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Identification and Characterization of an Antennae-Specific Glutathione S-Transferase From the Indian Meal Moth
Insect glutathione-S-transferases (GSTs) play essential roles in metabolizing endogenous and exogenous compounds. GSTs that are uniquely expressed in antennae are assumed to function as scavengers of pheromones and host volatiles in the odorant detection system. Based on this assumption, antennae-sp...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8427598/ https://www.ncbi.nlm.nih.gov/pubmed/34512396 http://dx.doi.org/10.3389/fphys.2021.727619 |
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author | Liu, Hongmin Tang, Yin Wang, Qinying Shi, Hongzhong Yin, Jian Li, Chengjun |
author_facet | Liu, Hongmin Tang, Yin Wang, Qinying Shi, Hongzhong Yin, Jian Li, Chengjun |
author_sort | Liu, Hongmin |
collection | PubMed |
description | Insect glutathione-S-transferases (GSTs) play essential roles in metabolizing endogenous and exogenous compounds. GSTs that are uniquely expressed in antennae are assumed to function as scavengers of pheromones and host volatiles in the odorant detection system. Based on this assumption, antennae-specific GSTs have been identified and functionally characterized in increasing number of insect species. In the present study, 17 putative GSTs were identified from the antennal transcriptomic dataset of the Indian meal moth, Plodia interpunctella, a severe stored-grain pest worldwide. Among the GSTs, only PiGSTd1 is antennae-specific according to both Fragments Per Kilobase Million (FPKM) and quantitative real-time PCR (qRT-PCR) analysis. Sequence analysis revealed that PiGSTd1 has a similar identity as many delta GSTs from other moths. Enzyme kinetic assays using 1-chloro-2,4-dinitrobenzene (CDNB) as substrates showed that the recombinant PiGSTd1 gave a K(m) of 0.2292 ± 0.01805 mM and a V(max) of 14.02 ± 0.2545 μmol·mg(−1)·min(−1) under the optimal catalytic conditions (35°C and pH = 7.5). Further analysis revealed that the recombinant PiGSTd1 could efficiently degrade the sex pheromone component Z9-12:Ac (75.63 ± 5.52%), as well as aldehyde volatiles, including hexanal (89.10 ± 2.21%), heptanal (63.19 ± 5.36%), (E)-2-octenal (73.58 ± 3.92%), (E)-2-nonenal (75.81 ± 1.90%), and (E)-2-decenal (61.13 ± 5.24%). Taken together, our findings suggest that PiGSTd1 may play essential roles in degrading and inactivating a variety of odorants, especially sex pheromones and host volatiles of P. interpunctella. |
format | Online Article Text |
id | pubmed-8427598 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-84275982021-09-10 Identification and Characterization of an Antennae-Specific Glutathione S-Transferase From the Indian Meal Moth Liu, Hongmin Tang, Yin Wang, Qinying Shi, Hongzhong Yin, Jian Li, Chengjun Front Physiol Physiology Insect glutathione-S-transferases (GSTs) play essential roles in metabolizing endogenous and exogenous compounds. GSTs that are uniquely expressed in antennae are assumed to function as scavengers of pheromones and host volatiles in the odorant detection system. Based on this assumption, antennae-specific GSTs have been identified and functionally characterized in increasing number of insect species. In the present study, 17 putative GSTs were identified from the antennal transcriptomic dataset of the Indian meal moth, Plodia interpunctella, a severe stored-grain pest worldwide. Among the GSTs, only PiGSTd1 is antennae-specific according to both Fragments Per Kilobase Million (FPKM) and quantitative real-time PCR (qRT-PCR) analysis. Sequence analysis revealed that PiGSTd1 has a similar identity as many delta GSTs from other moths. Enzyme kinetic assays using 1-chloro-2,4-dinitrobenzene (CDNB) as substrates showed that the recombinant PiGSTd1 gave a K(m) of 0.2292 ± 0.01805 mM and a V(max) of 14.02 ± 0.2545 μmol·mg(−1)·min(−1) under the optimal catalytic conditions (35°C and pH = 7.5). Further analysis revealed that the recombinant PiGSTd1 could efficiently degrade the sex pheromone component Z9-12:Ac (75.63 ± 5.52%), as well as aldehyde volatiles, including hexanal (89.10 ± 2.21%), heptanal (63.19 ± 5.36%), (E)-2-octenal (73.58 ± 3.92%), (E)-2-nonenal (75.81 ± 1.90%), and (E)-2-decenal (61.13 ± 5.24%). Taken together, our findings suggest that PiGSTd1 may play essential roles in degrading and inactivating a variety of odorants, especially sex pheromones and host volatiles of P. interpunctella. Frontiers Media S.A. 2021-08-26 /pmc/articles/PMC8427598/ /pubmed/34512396 http://dx.doi.org/10.3389/fphys.2021.727619 Text en Copyright © 2021 Liu, Tang, Wang, Shi, Yin and Li. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Physiology Liu, Hongmin Tang, Yin Wang, Qinying Shi, Hongzhong Yin, Jian Li, Chengjun Identification and Characterization of an Antennae-Specific Glutathione S-Transferase From the Indian Meal Moth |
title | Identification and Characterization of an Antennae-Specific Glutathione S-Transferase From the Indian Meal Moth |
title_full | Identification and Characterization of an Antennae-Specific Glutathione S-Transferase From the Indian Meal Moth |
title_fullStr | Identification and Characterization of an Antennae-Specific Glutathione S-Transferase From the Indian Meal Moth |
title_full_unstemmed | Identification and Characterization of an Antennae-Specific Glutathione S-Transferase From the Indian Meal Moth |
title_short | Identification and Characterization of an Antennae-Specific Glutathione S-Transferase From the Indian Meal Moth |
title_sort | identification and characterization of an antennae-specific glutathione s-transferase from the indian meal moth |
topic | Physiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8427598/ https://www.ncbi.nlm.nih.gov/pubmed/34512396 http://dx.doi.org/10.3389/fphys.2021.727619 |
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