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Identification and Characterization of an Antennae-Specific Aldehyde Oxidase from the Navel Orangeworm
Antennae-specific odorant-degrading enzymes (ODEs) are postulated to inactivate odorant molecules after they convey their signal. Different classes of insect ODEs are specific to esters, alcohols, and aldehydes – the major functional groups of female-produced, hydrophobic sex pheromones from moth sp...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Public Library of Science
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3691121/ https://www.ncbi.nlm.nih.gov/pubmed/23826341 http://dx.doi.org/10.1371/journal.pone.0067794 |
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author | Choo, Young-Moo Pelletier, Julien Atungulu, Elizabeth Leal, Walter S. |
author_facet | Choo, Young-Moo Pelletier, Julien Atungulu, Elizabeth Leal, Walter S. |
author_sort | Choo, Young-Moo |
collection | PubMed |
description | Antennae-specific odorant-degrading enzymes (ODEs) are postulated to inactivate odorant molecules after they convey their signal. Different classes of insect ODEs are specific to esters, alcohols, and aldehydes – the major functional groups of female-produced, hydrophobic sex pheromones from moth species. Esterases that rapidly inactive acetate and other esters have been well-studied, but less is known about aldehyde oxidases (AOXs). Here we report cloning of an aldehyde oxidase, AtraAOX2, from the antennae of the navel orangeworm (NOW), Amyelois transitella, and the first activity characterization of a recombinant insect AOX. AtraAOX2 gene spans 3,813 bp and encodes a protein with 1,270 amino acid residues. AtraAOX2 cDNA was expressed in baculovirus-infected insect Sf21 cells as a ≈280 kDa homodimer with 140 kDa subunits. Recombinant AtraAOX2 degraded Z11Z13–16Ald and plant volatile aldehydes as substrates. However, as expected for aldehyde oxidases, recombinant AtraAOX2 did not show specificity for Z11Z13–16Ald, the main constituent of the sex pheromone, but showed high activity for plant volatile aldehydes. Our data suggest AtraAOX2 might be involved in degradation of a diversity of aldehydes including sex pheromones, plant-derived semiochemicals, and chemical cues for oviposition sites. Additionally, AtraAOX2 could protect the insect's olfactory system from xenobiotics, including pesticides that might reach the sensillar lymph surrounding the olfactory receptor neurons. |
format | Online Article Text |
id | pubmed-3691121 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-36911212013-07-03 Identification and Characterization of an Antennae-Specific Aldehyde Oxidase from the Navel Orangeworm Choo, Young-Moo Pelletier, Julien Atungulu, Elizabeth Leal, Walter S. PLoS One Research Article Antennae-specific odorant-degrading enzymes (ODEs) are postulated to inactivate odorant molecules after they convey their signal. Different classes of insect ODEs are specific to esters, alcohols, and aldehydes – the major functional groups of female-produced, hydrophobic sex pheromones from moth species. Esterases that rapidly inactive acetate and other esters have been well-studied, but less is known about aldehyde oxidases (AOXs). Here we report cloning of an aldehyde oxidase, AtraAOX2, from the antennae of the navel orangeworm (NOW), Amyelois transitella, and the first activity characterization of a recombinant insect AOX. AtraAOX2 gene spans 3,813 bp and encodes a protein with 1,270 amino acid residues. AtraAOX2 cDNA was expressed in baculovirus-infected insect Sf21 cells as a ≈280 kDa homodimer with 140 kDa subunits. Recombinant AtraAOX2 degraded Z11Z13–16Ald and plant volatile aldehydes as substrates. However, as expected for aldehyde oxidases, recombinant AtraAOX2 did not show specificity for Z11Z13–16Ald, the main constituent of the sex pheromone, but showed high activity for plant volatile aldehydes. Our data suggest AtraAOX2 might be involved in degradation of a diversity of aldehydes including sex pheromones, plant-derived semiochemicals, and chemical cues for oviposition sites. Additionally, AtraAOX2 could protect the insect's olfactory system from xenobiotics, including pesticides that might reach the sensillar lymph surrounding the olfactory receptor neurons. Public Library of Science 2013-06-24 /pmc/articles/PMC3691121/ /pubmed/23826341 http://dx.doi.org/10.1371/journal.pone.0067794 Text en © 2013 Choo et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Choo, Young-Moo Pelletier, Julien Atungulu, Elizabeth Leal, Walter S. Identification and Characterization of an Antennae-Specific Aldehyde Oxidase from the Navel Orangeworm |
title | Identification and Characterization of an Antennae-Specific Aldehyde Oxidase from the Navel Orangeworm |
title_full | Identification and Characterization of an Antennae-Specific Aldehyde Oxidase from the Navel Orangeworm |
title_fullStr | Identification and Characterization of an Antennae-Specific Aldehyde Oxidase from the Navel Orangeworm |
title_full_unstemmed | Identification and Characterization of an Antennae-Specific Aldehyde Oxidase from the Navel Orangeworm |
title_short | Identification and Characterization of an Antennae-Specific Aldehyde Oxidase from the Navel Orangeworm |
title_sort | identification and characterization of an antennae-specific aldehyde oxidase from the navel orangeworm |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3691121/ https://www.ncbi.nlm.nih.gov/pubmed/23826341 http://dx.doi.org/10.1371/journal.pone.0067794 |
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