02009nas a2200253   4500008004100000022001400041245007800055210006900133260006700202300001200269490000700281520116500288653001501453653001701468653002501485653001401510653001201524100002401536700002001560700002201580700002101602700002001623856011201643       2013                        eng d  a0962-107500aDifferential protease activity augments polyphagy in helicoverpa armigera0 aDifferential protease activity augments polyphagy in helicoverpa  a111 RIVER ST, HOBOKEN 07030-5774, NJ USAbWILEY-BLACKWELLcJUN  a258-2720 v223 a<p>Helicoverpa armigera (Lepidoptera: Noctuidae) and other polyphagous agricultural pests are extending their plant host range and emerging as serious agents in restraining crop productivity. Dynamic regulation, coupled with a diversity of digestive and detoxifying enzymes, play a crucial role in the adaptation of polyphagous insects. To investigate the functional intricacy of serine proteases in the development and polyphagy of H.armigera, we profiled the expression of eight trypsin-like and four chymotrypsin-like phylogenetically diverse mRNAs from different life stages of H.armigera reared on nutritionally distinct host plants. These analyses revealed diet- and stage-specific protease expression patterns. The trypsins expressed showed structural variations, which might result in differential substrate specificity and interaction with inhibitors. Protease profiles in the presence of inhibitors and their mass spectrometric analyses revealed insight into their differential activity. These findings emphasize the differential expression of serine proteases and their consequences for digestive physiology in promoting polyphagy in H.armigera.</p>10aadaptation10achymotrypsin10aHelicoverpa armigera10apolyphagy10aTrypsin1 aChikate, Yojana, R.1 aTamhane, V., A.1 aJoshi, Rakesh, S.1 aGupta, Vidya, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/differential-protease-activity-augments-polyphagy-helicoverpa-armigera-002205nas a2200229   4500008004100000022001400041245014400055210006900199260010600268300001000374490000800384520127700392653002001669653002501689653002901714653001401743653002601757100002201783700002101805700002001826856012901846       2014                        eng d  a0031-942200aDifferential antibiosis against helicoverpa armigera exerted by distinct inhibitory repeat domains of capsicum annuum proteinase inhibitors0 aDifferential antibiosis against helicoverpa armigera exerted by   aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcMAY  a16-220 v1013 a<p>Plant defensive serine proteinase inhibitors (Pis) are known to have negative impact on digestive physiology of herbivore insects and thus have a crucial role in plant protection. Here, we have assessed the efficacy and specificity of three previously characterized inhibitory repeat domain (IRD) variants from Capsicum annuum PIs viz., IRD-7, -9 and -12 against gut proteinases from Helicoverpa armigera. Comparative study of in silico binding energy revealed that IRD-9 possesses higher affinity towards H. armigera serine proteinases as compared to IRD-7 and -12. H. armigera fed on artificial diet containing 5 TIU/g of recombinant IRD proteins exhibited differential effects on larval growth, survival rate and other nutritional parameters. Major digestive gut trypsin and chymotrypsin genes were down regulated in the IRD fed larvae, while few of them were up-regulated, this indicate alterations in insect digestive physiology. The results corroborated with proteinase activity assays and zymography. These findings suggest that the sequence variations among Pis reflect in their efficacy against proteinases in vitro and in vivo, which also could be used for developing tailor-made multi-domain inhibitor gene(s). (C) 2014 Elsevier Ltd. All rights reserved.