Drosophila acetylcholinesterase: Mechanisms of resistance to organophosphates
Quantitative and qualitative changes of acetylcholinesterase can affect the sensitivity of insects to insecticides. First, the amount of acetylcholinesterase in the central nervous system is important in Drosophila melanogaster, flies which overexpress the enzyme are more resistant than wild-type fl...
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| Veröffentlicht in: | Chemico-biological interactions 1993-06, Vol.87 (1), p.233-238 |
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| creator | Fournier, Didier Mutero, Annick Pralavorio, Madeleine Bride, Jean-Marc |
| description | Quantitative and qualitative changes of acetylcholinesterase can affect the sensitivity of insects to insecticides. First, the amount of acetylcholinesterase in the central nervous system is important in
Drosophila melanogaster, flies which overexpress the enzyme are more resistant than wild-type flies. On the contrary, flies which express low levels of acetylcholinesterase are more susceptible. An overproduction of acetylcholinesterase outside the central nervous system also protects against organophosphate poisoning, that is, flies producing a soluble acetylcholinesterase, secreted in the haemolymph, are resistant to organophosphates. Second, resistance can also result from a qualitative modification of acetylcholinesterase. Four mutations have been identified in resistant strains: Phe
115 to Ser, Ileu
199 to Val, Gly
303 to Ala and Phe
368 to Tyr. Each of these mutations led to a different pattern of resistance and combinations between these mutations led to highly resistant enzymes. |
| doi_str_mv | 10.1016/0009-2797(93)90047-3 |
| format | Article |
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Drosophila melanogaster, flies which overexpress the enzyme are more resistant than wild-type flies. On the contrary, flies which express low levels of acetylcholinesterase are more susceptible. An overproduction of acetylcholinesterase outside the central nervous system also protects against organophosphate poisoning, that is, flies producing a soluble acetylcholinesterase, secreted in the haemolymph, are resistant to organophosphates. Second, resistance can also result from a qualitative modification of acetylcholinesterase. Four mutations have been identified in resistant strains: Phe
115 to Ser, Ileu
199 to Val, Gly
303 to Ala and Phe
368 to Tyr. Each of these mutations led to a different pattern of resistance and combinations between these mutations led to highly resistant enzymes.</description><identifier>ISSN: 0009-2797</identifier><identifier>EISSN: 1872-7786</identifier><identifier>DOI: 10.1016/0009-2797(93)90047-3</identifier><identifier>PMID: 8343979</identifier><identifier>CODEN: CBINA8</identifier><language>eng</language><publisher>Shannon: Elsevier Ireland Ltd</publisher><subject>Acetylcholinesterase ; Acetylcholinesterase - genetics ; Acetylcholinesterase - metabolism ; Animals ; Biological and medical sciences ; Chemical control ; Cholinesterase Inhibitors - pharmacology ; Control ; Drosophila melanogaster - enzymology ; Drosophila melanogaster - genetics ; Fundamental and applied biological sciences. Psychology ; Insecticide ; Insecticide Resistance - genetics ; Insecticides - pharmacology ; Invertebrates ; Life Sciences ; Organophosphates ; Organophosphorus Compounds ; Phytopathology. Animal pests. Plant and forest protection ; Point Mutation ; Protozoa. Invertebrates ; Resistance</subject><ispartof>Chemico-biological interactions, 1993-06, Vol.87 (1), p.233-238</ispartof><rights>1993</rights><rights>1993 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c420t-636108830e674d964836532e6582f6d4357453255cf60489d89cd67d0af88c03</citedby><cites>FETCH-LOGICAL-c420t-636108830e674d964836532e6582f6d4357453255cf60489d89cd67d0af88c03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0009279793900473$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,309,310,314,776,780,785,786,881,3537,23909,23910,25118,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4799221$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8343979$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02708213$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Fournier, Didier</creatorcontrib><creatorcontrib>Mutero, Annick</creatorcontrib><creatorcontrib>Pralavorio, Madeleine</creatorcontrib><creatorcontrib>Bride, Jean-Marc</creatorcontrib><title>Drosophila acetylcholinesterase: Mechanisms of resistance to organophosphates</title><title>Chemico-biological interactions</title><addtitle>Chem Biol Interact</addtitle><description>Quantitative and qualitative changes of acetylcholinesterase can affect the sensitivity of insects to insecticides. First, the amount of acetylcholinesterase in the central nervous system is important in
Drosophila melanogaster, flies which overexpress the enzyme are more resistant than wild-type flies. On the contrary, flies which express low levels of acetylcholinesterase are more susceptible. An overproduction of acetylcholinesterase outside the central nervous system also protects against organophosphate poisoning, that is, flies producing a soluble acetylcholinesterase, secreted in the haemolymph, are resistant to organophosphates. Second, resistance can also result from a qualitative modification of acetylcholinesterase. Four mutations have been identified in resistant strains: Phe
115 to Ser, Ileu
199 to Val, Gly
303 to Ala and Phe
