Gene identification and proteomic analysis of the esterases of the cotton bollworm, Helicoverpa armigera

作者：Teese Mark G; Campbell Peter M; Scott Colin; Gordon Karl H J; Southon Adam; Hovan Daniel; Robin Charles; Russell Robyn J; Oakeshott John G^*

来源：Insect Biochemistry and Molecular Biology, 2010, 40(1): 1-16.

DOI：10.1016/j.ibmb.2009.12.002

• Comparative genomics
• Cholinesterase-like adhesion molecule
• Midgut
• GPI anchor
• Protein purification
• Tandem mass spectrometry

Some of the resistance of Helicoverpa armigera to conventional insecticides such as organophosphates and synthetic pyrethroids appears to be due to metabolic detoxification by carboxylesterases. To investigate the H. armigera carboxyl/cholinesterases, we created a data set of 39 putative paralogous H. armigera carboxyl/cholinesterase sequences from cDNA libraries and other sources. Phylogenetic analysis revealed a close relationship between these sequences and 70 carboxyl/cholinesterases from the recently sequenced genome of the silkworm, Bombyx mori, including several conserved clades of non-catalytic proteins. A juvenile hormone esterase candidate from H. armigera was identified, and B. man orthologues were proposed for 31% of the sequences examined, however low similarity was found between lepidopteran sequences and esterases previously associated with insecticide resistance from other insect orders. A proteomic analysis of larval esterases then enabled us to match seven of the H. armigera carboxyl/cholinesterase sequences to specific esterase isozymes. All identified sequences were predicted to encode catalytically active carboxylesterases, including six proteins with N-terminal signal peptides and N-glycans, with two also containing C-terminal signals for glycosylphosphatidylinositol anchor attachment. Five of these sequences were matched to zones of activity on native PAGE at relative mobility values previously associated with insecticide resistance in this species.

• 出版日期2010-1
• 单位CSIRO