Characterization of the cDNA Encoding Membrane-Bound Trehalase, its Expression and Enzyme Activity in<i>Bactrocera dorsalis</i>(Diptera: Tephritidae)

Xie, Yifei; Yang, Wen‐Jia; Dou, Wei; Wang, Jinjun

doi:10.1653/024.096.0401

Cited by 14 publications

(18 citation statements)

References 34 publications

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“…The trehalase content in the different organs of H. armigera was measured, and the enzyme was found primarily in the midgut, which was consistent with that in other insects (Tan et al, ; Xie, Yang, Dou, & Wang, ). According to the alternation of the three carbohydrates and the related enzymes, all of the three β‐glucosides can inhibit trehalase, and it can also be proven that santonin was the most effective inhibitor in H. armigera .…”

Section: Discussionsupporting

confidence: 81%

Effects of toxic β‐glucosides on carbohydrate metabolism in cotton bollworm, Helicoverpa armigera (Hübner)

Lin

et al. 2019

Arch Insect Biochem Physiol

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The purpose of this study was to evaluate the effects of three toxic β-glucosides, phlorizin, santonin, and amygdalin, on carbohydrate metabolism in the cotton bollworm, Helicoverpa armigera (Hübner), when diets mixed with β-glucosides were fed to third-instar larvae. The growth of the larvae was significantly inhibited by exposure to santonin after 96 hr but not obviously affected by phlorizin and amygdalin. The midgut trehalase activities were only 51.7%, 32%, and 42.5% of that of the control after treatment with phlorizin, santonin and amygdalin at 2 mg/ml, respectively. In the hemolymph and fat body, the amount of trehalose decreased in all cases. However, the effects of santonin on the alteration of the glycogen and glucose levels as well as the activities of glycogen phosphorylase, were different than those of the other two β-glucosides. It appears that the three β-glucosides have different influences on the carbohydrate metabolism of cotton bollworm. K E Y W O R D Scarbohydrate metabolism, cotton bollworm, trehalase, β-glucosides

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Section: Discussionsupporting

confidence: 81%

Effects of toxic β‐glucosides on carbohydrate metabolism in cotton bollworm, Helicoverpa armigera (Hübner)

Lin

et al. 2019

Arch Insect Biochem Physiol

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“…This pest can inflict severe damage across a range of economically important tropical and subtropical fruit plants, including guava (Psidium guajava), mango (Mangifera indica), and citrus (Citrus grandis) (Steiner et al, 1965;Jin et al, 2011;Jayanthi et al, 2012). Unfortunately, highly insecticide-resistant populations have emerged in both China and Pakistan (Jin et al, 2011;Xie et al, 2013;Khan and Akram, 2018), which reduces pesticide efficiency in controlling this agricultural pest. As such, there is an urgent need to find an alternative, and more environmentally friendly method for control, perhaps including mass trapping using semiochemicals.…”

Section: Introductionmentioning

confidence: 99%

An Antennae-Specific Odorant-Binding Protein Is Involved in Bactrocera dorsalis Olfaction

Zhao

Liang

et al. 2020

Front. Ecol. Evol.

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Insect antennae are important olfactory organs that house high concentrations of odorant-binding proteins (OBPs) in the sensillum lymph. Previous studies in other insects have shown that OBPs play important roles in transporting odorants and enhancing the sensitivity of the olfactory system. However, the functions of OBPs in the oriental fruit fly, Bactrocera dorsalis, especially those specifically expressed in antennae, have not been fully elucidated. In this study, cDNA libraries were constructed from both the male and female antennal transcriptome, and twenty OBPs were identified in total. The expression profiles of these OBPs were examined in the adult antenna, head, thorax, leg, and abdomen of both sexes. Seven of the identified OBP genes had significantly higher expression in both the male and female antennae than in other tissues, while the transcript levels of the remaining OBPs varied across different tissues. Regarding the function of antenna-specific OBPs, we targeted Bdorsobp2 as a representative for further RNA interference (RNAi) and identified via electrophysiology a decrease in detection of a potential species-specific a potent attractant, methyl eugenol. Moreover, subsequent behavioral assay data showed that the behavioral response of B. dorsalis toward this odorant decreased when Bdorobp2 was silenced with injection of double-stranded RNA (dsRNA). Combined, these results support our initial hypothesis that antennae-specific OBPs are of critical importance for insect odorant detection, sensitivity, and behavior.

