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RNA interference of a trehalose‐6‐phosphate synthase gene reveals its roles in the biosynthesis of chitin and lipids in Heortia vitessoides (Lepidoptera: Crambidae)

Trehalose‐6‐phosphate synthase (TPS), an enzyme that hydrolyzes two glucose molecules to yield trehalose, plays a pivotal role in various physiological processes. In this study, we cloned the trehalose‐6‐phosphate synthase gene (HvTPS) and investigated its expression patterns in various tissues and...

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Autores principales: Chen, Jing‐Xiang, Lyu, Zi‐Hao, Wang, Chun‐Yan, Cheng, Jie, Lin, Tong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7379938/
https://www.ncbi.nlm.nih.gov/pubmed/30397994
http://dx.doi.org/10.1111/1744-7917.12650
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author Chen, Jing‐Xiang
Lyu, Zi‐Hao
Wang, Chun‐Yan
Cheng, Jie
Lin, Tong
author_facet Chen, Jing‐Xiang
Lyu, Zi‐Hao
Wang, Chun‐Yan
Cheng, Jie
Lin, Tong
author_sort Chen, Jing‐Xiang
collection PubMed
description Trehalose‐6‐phosphate synthase (TPS), an enzyme that hydrolyzes two glucose molecules to yield trehalose, plays a pivotal role in various physiological processes. In this study, we cloned the trehalose‐6‐phosphate synthase gene (HvTPS) and investigated its expression patterns in various tissues and developmental stages in Heortia vitessoides Moore (Lepidoptera: Crambidae). HvTPS was highly expressed in the fat body and after pupation or before molting. We knocked down TPS in H. vitessoides by RNA interference and found that 3.0 μg of dsHvTPS resulted in optimal interference at 24 h and 36 h post‐injection and caused a sharp decline in the survival rate during the 5th instar larval–pupal stage and obviously abnormal or lethal phenotypes. Additionally, compared to the controls, TPS activity and trehalose contents were significantly lower and the glucose content was significantly higher 24 h or 36 h after injection with 3.0 μg of dsHvTPS. Furthermore, the silencing of HvTPS suppressed the expression of six key genes in the chitin biosynthesis pathway and one key gene related to lipid catabolism. The expression levels of two genes associated with lipid biosynthesis were upregulated. These results strongly suggest that HvTPS is essential for the normal growth and development of H. vitessoides and provide a reference for further studies of the utility of key genes involved in chitin and lipid biosynthesis for controlling insect development.
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spelling pubmed-73799382020-07-27 RNA interference of a trehalose‐6‐phosphate synthase gene reveals its roles in the biosynthesis of chitin and lipids in Heortia vitessoides (Lepidoptera: Crambidae) Chen, Jing‐Xiang Lyu, Zi‐Hao Wang, Chun‐Yan Cheng, Jie Lin, Tong Insect Sci Original Articles Trehalose‐6‐phosphate synthase (TPS), an enzyme that hydrolyzes two glucose molecules to yield trehalose, plays a pivotal role in various physiological processes. In this study, we cloned the trehalose‐6‐phosphate synthase gene (HvTPS) and investigated its expression patterns in various tissues and developmental stages in Heortia vitessoides Moore (Lepidoptera: Crambidae). HvTPS was highly expressed in the fat body and after pupation or before molting. We knocked down TPS in H. vitessoides by RNA interference and found that 3.0 μg of dsHvTPS resulted in optimal interference at 24 h and 36 h post‐injection and caused a sharp decline in the survival rate during the 5th instar larval–pupal stage and obviously abnormal or lethal phenotypes. Additionally, compared to the controls, TPS activity and trehalose contents were significantly lower and the glucose content was significantly higher 24 h or 36 h after injection with 3.0 μg of dsHvTPS. Furthermore, the silencing of HvTPS suppressed the expression of six key genes in the chitin biosynthesis pathway and one key gene related to lipid catabolism. The expression levels of two genes associated with lipid biosynthesis were upregulated. These results strongly suggest that HvTPS is essential for the normal growth and development of H. vitessoides and provide a reference for further studies of the utility of key genes involved in chitin and lipid biosynthesis for controlling insect development. John Wiley and Sons Inc. 2018-12-11 2020-04 /pmc/articles/PMC7379938/ /pubmed/30397994 http://dx.doi.org/10.1111/1744-7917.12650 Text en © 2018 The Authors. Insect Science published by John Wiley & Sons Australia, Ltd on behalf of Institute of Zoology, Chinese Academy of Sciences This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Articles
Chen, Jing‐Xiang
Lyu, Zi‐Hao
Wang, Chun‐Yan
Cheng, Jie
Lin, Tong
RNA interference of a trehalose‐6‐phosphate synthase gene reveals its roles in the biosynthesis of chitin and lipids in Heortia vitessoides (Lepidoptera: Crambidae)
title RNA interference of a trehalose‐6‐phosphate synthase gene reveals its roles in the biosynthesis of chitin and lipids in Heortia vitessoides (Lepidoptera: Crambidae)
title_full RNA interference of a trehalose‐6‐phosphate synthase gene reveals its roles in the biosynthesis of chitin and lipids in Heortia vitessoides (Lepidoptera: Crambidae)
title_fullStr RNA interference of a trehalose‐6‐phosphate synthase gene reveals its roles in the biosynthesis of chitin and lipids in Heortia vitessoides (Lepidoptera: Crambidae)
title_full_unstemmed RNA interference of a trehalose‐6‐phosphate synthase gene reveals its roles in the biosynthesis of chitin and lipids in Heortia vitessoides (Lepidoptera: Crambidae)
title_short RNA interference of a trehalose‐6‐phosphate synthase gene reveals its roles in the biosynthesis of chitin and lipids in Heortia vitessoides (Lepidoptera: Crambidae)
title_sort rna interference of a trehalose‐6‐phosphate synthase gene reveals its roles in the biosynthesis of chitin and lipids in heortia vitessoides (lepidoptera: crambidae)
topic Original Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7379938/
https://www.ncbi.nlm.nih.gov/pubmed/30397994
http://dx.doi.org/10.1111/1744-7917.12650
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