Molecular cloning and expression analysis of soluble and membrane-bound trehalase genes in the cotton bollworm, Helicoverpa armigera

Ma, Ling; Dai, Wu; Li, Xianchun; Zhang, Yalin; Zhang, Chenyu

doi:10.1016/j.aspen.2015.01.002

Cited by 11 publications

(8 citation statements)

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“…Trehalase (EC 3.2.1.28) is an important enzyme that catalyzes the hydrolysis of one trehalose molecule into two glucose molecules. There are two forms of trehalase, soluble trehalase (Tre1) and membrane-bound trehalase (Tre2), which have been identified and cloned in many insect species, including Tribolium castaneum (Coleoptera: Tenebrionidae) [ 10 ], Bombyx mori (Lepidoptera: Bombycidae) [ 11 ], Aphis glycines (Homoptera: Aphididae) [ 12 ], Spodoptera exigua (Lepidoptera: Noctuidae) [ 13 ], and Helicoverpa armigera (Lepidoptera: Noctuidae) [ 14 ]. Moreover, the two trehalase genes show obvious tissue specificity in insects.…”

Section: Introductionmentioning

confidence: 99%

Characterization and Functional Analysis of trehalase Related to Chitin Metabolism in Glyphodes pyloalis Walker (Lepidoptera: Pyralidae)

Shao

Ding

Jiang

et al. 2021

Insects

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Glyphodes pyloalis Walker (G. pyloalis) is a serious pest on mulberry. Due to the increasing pesticide resistance, the development of new and effective environmental methods to control G. pyloalis is needed. Trehalase is an essential enzyme in trehalose hydrolysis and energy supply, and it has been considered a promising target for insect pest control. However, the specific function of trehalase in G. pyloalis has not been reported. In this study, two trehalase genes (GpTre1 and GpTre2) were identified from our previous transcriptome database. The functions of the trehalase in chitin metabolism were studied by injecting larvae with dsRNAs and trehalase inhibitor, Validamycin A. The open reading frames (ORFs) of GpTre1 and GpTre2 were 1,704 bp and 1,869 bp, which encoded 567 and 622 amino acid residues, respectively. Both of GpTre1 and GpTre2 were mainly expressed in the head and midgut. The highest expression levels of them were in 5th instar during different development stages. Moreover, knockdown both of GpTre1 and GpTre2 by the dsRNAs led to significantly decreased expression of chitin metabolism pathway-related genes, including GpCHSA, GpCDA1, GpCDA2, GpCHT3a, GpCHT7, GpCHSB, GpCHT-h, GpCHT3b, GpPAGM, and GpUAP, and abnormal phenotypes. Furthermore, the trehalase inhibitor, Validamycin A, treatment increased the expressions of GpTre1 and GpTre2, increased content of trehalose, and decreased the levels of glycogen and glucose. Additionally, the inhibitor caused a significantly increased cumulative mortality of G. pyloalis larvae on the 2nd (16%) to 6th (41.3%) day, and decreased the rate of cumulative pupation (72.3%) compared with the control group (95.6%). After the activities of trehalase were suppressed, the expressions of 6 integument chitin metabolism-related genes decreased significantly at 24 h and increased at 48 h. The expressions of GpCHSB and GpCHT-h, involved in chitin metabolism pathway of peritrophic membrane in the midgut, increased at 24 h and 48 h, and there were no changes to GpCHT3b and GpPAGM. These results reveal that GpTre1 and GpTre2 play an essential role in the growth of G. pyloalis by affecting chitin metabolism, and this provides useful information for insect pest control in the future.

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Section: Introductionmentioning

confidence: 99%

Characterization and Functional Analysis of trehalase Related to Chitin Metabolism in Glyphodes pyloalis Walker (Lepidoptera: Pyralidae)

Shao

Ding

Jiang

et al. 2021

Insects

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“…Trehalase hydrolyzes the α-1, 1-glycosidic linkage of trehalose to release two glucose molecules (Shukla et al, 2015; Łopieńska-Biernat et al, 2019). Trehalase was discovered in Aspergillus niger in 1893 and was classified into two types, namely, soluble trehalase (TRE1) and membrane-bound trehalase (TRE2) (Forcella et al, 2010; Ma et al, 2015). It has been identified in several insect species, such as Apis mellifera (Lee et al, 2007), Aphis glycines (Bansal et al, 2013), Spodoptera exigua (Tang et al, 2008; Zou et al, 2013), Tribolium castaneum (Parkinson et al, 2003; Tang et al, 2016), Nilaparvata lugens (Zhao et al, 2016), and Chironomus ramosus (Shukla et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

Evaluation of the Expression and Function of the TRE2-like and TRE2 Genes in Ecdysis of Harmonia axyridis

Chen²,

Wang

et al. 2019

Front. Physiol.

