02563nas a2200241 4500008004100000022001400041245012300055210006900178260009500247300001200342490000800354520164900362653001802011653001402029653002102043653001602064653002802080653001402108100002202122700002502144700002402169856012802193 2012 eng d a0006-291X00aTrehalose as an indicator of desiccation stress in Drosophila melanogaster larvae: a potential marker of anhydrobiosis0 aTrehalose as an indicator of desiccation stress in Drosophila me a525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USAbACADEMIC PRESS INC ELSEVIER SCIENCEcMAR a638-6420 v4193 a

In the current scenario of global climate change, desiccation is considered as one of the major environmental stressors for the biota exposed to altered levels of ambient temperature and humidity. Drosophila melanogaster, a cosmopolitan terrestrial insect has been chosen as a humidity-sensitive bioindicator model for the present study since its habitat undergoes frequent stochastic and/or seasonally aggravated dehydration regimes. We report here for the first time the occurrence of anhydrobiosis in D. melanogaster larvae by subjecting them to desiccation stress under laboratory conditions. Larvae desiccated for ten hours at <5% relative humidity could enter anhydrobiosis and could revive upon rehydration followed by resumption of active metabolism. As revealed by FIR and HPLC analyzes, our findings strongly indicated the synthesis and accumulation of trehalose in the desiccating larvae. Biochemical measurements pointed out the desiccation-responsive trehalose metabolic pathway that was found to be coordinated in concert with the enzymes trehalose 6-phosphate synthase and trehalase. Further, an inhibitor-based experimental approach using deoxynojirimycin, a specific trehalase inhibitor, demonstrated the pivotal role of trehalose in larval anhydrobiosis of D. melanogaster. We therefore propose trehalose as a potential marker for the assessment of anhydrobiosis in Drosophila. The present findings thus add to the growing list of novel biochemical markers in specific bioindicator organisms for fulfilling the urgent need of environmental biomonitoring of climate change. (C) 2012 Elsevier Inc. All rights reserved.

10aAnhydrobiosis10abiomarker10aDeoxynojirimycin10aDesiccation10aDrosophila melanogaster10atrehalose1 aThorat, Leena, J.1 aGaikwad, Sushama, M.1 aNath, Bimalendu, B. uhttps://library.ncl.res.in/content/trehalose-indicator-desiccation-stress-drosophila-melanogaster-larvae-potential-marker-202108nas a2200241 4500008004100000022001400041245007600055210006900131260008100200300001200281490000700293520126000300653002801560653002601588653002401614653001401638653001401652100001701666700002201683700002401705700002501729856011201754 2015 eng d a0959-665800aInsect trehalase: physiological significance and potential applications0 aInsect trehalase physiological significance and potential applic aJOURNALS DEPT, 2001 EVANS RD, CARY, NC 27513 USAbOXFORD UNIV PRESS INCcAPR a357-3670 v253 a

Trehalose, a non-reducing disaccharide, is widespread throughout the biological world. It is the major blood sugar in insects playing a crucial role as an instant source of energy and in dealing with abiotic stresses. The hydrolysis of trehalose is under the enzymatic control of trehalase. The enzyme trehalase is gaining interest in insect physiology as it regulates energy metabolism and glucose generation via trehalose catabolism. The two forms of insect trehalase namely, Tre-1 and Tre-2, are important in energy supply, growth, metamorphosis, stress recovery, chitin synthesis and insect flight. Insect trehalase has not been reviewed in depth and the information available is quite scattered. The present mini review discusses our recent understanding of the regulation, mechanism and biochemical characterization of insect trehalase with respect to its physiological role in vital life functions. We also highlight the molecular and biochemical properties of insect trehalase that makes it amenable to competitive inhibition by most glycosidase inhibitors. Due to its crucial role in carbon metabolism in insects, application of inhibitors against trehalose can form a promising area towards formulating strategies for insect pest control.

