Identification and characterization of ace2-type acetylcholinesterase in insecticide-resistant and -susceptible parasitoid wasp Oomyzus sokolowskii (Hymenoptera: Eulophidae).
Mol Biol Rep
; 41(11): 7525-34, 2014 Nov.
Article
em En
| MEDLINE
| ID: mdl-25074274
ABSTRACT
A full-length acetylcholinesterase (AChE) cDNA sequence (Os-ace2.s) from insecticide-susceptible (S) parasitoid Oomyzus sokolowskii (Hymenoptera Eulophidae) and a partial cDNA sequence (Os-ace2.r) from insecticide- resistant (R) O. sokolowskii were identified firstly. Both Os-ace2.s (encoding a protein of 639 amino acid residues) and Os-ace2.r (encoding a protein of 530 amino acid residues) contained the typical conserved motifs, including FGESAGdomains, catalytic triad, acyl pocket, three oxy-anino hole, choline binding site, peripheral anionic site, omega loop and conserved aromatic residues. The multiple alignment and Blast results indicated that Os-ace2.s were ace2 member of AChE gene. There were three replacements of the amino acid residues (Glu 115 Leu, Phe 394 Leu, and Lys 424 Arg) between Os-ace2.s and Os-ace2.r. The ace2 of O. sokolowskii was the AChE gene firstly isolated from hymenopteran parasitoid so far. R O. sokolowskii displayed about 15-20-folds resistance ratios to methamidophos and avermectin. The bimolecular rate constant (k i) value in S O. sokolowskii was 3.8-folds for methamidophos and 12.3 for dichlorvos, respectively higher than those in R O. sokolowskii. The results indicated that the insensitive AChE and replacements of the amino acid residues in Os-ace2 might be involved in the resistance to methamidophos in R O. sokolowskii.
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Base de dados:
MEDLINE
Assunto principal:
Acetilcolinesterase
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Vespas
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Resistência a Inseticidas
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article