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Harmonia axyridis is an important predatory insect and widely used in biological control of agricultural and forestry pests. Trehalose is directly involved in the energy storage of the H. axyridis and in the oxidative function of various physiological activities thereby providing an energy source for its growth and development. The aim of this study was to explore the potential function of membrane-bound-like trehalase (TRE2-like) and membrane-bound trehalase (TRE2) genes in H. axyridis by RNAi. In addition, the activity of soluble and membrane-bound trehalase and the expression of genes related to trehalose and glycogen metabolism were determined in the larvae injected with dsTRE2like or dsTRE2. The results showed that wing abnormality and mortality appeared in adults, as well as the activity of soluble trehalase and glycogen contents increased when interfering with TRE2-like gene. However, the activity of membrane-bound trehalase, trehalose and glucose contents in the larvae decreased. The expression of glycogen synthase (GS) and glycogen phosphorylase (GP) genes were decreased after RNAi in the ecdysis stage. The expression of chitin synthase gene A (CHSA), chitin synthase gene B (CHSB), and trehalose-6-phosphate synthase genes (TPS) were decreased significantly after RNAi, especially in the ecdysis stage. These results indicated that RNA interference is capable of knocking down gene expression of TRE2-like and TRE2, thereby disrupting trehalose metabolism which affects the chitin synthesis pathway in turn and also leads to developmental defects, such as wing deformities. This study could provide some theoretical guidance for the function of TRE2 gene in other insects.

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“…Treh2 possesses a transmembrane domain and is usually larger, whereas Treh1 lacks a transmembrane domain (Shukla et al 2015). Treh1 is a cytosolic enzyme that hydrolyses endogenous trehalose, whereas Treh2 is an extracellular enzyme (Ma et al 2015). Treh2 is believed to face the blood side, degrading the extracellular trehalose (Mitsumasu et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Three novel trehalase genes from Harmonia axyridis (Coleoptera: Coccinellidae): cloning and regulation in response to rapid cold and re-warming

et al. 2019

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Trehalose is the main blood sugar in insects. To study the function of trehalase during exposure to low temperatures, three other novel cDNAs of trehalase were cloned from Harmonia axyridis by transcriptome sequencing and rapid amplification of cDNA ends. One of the cloned cDNAs encoded a soluble trehalase, the second trehalase cDNA encoded a transmembrane-like domain, and the third cDNA encoded a membrane-bound protein. Therefore, these cDNAs were, respectively, named HaTreh1 - 5 , HaTreh2 - like , and HaTreh2 . HaTreh1 - 5 , HaTreh2 - like , and HaTreh2 cDNAs encoded proteins containing 586, 553, and 633 amino acids with predicted masses of approximately 69.47, 63.46, and 73.66 kDa, and pIs of 9.20, 5.52, and 6.31, respectively. All three novel trehalases contained signal motifs “PGGINKESYYLDSY”, “QWDYPNAWPP”, and a highly conserved glycine-rich (GGGGEY) region. The expression levels of HaTreh1 - 5 and HaTreh2 mRNAs were high during adult stages, whereas HaTreh2 - like was expressed in low amounts in the fourth larval stage. The results showed that the activity of membrane-bound trehalases decreased from 25 to 10 °C and from 5 to − 5 °C during cooling. The results also revealed a decreasing trend in expression of the three HaTreh mRNAs during the cooling treatment, and an initial decrease followed by an increase during the process of re-warming. Electronic supplementary material The online version of this article (10.1007/s13205-019-1839-9) contains supplementary material, which is available to authorized users.

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Molecular cloning and expression analysis of soluble and membrane-bound trehalase genes in the cotton bollworm, Helicoverpa armigera

Cited by 11 publications

References 35 publications

Characterization and Functional Analysis of trehalase Related to Chitin Metabolism in Glyphodes pyloalis Walker (Lepidoptera: Pyralidae)

Characterization and Functional Analysis of trehalase Related to Chitin Metabolism in Glyphodes pyloalis Walker (Lepidoptera: Pyralidae)

Evaluation of the Expression and Function of the TRE2-like and TRE2 Genes in Ecdysis of Harmonia axyridis

Three novel trehalase genes from Harmonia axyridis (Coleoptera: Coccinellidae): cloning and regulation in response to rapid cold and re-warming

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