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Altered acetylcholinesterase confers organophosphate resistance in the olive fruit fly Bactrocera oleae

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dc.contributor.author Vontas, JG en
dc.contributor.author Cosmidis, N en
dc.contributor.author Loukas, M en
dc.contributor.author Tsakas, S en
dc.contributor.author Hejazi, MJ en
dc.contributor.author Ayoutanti, A en
dc.contributor.author Hemingway, J en
dc.date.accessioned 2014-06-06T06:44:34Z
dc.date.available 2014-06-06T06:44:34Z
dc.date.issued 2001 en
dc.identifier.issn 00483575 en
dc.identifier.uri http://dx.doi.org/10.1006/pest.2001.2568 en
dc.identifier.uri http://62.217.125.90/xmlui/handle/123456789/1957
dc.subject Altered acetylcholinesterase en
dc.subject Bactrocera oleae en
dc.subject Dimethoate en
dc.subject Organophosphate resistance en
dc.subject.other Bactrocera oleae en
dc.subject.other Drosophila melanogaster en
dc.subject.other Hexapoda en
dc.subject.other Insecta en
dc.title Altered acetylcholinesterase confers organophosphate resistance in the olive fruit fly Bactrocera oleae en
heal.type journalArticle en
heal.identifier.primary 10.1006/pest.2001.2568 en
heal.publicationDate 2001 en
heal.abstract An organophosphate-resistant strain of the olive fruit fly Bactrocera oleae, the most important pest for olive orchards worldwide, was obtained by laboratory selection with dimethoate. Resistance mechanisms were investigated in comparison with the colonized parental strain and a field population collected from the same area after 12 years of continuous dimethoate-based insecticide pressure. Combined biochemical and bioassay data suggested that, although esterase and/or glutathione S-transferase metabolic pathways were present and active against dimethoate, they were not selected for and did not have a major role in resistance. There was no evidence of increased oxidase activity in the resistant strains or significant synergism of dimethoate toxicity by piperonyl butoxide; thus, oxidative metabolism was not a major component of resistance. An altered acetylcholinesterase (ACHE) with poorer catalytic efficiency for the substrate acetylthiocholine iodide and 5- to 16-fold lower sensitivity to inhibition by omethoate was the major resistance mechanism. Dimethoate selected the insensitive AChE allele(s) in the resistant insects, which were also insensitive to paraoxon, but the altered AChE mechanism conferred negative cross-resistance to the carbamate propoxur. © 2001 Academic Press. en
heal.journalName Pesticide Biochemistry and Physiology en
dc.identifier.issue 2 en
dc.identifier.volume 71 en
dc.identifier.doi 10.1006/pest.2001.2568 en
dc.identifier.spage 124 en
dc.identifier.epage 132 en


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