10acarbohydrate metabolism10aglycosidase inhibitor10aglycoside hydrolase10atrehalase10atrehalose1 aShukla, Ekta1 aThorat, Leena, J.1 aNath, Bimalendu, B.1 aGaikwad, Sushama, M. uhttps://library.ncl.res.in/content/insect-trehalase-physiological-significance-and-potential-applications-002644nas a2200277 4500008004100000022001400041245011100055210006900166260000800235300000800243490000600251520174300257653002102000653002302021653001102044653002402055653001402079100001702093700001802110700002202128700002002150700002102170700002402191700002502215856012602240 2018 eng d a2190-572X00aCloning and characterization of trehalase: a conserved glycosidase from oriental midge, Chironomus ramosus0 aCloning and characterization of trehalase a conserved glycosidas cAUG a3520 v83 a

Insect trehalase is a multiferous enzyme, crucial for normal physiological functions as well as under stress conditions. In this report, we present a fundamental study of the trehalase gene segment (1587 bp) from Chironomus ramosus (CrTre) encoding for 529 amino acids, using appropriate bioinformatics tools. C. ramosus, a tropical midge is an emerging animal model to investigate the consequences of environmental stresses. We observed that CrTre belongs to GH family 37 in the CAZy database and possess 57-92% identity to dipteran trehalases. In silico characterization provided information regarding the structural, functional and evolutionary aspects of midge trehalase. In the phylogenetic tree, CrTre clustered with the soluble dipteran trehalases. Moreover, domain functional characterization of the deduced protein sequence by InterProScan (IPR001661), ProSite (PS00927 and PS00928) and Pfam (PF01204) indicated presence of highly conserved signature motifs which are important for the identification of trehalase superfamily. Furthermore, the instability index of CrTre was predicted to be < 40 suggesting its in vivo stability while, the high aliphatic index indicated towards its thermal stability (index value 71-81). The modelled 3D tertiary structure of CrTre depicts a (alpha/alpha)(6) barrel toroidal core. The catalytic domain of the enzyme comprised Glu424 and Asp226 as the putative active site residues. Interestingly, the conserved motifs were observed to be formed by the flexible loopy regions in the tertiary structure. This study revealed essential sequence features of the midge trehalase and offers better insights into the structural aspects of this enzyme which can be correlated with its function.

10aConserved motifs10aHomology modelling10aMidges10aSecondary structure10atrehalose1 aShukla, Ekta1 aThorat, Leena1 aBendre, Ameya, D.1 aJadhav, Santosh1 aPal, Jayanta, K.1 aNath, Bimalendu, B.1 aGaikwad, Sushama, M. uhttps://library.ncl.res.in/content/cloning-and-characterization-trehalase-conserved-glycosidase-oriental-midge-chironomus01646nas a2200229 4500008004100000022001400041245010700055210006900162260000800231300001400239490000700253520085700260653001901117653002101136653001901157653002701176653001401203100002201217700002401239700002301263856013001286 2020 eng d a1433-785100aCrystal-to-crystal synthesis of helically ordered polymers of trehalose by topochemical polymerization0 aCrystaltocrystal synthesis of helically ordered polymers of treh cFEB a2897-29030 v593 a

The synthesis of crystalline helical polymers of trehalose via topochemical azide-alkyne cycloaddition (TAAC) of a trehalose-based monomer is presented. An unsymmetrical trehalose derivative having azide and alkyne crystallizes in two different forms having almost similar packing. Upon heating, both the crystals undergo TAAC reaction to form crystalline polymers. Powder X-ray diffraction (PXRD) studies revealed that the monomers in both the crystals polymerize in a crystal-to-crystal fashion; circular dichroism (CD) studies of the product crystals revealed that the formed polymer is helically ordered. This solvent-free, catalyst-free polymerization method that eliminates the tedious purification of the polymeric product exemplifies the advantage of topochemical polymerization reaction over traditional solution-phase polymerization.

