Is acetyl/butyrylcholine specificity a marker for insecticide-resistance mutations in insect acetylcholinesterase ?
Substrate specificity has been widely studied in vertebrate cholinesterases and it has been shown that two phenylalanines in the acyl pocket of acetylcholinesterase govern the acceptance of the acetyl/butyryl moiety of the choline esters. As an insecticide-resistance mutation has been evidenced in the acyl pocket of Drosophila melanogaster and Musca domestica acetylcholinesterase we investigated the possibility of linking changes in acetyl/butyrylthiocholine specificity with mutations in insect acetylcholinesterase. We thus analyzed the effect of 28 mutations in Drosophila enzyme on acetyl/butyrylthiocholine, N-methyl/N-propyl-carbamates and ethyl/methyl-paraoxon preference. It appeared that the highest changes on acetyl/butyrylthiocholine and N-propyl/N-methyl-carbamates preference were due to mutations in the acyl pocket. Nevertheless, other insecticide-resistance mutations, not located in the acyl pocket, also modified these substrate preferences. Moreover, the effect of mutations in the acyl pocket was hidden when some other insecticide-resistance mutations were combined in the enzyme. Consequently, acetyl/butyrylthiocholine preference alteration cannot be used as a marker to localize a mutation in the insect AChE.
| Main Authors: | , , , , |
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| Format: | article biblioteca |
| Language: | eng |
| Subjects: | H10 - Ravageurs des plantes, résistance aux produits chimiques, insecticide, mutation, choline, Drosophila melanogaster, Musca domestica, acétylcholinestérase, http://aims.fao.org/aos/agrovoc/c_5736, http://aims.fao.org/aos/agrovoc/c_3887, http://aims.fao.org/aos/agrovoc/c_5014, http://aims.fao.org/aos/agrovoc/c_1585, http://aims.fao.org/aos/agrovoc/c_30543, http://aims.fao.org/aos/agrovoc/c_30566, http://aims.fao.org/aos/agrovoc/c_85, |
| Online Access: | http://agritrop.cirad.fr/486151/ http://agritrop.cirad.fr/486151/1/ID486151.pdf |
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| Summary: | Substrate specificity has been widely studied in vertebrate cholinesterases and it has been shown that two phenylalanines in the acyl pocket of acetylcholinesterase govern the acceptance of the acetyl/butyryl moiety of the choline esters. As an insecticide-resistance mutation has been evidenced in the acyl pocket of Drosophila melanogaster and Musca domestica acetylcholinesterase we investigated the possibility of linking changes in acetyl/butyrylthiocholine specificity with mutations in insect acetylcholinesterase. We thus analyzed the effect of 28 mutations in Drosophila enzyme on acetyl/butyrylthiocholine, N-methyl/N-propyl-carbamates and ethyl/methyl-paraoxon preference. It appeared that the highest changes on acetyl/butyrylthiocholine and N-propyl/N-methyl-carbamates preference were due to mutations in the acyl pocket. Nevertheless, other insecticide-resistance mutations, not located in the acyl pocket, also modified these substrate preferences. Moreover, the effect of mutations in the acyl pocket was hidden when some other insecticide-resistance mutations were combined in the enzyme. Consequently, acetyl/butyrylthiocholine preference alteration cannot be used as a marker to localize a mutation in the insect AChE. |
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