</p>10aCapsicum annuum10aHelicoverpa armigera10aInhibitory repeat domain10aProteases10aProteinase inhibitors1 aJoshi, Rakesh, S.1 aGupta, Vidya, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/differential-antibiosis-against-helicoverpa-armigera-exerted-distinct-inhibitory-repeat-002993nas a2200289   4500008004100000022001400041245017700055210006900232260008600301300001000387490000700397520189300404653002002297653002502317653001402342653002502356100002202381700001902403700002802422700001902450700002402469700001902493700002002512700002102532700002002553856013002573       2014                        eng d  a0739-110200aRemarkable efficiency of a pin-II proteinase inhibitor sans two conserved disulfide bonds is due to enhanced flexibility and hydrogen bond density in the reactive site loop0 aRemarkable efficiency of a pinII proteinase inhibitor sans two c  a325 CHESTNUT ST, SUITE 800, PHILADELPHIA, PA 19106 USAbTAYLOR & FRANCIS INCcJAN  a13-260 v323 a<p>Capsicum annuum (L.) expresses diverse potato type II family proteinase inhibitors comprising of inhibitory repeat domain (IRD) as basic functional unit. Most IRDs contain eight conserved cysteines forming four disulfide bonds, which are indispensible for their stability and activity. We investigated the functional significance of evolutionary variations in IRDs and their role in mediating interaction between the inhibitor and cognate proteinase. Among the 18 IRDs encoded by C. annuum, IRD-7, -9, and -12 were selected for further characterization on the basis of variation in their reactive site loop, number of conserved cysteine residues, and higher theoretical G(bind) for interaction with Helicoverpa armigera trypsin. Moreover, inhibition kinetics showed that IRD-9, despite loss of some of the disulfide bonds, was a more potent proteinase inhibitor among the three selected IRDs. Molecular dynamic simulations revealed that serine residues in the place of cysteines at seventh and eighth positions of IRD-9 resulted in an increase in the density of intramolecular hydrogen bonds and reactive site loop flexibility. Results of the serine residues chemical modification also supported this observation and provided a possible explanation for the remarkable inhibitory potential of IRD-9. Furthermore, this natural variant among IRDs showed special attributes like stability to proteolysis and synergistic inhibitory effect on other IRDs. It is likely that IRDs have coevolved selective specialization of their structure and function as a response towards specific insect proteases they encountered. Understanding the molecular mechanism of pest protease-plant proteinaceous inhibitor interaction will help in developing effective pest control strategies.An animated interactive 3D complement (I3DC) is available in Proteopedia at http://proteopedia.org/w/Journal:JBSD:39</p>10aCapsicum annuum10aHelicoverpa armigera10aProteases10aProteinase inhibitor1 aJoshi, Rakesh, S.1 aMishra, Manasi1 aTamhane, Vaijayanti, A.1 aGhosh, Anirban1 aSonavane, Uddhavesh1 aSuresh, C., G.1 aJoshi, Rajendra1 aGupta, Vidya, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/remarkable-efficiency-pin-ii-proteinase-inhibitor-sans-two-conserved-disulfide-bonds-due-002128nas a2200289   4500008004100000022001400041245013100055210006900186260007100255300001600326490000700342520109100349653001701440653002501457653002601482653002301508100002201531700001701553700001501570700002201585700001701607700002301624700002201647700002101669700002001690856012801710       2014                        eng d  a0021-856100aWay toward ``dietary pesticides'': molecular investigation of insecticidal action of caffeic acid against helicoverpa armigera0 aWay toward dietary pesticides molecular investigation of insecti  a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcNOV  a10847-108540 v623 a<p>Bioprospecting of natural molecules is essential to overcome serious environmental issues and pesticide resistance in insects. Here we are reporting insights into insecticidal activity of a plant natural phenol. In silico and in vitro screening of multiple molecules supported by in vivo validations suggested that caffeic acid (CA) is a potent inhibitor of Helicoverpa armigera gut proteases. Protease activity and gene expression were altered in CA-fed larvae. The structure-activity relationship of CA highlighted that all the functional groups are crucial for inhibition of protease activity. Biophysical studies and molecular dynamic simulations revealed that sequential binding of multiple CA molecules induces conformational changes in the protease(s) and thus lead to a significant decline in their activity. CA treatment significantly inhibits the insect's detoxification enzymes, thus intensifying the insecticidal effect. Our findings suggest that CA can be implicated as a potent insecticidal molecule and explored for the development of effective dietary pesticides.