10aClick reaction10ahelical polymers10apolysaccharide10atopochemical reactions10atrehalose1 aHema, Kuntrapakam1 aGonnade, Rajesh, G.1 aSureshan, Kana, M. uhttps://library.ncl.res.in/content/crystal-crystal-synthesis-helically-ordered-polymers-trehalose-topochemical-polymerization02281nas a2200265 4500008004100000022001400041245014600055210006900201260000800270300001100278490000800289520143600297653002101733653001201754653001601766653001301782653001901795653001401814100002301828700002701851700002501878700002001903700002001923856007201943 2022 eng d a0168-945200aDietary influence on modulation of Helicoverpa armigera oral secretion composition leading to differential regulation of tomato plant defense0 aDietary influence on modulation of Helicoverpa armigera oral sec cJAN a1111200 v3143 aLittle is known about how different plant-based diets influence the insect herbivores’ oral secretion (OS) composition and eventually the plant defense responses. We analyzed the OS composition of the generalist Lepidopteran insect, Helicoverpa armigera feeding on the host plant tomato (OSH), non-host plant capsicum (OSNH), and artificial diet (OSAD) using Liquid Chromatography-Quadrupole Time of Flight Mass Spectrometry. Higher numbers and levels of alkaloids and terpenoids were observed in OSH and OSNH, respectively while OSAD was rich in phospholipids. Interestingly, treatment of H. armigera OSAD, OSH and OSNH on wounded tomato leaves showed differential expression of (i) genes involved in JA and SA biosynthesis and their responsive genes, and (ii) biosynthetic pathway genes of chlorogenic acid (CGA) and trehalose, which exhibited increased accumulation along with several other plant defensive metabolites. Specifically, high levels of CGA were detected after OSH and OSNH treatments in tomato leaves. There was higher expression of the genes involved in phenylpropanoid biosynthesis, which may lead to the increased accumulation of CGA and related metabolites. In the insect bioassay, CGA significantly inhibited H. armigera larval growth. Our results underline the differential accumulation of plant and insect OS metabolites and identified potential plant metabolite(s) affecting insect growth and development.10aChlorogenic acid10adefense10aMetabolites10aNon-host10aOral secretion10atrehalose1 aKallure, Gopal, S.1 aShinde, Balkrishna, A.1 aBarvkar, Vitthal, T.1 aKumari, Archana1 aGiri, Ashok, P. uhttps://www.sciencedirect.com/science/article/pii/S016894522100316202347nas a2200265 4500008004100000022001400041245014700055210006900202260000800271300001100279490000800290520144700298653002101745653001201766653001601778653001301794653001901807653001401826100002301840700002701863700002501890700002001915700002001935856012601955 2022 eng d a0168-945200aDietary influence on modulation of Helicoverpa armigera oral secretion composition leading to differential regulation of tomato plant defense.0 aDietary influence on modulation of Helicoverpa armigera oral sec cJAN a1111200 v3143 a

Little is known about how different plant-based diets influence the insect herbivores' oral secretion (OS) composition and eventually the plant defense responses. We analyzed the OS composition of the generalist Lepidopteran insect, Helicoverpa armigera feeding on the host plant tomato (OSH), non-host plant capsicum (OSNH), and artificial diet (OSAD) using Liquid Chromatography-Quadrupole Time of Flight Mass Spectrometry. Higher numbers and levels of alkaloids and terpenoids were observed in OSH and OSNH, respectively while OSAD was rich in phospholipids. Interestingly, treatment of H. armigera OSAD, OSH and OSNH on wounded tomato leaves showed differential expression of (i) genes involved in JA and SA biosynthesis and their responsive genes, and (ii) biosynthetic pathway genes of chlorogenic acid (CGA) and trehalose, which exhibited increased accumulation along with several other plant defensive metabolites. Specifically, high levels of CGA were detected after OSH and OSNH treatments in tomato leaves. There was higher expression of the genes involved in phenyl-propanoid biosynthesis, which may lead to the increased accumulation of CGA and related metabolites. In the insect bioassay, CGA significantly inhibited H. armigera larval growth. Our results underline the differential accumulation of plant and insect OS metabolites and identified potential plant metabolite(s) affecting insect growth and development.

10aChlorogenic acid10adefense10aMetabolites10aNon-host10aOral secretion10atrehalose1 aKallure, Gopal, S.1 aShinde, Balkrishna, A.1 aBarvkar, Vitthal, T.1 aKumari, Archana1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/dietary-influence-modulation-helicoverpa-armigera-oral-secretion-composition-leading-002364nas a2200229 4500008004100000022001400041245008700055210006900142260000900211300001200220490000700232520163500239653001201874653002301886653002501909653001101934653001401945100002601959700002401985700002202009856010302031 2023 eng d a0959-665800aRegulation of trehalose metabolism in insects: from genes to the metabolite window0 aRegulation of trehalose metabolism in insects from genes to the  cMAY  a262-2730 v333 a

