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 |