</p>10aCaffeic acid10aHelicoverpa armigera10ainsecticidal activity10aprotease inhibitor1 aJoshi, Rakesh, S.1 aWagh, T., P.1 aSharma, N.1 aMulani, Fayaj, A.1 aSonavane, U.1 aThulasiram, H., V.1 aJoshi, Rakesh, S.1 aGupta, Vidya, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/way-toward-dietary-pesticides-molecular-investigation-insecticidal-action-caffeic-acid-002335nas a2200253   4500008004100000022001200041245015200053210006900205260000900274300001000283490000700293520141700300653002501717653001301742653002301755653003401778100002601812700002201838700002401860700002401884700002301908700002001931856013001951       2018                        eng d  a965174800aTripeptides derived from reactive centre loop of potato type II protease inhibitors preferentially inhibit midgut proteases of Helicoverpa armigera0 aTripeptides derived from reactive centre loop of potato type II   cAPR   a17-250 v953 a<p>Potato type II protease inhibitors (Pin-II PIs) impede the growth of lepidopteran insects by inhibiting serine protease-like enzymes in the larval gut. The three amino acid reactive centre loop (RCL) of these proteinaceous inhibitors is crucial for protease binding and is conserved across the Pin-II family. However, the molecular mechanism and inhibitory potential of the RCL tripeptides in isolation of the native protein has remained elusive. In this study, six peptides corresponding to the RCLs of the predominant Pin-II PIs were identified, synthesized and evaluated for in vitro and in vivo inhibitory activity against serine proteases of the polyphagous insect, Helicoverpa armigera. RCL peptides with sequences PRN, PRY and TRE were found to be potent inhibitors that adversely affected the growth and development of H. armigera. The binding mechanism and differential affinity of the RCL peptides with serine proteases was delineated by crystal structures of complexes of the RCL peptides with trypsin. Residues P1 and P2 of the inhibitors play a crucial role in the interaction and specificity of these inhibitors. Important features of RCL peptides like higher inhibition of insect proteases, enhanced efficacy at alkaline gut pH, longer retention and high stability in insect gut make them suitable molecules for the development of sustainable pest management strategies for crop protection.</p>10aHelicoverpa armigera10aProtease10aprotease inhibitor10aReactive centre loop peptides1 aSaikhedkar, Nidhi, S.1 aJoshi, Rakesh, S.1 aBhoite, Ashwini, S.1 aMohandasan, Radhika1 aYadav, Amit, Kumar1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/tripeptides-derived-reactive-centre-loop-potato-type-ii-protease-inhibitors-preferentially01924nas a2200265   4500008004100000022001400041245018700055210006900242260000800311520091700319653001801236653002001254653002501274653003301299653001801332653003001350100001901380700002201399700002201421700002001443700002001463700002201483700002601505856012701531       2019                        eng d  a0739-110200aNMR structure and dynamics of inhibitory repeat domain variant 12, a plant protease inhibitor from Capsicum annuum, and its structural relationship to other plant protease inhibitors0 aNMR structure and dynamics of inhibitory repeat domain variant 1  cAPR3 a<p>Although several plant protease inhibitors have been structurally characterized using X-ray crystallography, very few have been studied using NMR techniques. Here, we report an NMR study of the solution structure and dynamics of an inhibitory repeat domain (IRD) variant 12 from the wound-inducible Pin-II type proteinase inhibitor from Capsicum annuum. IRD variant 12 (IRD12) showed strong anti-metabolic activity against the Lepidopteran insect pest, Helicoverpa armigera. The NMR-derived three-dimensional structure of IRD12 reveals a three-stranded anti-parallel beta-sheet rigidly held together by four disulfide bridges and shows structural homology with known IRDs. It is interesting to note that the IRD12 structure containing similar to 75% unstructured part still shows substantial amount of rigidity of N-H bond vectors with respect to its molecular motion. Communicated by Ramaswamy H. Sarma</p>