Trehalose is a major circulatory sugar in the haemolymph of insects. It provides instant energy and protection against stress. Trehalose metabolism is associated with insect growth and development. The architecture and spatio-temporal expression dynamics of trehalose metabolism and transport genes are key for regulation. These genes are controlled by various transcription factors, largely linked to nutrition, insect development, and metamorphosis. Also, trehalose levels are affected by substrate affinities and modifications of enzymes involved in the pathway. A feedback mechanism involving the precursors and products can regulate trehalose metabolism. Further, the neuroendocrine system controls trehalose levels under normal and stressed conditions by producing different hormones. Hypotrehalosemic hormones work under surplus energy conditions to activate haemolymph trehalose uptake and degradation. In contrast, hypertrehalosemic hormones stimulate trehalose production in the fat body and its transport to the haemolymph. However, trehalose metabolism regulation in insects needs to be studied in detail. This review discusses aspects of trehalose synthesis, transport, and degradation dynamics in developmental transition and stress response. Unraveling the epigenetic factors, transcriptional control and chemical or genetic modulators can provide further insights into the intricate regulation of trehalose in a development- and tissue-specific manner. This molecular information about effectors and regulators of trehalose metabolism can be applied in developing diverse biotechnological applications.

10aHormone10aInsect development10aMetabolic regulation10aStress10atrehalose1 aTellis, Meenakshi, B.1 aKotkar, Hemlata, M.1 aJoshi, Rakesh, S. uhttps://library.ncl.res.in/content/regulation-trehalose-metabolism-insects-genes-metabolite-window02593nas a2200277 4500008004100000022001400041245012100055210006900176260000800245300001100253490000800264520165000272653002001922653002501942653001101967653002101978653001401999100002602013700003002039700002602069700002202095700002502117700002402142700002202166856012702188 2023 eng d a0378-111900aTrehalose transporter-like gene diversity and dynamics enhances stress response and recovery in Helicoverpa armigera0 aTrehalose transporterlike gene diversity and dynamics enhances s cAPR a1472590 v8623 a

Trehalose is a primary sugar and its distribution across the insect body, regulated by trehalose transporters (TRETs), is essential for sugar metabolism and energy homeostasis. The large diversity of Tret-like sugar trans-porters (ST), belonging to SLC2A transporter family, in polyphagous insects probably contributes to their extremely adaptive nature. We aim to study spatio-temporal expression dynamics and functional relevance of ST transcript variants in the lepidopteran model organism, Helicoverpa armigera. Identification of 69 putative Tret-like HaST transcript variants from databases and their digital gene expression analysis indicated tissue and development-specific expression patterns. Phylogenetic and sequence similarity network analysis of HaSTs signify evolutionary divergence, while motif and structure analysis depicted conserved signatures. In vitro gene expression validation for selected genes depicts that HaST09 and 69 are fat body and haemolymph-specific. While, HaST06, 30, 36 and 57 are developmental stage or sex-specific. HaST69 has high expression in the haemolymph of fifth instar larvae. In the presence of trehalose metabolism inhibitors and abiotic stress, HaSTs expression show dysregulation, indicating their possible association with trehalose metabolism and stress re-covery. In vivo gene silencing of HaST69 resulted in reduced trehalose accumulation in the insect body, sug-gesting its plausible role in sugar metabolism. The overall understanding of HaST diversity and expression dynamics highlights their putative roles in sugar transport during adaptation and stress recovery of insects.

10aGene expression10aHelicoverpa armigera10aStress10aTransporter-like10atrehalose1 aTellis, Meenakshi, B.1 aChaudhari, Bhagyashri, Y.1 aDeshpande, Shweta, V.1 aNikam, Sanika, V.1 aBarvkar, Vitthal, T.1 aKotkar, Hemlata, M.1 aJoshi, Rakesh, S. uhttps://library.ncl.res.in/content/trehalose-transporter-gene-diversity-and-dynamics-enhances-stress-response-and-recovery02668nas a2200253 4500008004100000022001400041245007600055210006900131260000800200490000600208520183100214653001602045653002602061653001402087653003802101100002602139700002402165700002602189700003002215700001802245700002402263700002202287856010502309 2024 eng d a2701-019800aInhibition of trehalose synthesis in lepidoptera reduces larval fitness0 aInhibition of trehalose synthesis in lepidoptera reduces larval  cFEB0 v83 a

