylcholinesterasemayprovideinsecticideresistance
AT fournierdidier highnumberofmutationsininsectacetylcholinesterasemayprovideinsecticideresistance
_version_ 1792495176575352832