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“…Soluble trehalase (Tre 1) acts within cells, whereas membrane-bound trehalase (Tre 2) hydrolyses hemolymph trehalose and supplies glucose to cells (Mitsumasu et al 2005 ). Trehalase has been isolated from many insect species which possessed both forms of the enzyme (Tang et al 2008 ; Tatun et al 2008 ; Gu et al 2009 ; Xie et al 2013 ). Similar observations have been made in the honeybee (Lefebvre and Huber 1970 ; Lee et al 2007 ; Mori et al 2009 ).…”

Section: Discussionmentioning

confidence: 99%

“…In A. mellifera and other insects (Tang et al 2008 ; Tatun et al 2008 ; Gu et al 2009 ; Xie et al 2013 ), this enzyme occurs in two forms as soluble trehalase and membrane-bound trehalase (Lefebvre and Huber 1970 ; Lee et al 2007 ). In insects, differences in the expression of genes encoding both trehalases are determined by sex, developmental stage and tissue (Tang et al 2008 ; Tatun et al 2008 ; Xie et al 2013 ). The relevant differences have not been studied in bees.…”

Section: Introductionmentioning

confidence: 99%

Developmental changes in gene expression and enzyme activities of anabolic and catabolic enzymes for storage carbohydrates in the honeybee, Apis mellifera

et al. 2018

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Glycogen and trehalose are important sources of energy in insects. The expression of genes encoding the key metabolic enzymes—glycogen synthase (GS), glycogen phosphorylase (GP), trehalose-6-phosphate synthase (TPS-1), soluble trehalase (Tre-1) and membrane-bound trehalase (Tre-2)—was analyzed in 12 developmental stages of Apis mellifera worker brood. The content of GS and GP proteins, TPS activity, total trehalase activity, and the activity of Tre-1 and Tre-2 were determined. Transcript quantity was not always correlated with the content of the encoded GS or GP protein. The correlation was higher for GS (r = 0.797) than GP (r = 0.651). The expression of the glycogen synthase gene (gs) and the glycogen phosphorylase gene (gp) was high in 4- and 7-day-old larvae and in pupae, excluding the last pupal stage. The expression of the tps-1 gene was highest in the mid-pupal stage and contributed to higher enzyme activity in that stage. The expression of the tre-1 gene was higher than the expression of the tre-2 gene throughout development. In newly hatched workers, the expression of genes encoding catabolic enzymes of both carbohydrates, gp and tre-1, was higher than the expression of genes encoding anabolic enzymes. The results of this study suggest that sugar metabolism genes have somewhat different control mechanisms during larval development and metamorphosis.Electronic supplementary materialThe online version of this article (10.1007/s00040-018-0648-1) contains supplementary material, which is available to authorized users.

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Characterization of the cDNA Encoding Membrane-Bound Trehalase, its Expression and Enzyme Activity inBactrocera dorsalis(Diptera: Tephritidae)

Abstract: BioOne Complete (complete.BioOne.org) is a full-text database of 200 subscribed and open-access titles in the biological, ecological, and environmental sciences published by nonprofit societies, associations, museums, institutions, and presses.

Cited by 14 publications

References 34 publications

Effects of toxic β‐glucosides on carbohydrate metabolism in cotton bollworm, Helicoverpa armigera (Hübner)

Effects of toxic β‐glucosides on carbohydrate metabolism in cotton bollworm, Helicoverpa armigera (Hübner)

An Antennae-Specific Odorant-Binding Protein Is Involved in Bactrocera dorsalis Olfaction

Developmental changes in gene expression and enzyme activities of anabolic and catabolic enzymes for storage carbohydrates in the honeybee, Apis mellifera

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