10aBt transgenic10aCapsicum annuum10aHelicoverpa armigera10ainhibitory repeating domains10aNMR structure10aProtease inhibitors (PIs)1 aGartia, Janeka1 aAnangi, Raveendra1 aJoshi, Rakesh, S.1 aGiri, Ashok, P.1 aKing, Glenn, F.1 aBarnwal, Ravi, P.1 aChary, Kandala, V. R.  uhttps://library.ncl.res.in/content/nmr-structure-and-dynamics-inhibitory-repeat-domain-variant-12-plant-protease-inhibitor02262nas a2200241   4500008004100000022001400041245009500055210006900150260000800219490000800227520149500235653001201730653002501742653001701767653002301784653002401807653001401831100001701845700000501862700002201867700001801889856011301907       2021                        eng d  a0022-263100aMolecular characterization of the beta(2)-like octopamine receptor of helicoverpa armigera0 aMolecular characterization of the beta2like octopamine receptor   cJUN0 v2543 a<p>Helicoverpa armigera is a devastating polyphagous and cosmopolitan crop pest. There are reports of this insect being resistant to a variety of pesticides raising concern worldwide. The Octopamine (OA) binding beta(2)-like receptor (OAR), a GPCR, is widely distributed in the nervous system of the insect and plays essential roles in the physiology and development and thus is an important target for insecticides. Yet, the molecular characterization of the H. armigera OAR (HarmOAR) and rational design of compounds based on this receptor is lacking. As a first step, we performed multiple sequence alignment of all insect OARs, which revealed that the sequences contained all conserved class A GPCR motifs. Phylogenetic studies showed clade-specific variations in the protein sequences primarily arising owing to differences in the ICL3 loop region. Further, a structural model of HarmOAR was built using the inactive human beta(2)AR as a template. 0.9 mu s atomistic simulations revealed conserved inter helical contacts and water molecules of HarmOAR. The detailed binding of octopamine was studied using molecular docking and 0.3 mu s atomistic simulations. Twenty-two insecticides active against octopamine receptors of other insects were compiled and docked to HarmOAR followed by rescoring with binding free energies to prioritize them for H. armigera. Our study suggests alpha-terpineol to be a good candidate as an insecticide or insect repellent for Helicoverpa armigera.</p>
10adocking10aHelicoverpa armigera10aInsecticides10amolecular dynamics10aOctopamine receptor10aPhylogeny1 aGujar, Nidhi1 a1 aJoshi, Rakesh, S.1 aJoshi, Manali  uhttps://library.ncl.res.in/content/molecular-characterization-beta2-octopamine-receptor-helicoverpa-armigera02593nas 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<p>
	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.</p>
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-recovery02422nas a2200277   4500008004100000022001400041245010100055210006900156260000800225300001100233490000800244520147200252653002501724653002801749653001501777653003701792653003101829100002201860700002101882700002501903700002201928700002701950700001801977700002201995856012702017       2025                        eng d  a0048-357500aAltered Octopamine synthesis impairs tyrosine metabolism affecting Helicoverpa armigera vitality0 aAltered Octopamine synthesis impairs tyrosine metabolism affecti  cMAR  a1063230 v2083 a<p>
