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

Mark G. Teese, Peter M. Campbell, Colin Scott, Karl H.J. Gordon, Adam Southon, Daniel Hovan, Charles Robin, Robyn J. Russell, John G. Oakeshott*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    66 Citations (Scopus)

    Abstract

    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. mori 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.

    Original languageEnglish
    Pages (from-to)1-16
    Number of pages16
    JournalInsect Biochemistry and Molecular Biology
    Volume40
    Issue number1
    DOIs
    Publication statusPublished - Jan 2010

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