368 to Tyr. Each of these mutations led to a different pattern of resistance and combinations between these mutations led to highly resistant enzymes.</description><subject>Acetylcholinesterase</subject><subject>Acetylcholinesterase - genetics</subject><subject>Acetylcholinesterase - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Chemical control</subject><subject>Cholinesterase Inhibitors - pharmacology</subject><subject>Control</subject><subject>Drosophila melanogaster - enzymology</subject><subject>Drosophila melanogaster - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Insecticide</subject><subject>Insecticide Resistance - genetics</subject><subject>Insecticides - pharmacology</subject><subject>Invertebrates</subject><subject>Life Sciences</subject><subject>Organophosphates</subject><subject>Organophosphorus Compounds</subject><subject>Phytopathology. Animal pests. Plant and forest protection</subject><subject>Point Mutation</subject><subject>Protozoa. Invertebrates</subject><subject>Resistance</subject><issn>0009-2797</issn><issn>1872-7786</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kD1PwzAQhi0EglL4ByBlYIAhcLEdfzAgIb6KVMTCbhnnQozSurIDEv8eh1YdmazzPa_v_BByUsFlBZW4AgBdUqnluWYXGoDLku2QSaUkLaVUYpdMtsgBOUzpM5dAOeyTfcU401JPyMt9DCmsOt_bwjocfnrXhd4vMQ0YbcLr4gVdZ5c-LVIR2iJi8mmwS4fFEIoQP-wyp0NadXbAdET2WtsnPN6cU_L2-PB2Nyvnr0_Pd7fz0nEKQymYqEApBigkb7TgiomaURS1oq1oOKslz3Vdu1YAV7pR2jVCNmBbpRywKblYP9vZ3qyiX9j4Y4L1ZnY7N-MdUAmKVuy7yixfsy5_NEVst4EKzOjRjJLMKMloZv48GpZjp-vY6ut9gc02tBGX-2ebvk3O9m3MSnzaYlxqTek4_WaNYbbx7TGa5Dxme42P6AbTBP__Hr_gjI0z</recordid><startdate>19930601</startdate><enddate>19930601</enddate><creator>Fournier, Didier</creator><creator>Mutero, Annick</creator><creator>Pralavorio, Madeleine</creator><creator>Bride, Jean-Marc</creator><general>Elsevier Ireland Ltd</general><general>Elsevier Science</general><general>Elsevier [1969-....]</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>1XC</scope></search><sort><creationdate>19930601</creationdate><title>Drosophila acetylcholinesterase: Mechanisms of resistance to organophosphates</title><author>Fournier, Didier ; Mutero, Annick ; Pralavorio, Madeleine ; Bride, Jean-Marc</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c420t-636108830e674d964836532e6582f6d4357453255cf60489d89cd67d0af88c03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Acetylcholinesterase</topic><topic>Acetylcholinesterase - genetics</topic><topic>Acetylcholinesterase - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Chemical control</topic><topic>Cholinesterase Inhibitors - pharmacology</topic><topic>Control</topic><topic>Drosophila melanogaster - enzymology</topic><topic>Drosophila melanogaster - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Insecticide</topic><topic>Insecticide Resistance - genetics</topic><topic>Insecticides - pharmacology</topic><topic>Invertebrates</topic><topic>Life Sciences</topic><topic>Organophosphates</topic><topic>Organophosphorus Compounds</topic><topic>Phytopathology. Animal pests. Plant and forest protection</topic><topic>Point Mutation</topic><topic>Protozoa. Invertebrates</topic><topic>Resistance</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fournier, Didier</creatorcontrib><creatorcontrib>Mutero, Annick</creatorcontrib><creatorcontrib>Pralavorio, Madeleine</creatorcontrib><creatorcontrib>Bride, Jean-Marc</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Chemico-biological interactions</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fournier, Didier</au><au>Mutero, Annick</au><au>Pralavorio, Madeleine</au><au>Bride, Jean-Marc</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Drosophila acetylcholinesterase: Mechanisms of resistance to organophosphates</atitle><jtitle>Chemico-biological interactions</jtitle><addtitle>Chem Biol Interact</addtitle><date>1993-06-01</date><risdate>1993</risdate><volume>87</volume><issue>1</issue><spage>233</spage><epage>238</epage><pages>233-238</pages><issn>0009-2797</issn><eissn>1872-7786</eissn><coden>CBINA8</coden><abstract>Quantitative and qualitative changes of acetylcholinesterase can affect the sensitivity of insects to insecticides. First, the amount of acetylcholinesterase in the central nervous system is important in
Drosophila melanogaster, flies which overexpress the enzyme are more resistant than wild-type flies. On the contrary, flies which express low levels of acetylcholinesterase are more susceptible. An overproduction of acetylcholinesterase outside the central nervous system also protects against organophosphate poisoning, that is, flies producing a soluble acetylcholinesterase, secreted in the haemolymph, are resistant to organophosphates. Second, resistance can also result from a qualitative modification of acetylcholinesterase. Four mutations have been identified in resistant strains: Phe
115 to Ser, Ileu
199 to Val, Gly
303 to Ala and Phe
368 to Tyr. Each of these mutations led to a different pattern of resistance and combinations between these mutations led to highly resistant enzymes.</abstract><cop>Shannon</cop><pub>Elsevier Ireland Ltd</pub><pmid>8343979</pmid><doi>10.1016/0009-2797(93)90047-3</doi><tpages>6</tpages></addata></record> |
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| ispartof | Chemico-biological interactions, 1993-06, Vol.87 (1), p.233-238 |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Acetylcholinesterase Acetylcholinesterase - genetics Acetylcholinesterase - metabolism Animals Biological and medical sciences Chemical control Cholinesterase Inhibitors - pharmacology Control Drosophila melanogaster - enzymology Drosophila melanogaster - genetics Fundamental and applied biological sciences. Psychology Insecticide Insecticide Resistance - genetics Insecticides - pharmacology Invertebrates Life Sciences Organophosphates Organophosphorus Compounds Phytopathology. Animal pests. Plant and forest protection Point Mutation Protozoa. Invertebrates Resistance |
| title | Drosophila acetylcholinesterase: Mechanisms of resistance to organophosphates |
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