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« Previous Abstract"The Peripheral Olfactory Repertoire of the Lightbrown Apple Moth, Epiphyas postvittana"    Next AbstractPollination of Campomanesia phaea (Myrtaceae) by night-active bees: a new nocturnal pollination system mediated by floral scent »

Curr Res Insect Sci


Title:Structure of an antennally-expressed carboxylesterase suggests lepidopteran odorant degrading enzymes are broadly tuned
Author(s):Corcoran JA; Hamiaux C; Faraone N; Lofstedt C; Carraher C;
Address:"USDA - Agricultural Research Service, Biological Control of Insects Research Laboratory, Columbia, MO, USA. Department of Biology, Lund University, Lund, Sweden. The New Zealand Institute for Plant and Food Research Limited, Auckland, New Zealand. Department of Chemistry, Acadia University, Wolfville, Nova Scotia, Canada"
Journal Title:Curr Res Insect Sci
Year:2023
Volume:20230605
Issue:
Page Number:100062 -
DOI: 10.1016/j.cris.2023.100062
ISSN/ISBN:2666-5158 (Electronic) 2666-5158 (Linking)
Abstract:"Insects rely on the detection of chemical cues present in the environment to guide their foraging and reproductive behaviour. As such, insects have evolved a sophisticated chemical processing system in their antennae comprised of several types of olfactory proteins. Of these proteins, odorant degrading enzymes are responsible for metabolising the chemical cues within the antennae, thereby maintaining olfactory system function. Members of the carboxyl/cholinesterase gene family are known to degrade odorant molecules with acetate-ester moieties that function as host recognition cues or sex pheromones, however, their specificity for these compounds remains unclear. Here, we evaluate expression levels of this gene family in the light-brown apple moth, Epiphyas postvittana, via RNAseq and identify putative odorant degrading enzymes. We then solve the apo-structure for EposCCE24 by X-ray crystallography to a resolution of 2.43 A and infer substrate specificity based on structural characteristics of the enzyme's binding pocket. The specificity of EposCCE24 was validated by testing its ability to degrade biologically relevant and non-relevant sex pheromone components and plant volatiles using GC-MS. We found that EposCCE24 is neither capable of discriminating between linear acetate-ester odorant molecules of varying chain length, nor between molecules with varying double bond positions. EposCCE24 efficiently degraded both plant volatiles and sex pheromone components containing acetate-ester functional groups, confirming its role as a broadly-tuned odorant degrading enzyme in the moth olfactory organ"
Keywords:Carboxyl/cholinesterase Crystal structure Epiphyas postvittana Gc-ms Odorant degrading enzyme RNAseq;
Notes:"PubMed-not-MEDLINECorcoran, Jacob A Hamiaux, Cyril Faraone, Nicoletta Lofstedt, Christer Carraher, Colm eng Netherlands 2023/07/03 Curr Res Insect Sci. 2023 Jun 5; 3:100062. doi: 10.1016/j.cris.2023.100062. eCollection 2023"

 
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Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
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