	Tyramine (1-hydroxylase (T(1H) is a key enzyme in the biosynthesis of octopamine (OA), a vital neurohormone in invertebrates. This study explores the expression patterns and functional role of Helicoverpa armigera T(1H (HaT(1H) across various tissues and developmental stages. HaT(1H expression was highest in the head and adult male stages, reflecting tissue-specific and developmental regulation. HaT(1H silencing significantly increased locomotion and decreased feeding behavior. OA supplementation in silenced insects or HaT(1H overexpression showed a contrary effect on locomotory and feeding behavior. In silico screening and inhibitory assays identified tomatidine, a tomato-derived metabolite, as a potent HaT beta H inhibitor with strong binding affinity. In vivo bioassays confirmed tomatidine's inhibitory effects, reducing feeding and increasing mortality in H. armigera. Modulation in HaT(1H expression or activity disturbs the tyrosine metabolic pathway, with altered levels of tyramine, octopamine, and dopamine. These results highlight HaT(1H as a key regulator of OA biosynthesis, influencing insect feeding, locomotion, and overall survival. The present study also introduces tomatidine as a potential candidate for insect control, given its ability to disrupt HaT beta H function. This work provides new insights into the physiological roles of HaT beta H and offers promising avenues for developing targeted pest management strategies.</p>
10aHelicoverpa armigera10aOctopamine biosynthesis10aTomatidine10aTyramine (1-hydroxylase (HaT(1H)10aTyrosine metabolic pathway1 aPatil, Yogita, P.1 aWagh, Deepti, S.1 aBarvkar, Vitthal, T.1 aGawari, Shyam, K.1 aPisalwar, Priyanka, D.1 aAhmed, Shadab1 aJoshi, Rakesh, S.  uhttps://library.ncl.res.in/content/altered-octopamine-synthesis-impairs-tyrosine-metabolism-affecting-helicoverpa-armigera02510nas a2200265   4500008004100000022001400041245015000055210006900205260000800274300001100282490000800293520158100301653001601882653001001898653002501908653002101933653002901954653001601983100002301999700002502022700002302047700002102070700002202091856013102113       2025                        eng d  a0141-813000aLDH-dsRNA nanocarrier-mediated spray-induced silencing of juvenile hormone degradation pathway genes for targeted control of Helicoverpa armigera0 aLDHdsRNA nanocarriermediated sprayinduced silencing of juvenile   cDEC  a1486730 v3323 a<p>
	Helicoverpa armigera, a devastating agricultural pest, poses significant threats to global crop productivity. Targeting the Juvenile Hormone (JH) degradation pathway may offer a promising approach for pest management, given its pivotal role in insect development and reproduction. In this study, we developed a nanoclay-based formulation of double-stranded RNA (dsRNA) targeting three key JH degradation pathway genes: Juvenile Hormone Esterase (HaJHE), Juvenile Hormone Epoxy Hydrolase (HaJHEH), and Juvenile Hormone Diol Kinase (HaJHDK). Expression analysis revealed tissue and stage-specific patterns of these genes, with qRT-PCR confirming high expression levels of specific isoforms in key developmental transition: the pre-pupal stage. Treatment with bacterially expressed dsRNAs achieved &gt;50 % silencing of target genes, resulting in delay in larval-to-pupal transitions. Bioassay demonstrated that treatment with LDH-based dsRNA nanocarrier resulted in downregulation of target genes, causing developmental delays, including prolonged larval and pupal stages. Metabolomic analysis further indicated reduced accumulation of JH degradation pathway metabolites, highlighting the pathway-specific action of dsRNAs. Furthermore, combinatorial application of dsRNAs resulted in higher mortalities compared to individual dsRNA application. These results suggest that the application of the LDH-based dsRNA nanocarrier formulation against H. armigera JH degradation pathway for spray-induced gene silencing could serve as a potential insect management strategy.</p>
10aDevelopment10adsRNA10aHelicoverpa armigera10aJuvenile hormone10aLayered double hydroxide10aNanocarrier1 aJoshi, Kaumudi, S.1 aBarvkar, Vitthal, T.1 aHadapad, Ashok, B.1 aHire, Ramesh, S.1 aJoshi, Rakesh, S.  uhttps://library.ncl.res.in/content/ldh-dsrna-nanocarrier-mediated-spray-induced-silencing-juvenile-hormone-degradation-pathway02341nas 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<p>
	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.</p>
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