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.
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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, |
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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 |
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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 |
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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 |
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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. |
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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 |
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