Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila

Faisal Younus; Nicholas J. Fraser; Chris W. Coppin; Jian Wei Liu; Galen J. Correy; Thomas Chertemps; Gunjan Pandey; Martine Maïbèche; Colin J. Jackson; John G. Oakeshott

doi:10.1038/srep46188

Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila

Faisal Younus, Nicholas J. Fraser, Chris W. Coppin, Jian Wei Liu, Galen J. Correy, Thomas Chertemps, Gunjan Pandey, Martine Maïbèche, Colin J. Jackson, John G. Oakeshott^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

38 Citations (Scopus)

Abstract

Previous electrophysiological and behavioural studies implicate esterase 6 in the processing of the pheromone cis-vaccenyl acetate and various food odorants that affect aggregation and reproductive behaviours. Here we show esterase 6 has relatively high activity against many of the short-mid chain food esters, but negligible activity against cis-vaccenyl acetate. The crystal structure of esterase 6 confirms its substrate-binding site can accommodate many short-mid chain food esters but not cis-vaccenyl acetate. Immunohistochemical assays show esterase 6 is expressed in non-neuronal cells in the third antennal segment that could be accessory or epidermal cells surrounding numerous olfactory sensilla, including basiconics involved in food odorant detection. Esterase 6 is also produced in trichoid sensilla, but not in the same cell types as the cis-vaccenyl acetate binding protein LUSH. Our data support a model in which esterase 6 acts as a direct odorant degrading enzyme for many bioactive food esters, but not cis-vaccenyl acetate.

Original language	English
Article number	46188
Journal	Scientific Reports
Volume	7
DOIs	https://doi.org/10.1038/srep46188
Publication status	Published - 10 Apr 2017

Access to Document

10.1038/srep46188

Cite this

@article{668dbeb25b994805a04b43c20cbd39d1,

title = "Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila",

abstract = "Previous electrophysiological and behavioural studies implicate esterase 6 in the processing of the pheromone cis-vaccenyl acetate and various food odorants that affect aggregation and reproductive behaviours. Here we show esterase 6 has relatively high activity against many of the short-mid chain food esters, but negligible activity against cis-vaccenyl acetate. The crystal structure of esterase 6 confirms its substrate-binding site can accommodate many short-mid chain food esters but not cis-vaccenyl acetate. Immunohistochemical assays show esterase 6 is expressed in non-neuronal cells in the third antennal segment that could be accessory or epidermal cells surrounding numerous olfactory sensilla, including basiconics involved in food odorant detection. Esterase 6 is also produced in trichoid sensilla, but not in the same cell types as the cis-vaccenyl acetate binding protein LUSH. Our data support a model in which esterase 6 acts as a direct odorant degrading enzyme for many bioactive food esters, but not cis-vaccenyl acetate.",

author = "Faisal Younus and Fraser, {Nicholas J.} and Coppin, {Chris W.} and Liu, {Jian Wei} and Correy, {Galen J.} and Thomas Chertemps and Gunjan Pandey and Martine Ma{\"i}b{\`e}che and Jackson, {Colin J.} and Oakeshott, {John G.}",

note = "Publisher Copyright: {\textcopyright} 2017 The Author(s).",

year = "2017",

month = apr,

day = "10",

doi = "10.1038/srep46188",

language = "English",

volume = "7",

journal = "Scientific Reports",

issn = "2045-2322",

publisher = "Nature Publishing Group",

}

TY - JOUR

T1 - Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila

AU - Younus, Faisal

AU - Fraser, Nicholas J.

AU - Coppin, Chris W.

AU - Liu, Jian Wei

AU - Correy, Galen J.

AU - Chertemps, Thomas

AU - Pandey, Gunjan

AU - Maïbèche, Martine

AU - Jackson, Colin J.

AU - Oakeshott, John G.

PY - 2017/4/10

Y1 - 2017/4/10

N2 - Previous electrophysiological and behavioural studies implicate esterase 6 in the processing of the pheromone cis-vaccenyl acetate and various food odorants that affect aggregation and reproductive behaviours. Here we show esterase 6 has relatively high activity against many of the short-mid chain food esters, but negligible activity against cis-vaccenyl acetate. The crystal structure of esterase 6 confirms its substrate-binding site can accommodate many short-mid chain food esters but not cis-vaccenyl acetate. Immunohistochemical assays show esterase 6 is expressed in non-neuronal cells in the third antennal segment that could be accessory or epidermal cells surrounding numerous olfactory sensilla, including basiconics involved in food odorant detection. Esterase 6 is also produced in trichoid sensilla, but not in the same cell types as the cis-vaccenyl acetate binding protein LUSH. Our data support a model in which esterase 6 acts as a direct odorant degrading enzyme for many bioactive food esters, but not cis-vaccenyl acetate.

AB - Previous electrophysiological and behavioural studies implicate esterase 6 in the processing of the pheromone cis-vaccenyl acetate and various food odorants that affect aggregation and reproductive behaviours. Here we show esterase 6 has relatively high activity against many of the short-mid chain food esters, but negligible activity against cis-vaccenyl acetate. The crystal structure of esterase 6 confirms its substrate-binding site can accommodate many short-mid chain food esters but not cis-vaccenyl acetate. Immunohistochemical assays show esterase 6 is expressed in non-neuronal cells in the third antennal segment that could be accessory or epidermal cells surrounding numerous olfactory sensilla, including basiconics involved in food odorant detection. Esterase 6 is also produced in trichoid sensilla, but not in the same cell types as the cis-vaccenyl acetate binding protein LUSH. Our data support a model in which esterase 6 acts as a direct odorant degrading enzyme for many bioactive food esters, but not cis-vaccenyl acetate.

UR - http://www.scopus.com/inward/record.url?scp=85017357980&partnerID=8YFLogxK

U2 - 10.1038/srep46188

DO - 10.1038/srep46188

M3 - Article

SN - 2045-2322

VL - 7

JO - Scientific Reports

JF - Scientific Reports

M1 - 46188

ER -

Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila

Abstract

Access to Document

Other files and links

Fingerprint

Cite this