Trehalose is synthesized in insects through the trehalose 6-phosphate synthase and phosphatase (TPS/TPP) pathway. TPP dephosphorylates trehalose 6-phosphate to release trehalose. Trehalose is involved in metamorphosis, but its relation with body weight, size, and developmental timing is unexplored. The expression and activity of TPS/TPP fluctuate depending on trehalose demand. Thus, TPS/TPP inhibition can highlight the significance of trehalose in insect physiology. TPS/TPP transcript levels are elevated in the pre-pupal and pupal stages in Helicoverpa armigera. The inhibition of recombinantly expressed TPP by N-(phenylthio)phthalimide (NPP), is validated by in vitro assays. In vivo inhibition of trehalose synthesis reduces larval weight and size, hampers metamorphosis, and reduces its overall fitness. Insufficient trehalose leads to a shift in glucose flux, reduced energy, and dysregulated fatty acid oxidation. Metabolomics reaffirms the depletion of trehalose, glucose, glucose 6-phosphate, and suppressed tricarboxylic acid cycle. Reduced trehalose hampers the energy level affecting larval vitality. Through trehalose synthesis inhibition, the importance of trehalose in insect physiology and development is investigated. Also, in two other lepidopterans, TPP inhibition impedes physiology and survival. NPP is also found to be effective as an insecticidal formulation. Overall, trehalose levels affect the larval size, weight, and metabolic homeostasis for larval-pupal transition in lepidoptera. Inhibition of trehalose synthesis enzyme TPS/TPP is a good model to study the contribution of trehalose in attaining body weight and in larval-pupal transition. Transcriptomics and metabolomics studies reveal overall reduced energy and dysregulated glucose, protein, and fatty acid metabolism.image

10aLepidoptera10ametabolic homeostasis10atrehalose10atrehalose 6-phosphate phosphatase1 aTellis, Meenakshi, B.1 aMohite, Sharada, D.1 aNair, Vineetkumar, S.1 aChaudhari, Bhagyashri, Y.1 aAhmed, Shadab1 aKotkar, Hemlata, M.1 aJoshi, Rakesh, S. uhttps://library.ncl.res.in/content/inhibition-trehalose-synthesis-lepidoptera-reduces-larval-fitness02341nas a2200253 4500008004100000022001400041245012000055210006900175260000800244300001200252490000700264520149400271653000801765653002501773653001501798653001701813653001701830653001401847100003001861700002301891700002501914700002201939856012601961 2026 eng d a2160-183600aMechanistic insights in the role of trehalose transporter in metabolic homeostasis in response to dietary trehalose0 aMechanistic insights in the role of trehalose transporter in met cFEB ajkaf3030 v163 a

Trehalose is the major sugar in insect hemolymph and plays a diverse role. Its level is regulated by the dynamics of biosynthesis and distribution by sugar transporters. The metabolic balance between trehalose synthesis and uptake remains poorly understood, despite its critical role in homeostasis. Here, we examined the role of the putative gut-specific sugar transporter, HaST46, in regulating trehalose levels in Helicoverpa armigera, a model Lepidopteran pest. Analysis of publicly available transcriptomics, proteomics data, and qRT-PCR study suggests that HaST46 showed localization in the posterior midgut and its expression alters in response to dietary contents. The liquid chromatography-mass spectrometry (LC-MS) analysis of HaST46 overexpressing Sf9 cells indicated that trehalose transport is preferred over glucose. HaST46 expression was found to be modulated tissue-specific manner in response to dietary trehalose availability. Furthermore, trehalose synthesis genes were found to be downregulated in the case of a 50 mM trehalose diet. This suggests that a potential increase in exogenous trehalose uptake may attenuate its endogenous synthesis. HaST46 overexpression and silencing lead to altered trehalose levels in the insect, while also having impact on trehalose metabolizing enzymes. Overall, our findings reveal the role of gut predominant sugar transporter, HaST46, in metabolic fine-tuning between exogenous trehalose uptake and endogenous synthesis.

10agut10aHelicoverpa armigera10aMetabolism10asugar uptake10atransporters10atrehalose1 aChaudhari, Bhagyashri, Y.1 aNichit, Vikram, J.1 aBarvkar, Vitthal, T.1 aJoshi, Rakesh, S. uhttps://library.ncl.res.in/content/mechanistic-insights-role-trehalose-transporter-metabolic-homeostasis-response-dietary