02159nas a2200241 4500008004100000022001400041245006700055210006700122260010600189300001200295490000700307520131200314653001501626653002001641653002501661653002601686653001101712100002801723700002001751700002401771700002101795856010101816 2005 eng d a0965-174800aGene expression patterns of helicoverpa armigera gut proteases0 aGene expression patterns of helicoverpa armigera gut proteases aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcAPR a355-3670 v353 a

Relative quantification of reported gut proteinase cDNAs from Helicoverpa armigera larvae fed on various host plants (cotton, chickpea, pigeonpea, tomato and okra), non-host plant Pis (winged bean, bitter gourd, ground nut, and capsicum) and during larval development has been carried out using semi-quantitative RT-PCR. Five trypsin-like and three chymotrypsin-like proteinases were categorized as insensitive or sensitive to most of the proteinase inhibitors (Pis) and insensitive/sensitive to specific Pis based on their expression analysis. These results were supported by amino acid sequence analysis, where diverged amino acids were observed in the regions, which are reported to be involved in typical trypsin trypsin inhibitor interactions and critical for proteinase inhibitor resistance. Among exopeptidases (five aminopeptidase and three carboxypeptidase), HaAmi4 and HaAmi5 of aminopeptidase and HaCar1 of carboxypeptidase exhibited considerable differential expression. Elastase and cathepsin B-like proteinases were expressed at negligible levels. The proteases identified in the study would be ideal candidates for further interactions studies with protease inhibitors to understand the structural reasons of protease inhibitor insensitivity (c) 2005 Elsevier Ltd. All rights reserved.

10aexpression10agut proteinases10aHelicoverpa armigera10aProteinase inhibitors10aRT-PCR1 aChougule, Nanasaheb, P.1 aGiri, Ashok, P.1 aSainani, Mohini, N.1 aGupta, Vidya, S. uhttps://library.ncl.res.in/content/gene-expression-patterns-helicoverpa-armigera-gut-proteases-002364nas a2200253 4500008004100000022001400041245022000055210006900275260010600344300001400450490000700464520128900471653002301760653002501783653002801808653002301836653001801859653002601877100001801903700002001921700002401941700002101965856012401986 2005 eng d a0031-942200aHigher accumulation of proteinase inhibitors in flowers than leaves and fruits as a possible basis for differential feeding preference of Helicoverpa armigera on tomato (Lycopersicon esculentum Mill, Cv. Dhanashree)0 aHigher accumulation of proteinase inhibitors in flowers than lea aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcNOV a2659-26670 v663 a

Tomato (Lycopersicon esculentum, Mill; cultivar- Dhanashree) proteinase inhibitors (Pis) were tested for their trypsin inhibitory (TT) and Helicoverpa armigera gut proteinases inhibitory (HGPI) activity in different organs of the tomato plants. Analysis of TI and HGPI distribution in various parts of the plant showed that flowers accumulated about 300 and 1000 times higher levels of TI while 700 and 400 times higher levels of HGPI as compared to those in leaves and fruits, respectively. Field observation that H. armigera larvae infest leaves and fruits but not the flowers could be at least partially attributed to the protective role-played by the higher levels of Pis in the flower tissue. Tomato Pis inhibited about 50-80% HGP activity of H. armigera larvae feeding on various host plants including tomato, of larvae exposed to non-host plant Pis and of various larval instars. Tomato Pis were found to be highly stable to insect proteinases wherein incubation of inhibitor with HGP even for 3 h at optimum conditions did not affect inhibitory activity. Bioassay using H. armigera larvae fed on artificial diet containing tomato PIs revealed adverse effect on larval growth, pupae development, adult formation and fecundity. (c) 2005 Elsevier Ltd. All rights reserved.

10aaccumulation of PI10aHelicoverpa armigera10aLycopersicon esculentum10aMidgut proteinases10aPlant defense10aProteinase inhibitors1 aDamle, M., S.1 aGiri, Ashok, P.1 aSainani, Mohini, N.1 aGupta, Vidya, S. uhttps://library.ncl.res.in/content/higher-accumulation-proteinase-inhibitors-flowers-leaves-and-fruits-possible-basis-002418nas a2200265 4500008004100000022001400041245011200055210006900167260007300236300001200309490000900321520145600330653001901786653001901805653002501824653002201849653002501871100002001896700002801916700002001944700001801964700002401982700002102006856012502027 2005 eng d a0304-416500aIn vivo and in vitro effect of capsicum annum proteinase inhibitors on helicoverpa armigera gut proteinases0 aIn vivo and in vitro effect of capsicum annum proteinase inhibit aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcMAR a156-1670 v17223 a

Two proteinase inhibitors (PIs), CapA1 and CapA2, were purified from Capsicum annum Linn. Var. Phule Jyoti leaves and assessed for their in vitro and in vivo activity against Helicoverpa armigera gut proteinases (HGPs). Both the inhibitors exhibited molecular weights of about 12 kDa with inhibitory activity against bovine trypsin and chymotrypsin indicating presence of probable two-inhibitor repeats of PIN II family. CapA1 and CapA2 inhibited 60-80% HGP (azocaseinolytic) activity of fourth instar larvae feeding on various host plants while 45-65% inhibition of HGP activity of various instars (II to VI) larvae reared on artificial diet. The partial purification of HGP isoforms, their characterization with synthetic inhibitors and inhibition by C. annum PIs revealed that most of the trypsin-like activity (68-91%) of HGPs was sensitive to C. annum PIs while 39-85% chymotrypsin-like activity of HGPs was insensitive to these inhibitors. The feeding of C. annum leaf extracts and two purified PIs in various doses to H. armigera larvae for two successive generations through artificial diet demonstrated their potential in inhibiting larval growth and development, delay in pupation period and dramatic reduction in fecundity and fertility. This is the first report-demonstrating efficacy of C. annum PIs against insect gut proteinases as well as larval growth and development of H. armigera. (c) 2004 Elsevier B.V. All rights reserved.

10aCapsicum annum10agut proteinase10aHelicoverpa armigera10ainsect resistance10aProteinase inhibitor1 aTamhane, V., A.1 aChougule, Nanasaheb, P.1 aGiri, Ashok, P.1 aDixit, A., R.1 aSainani, Mohini, N.1 aGupta, Vidya, S. uhttps://library.ncl.res.in/content/vivo-and-vitro-effect-capsicum-annum-proteinase-inhibitors-helicoverpa-armigera-gut-002786nas a2200265 4500008004100000022001400041245014000055210006900195260007400264300001200338490000700350520181600357653001302173653002002186653001502206653002502221653001102246653002502257100001902282700002002301700002502321700002202346700002102368856013102389 2005 eng d a0167-441200aKunitz trypsin inhibitor from chickpea (Cicer arietinum L.) that exerts anti-metabolic effect on podborer (Helicoverpa armigera) larvae0 aKunitz trypsin inhibitor from chickpea Cicer arietinum L that ex aVAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDSbSPRINGERcFEB a359-3740 v573 a

Chickpea (Cicer arietinum L.) seeds contain Bowman-Birk proteinase inhibitors, which are ineffective against the digestive proteinases of larvae of the insect pest Helicoverpa armigera. We have identified and purified a low expressing proteinase inhibitor (PI), distinct from the Bowman-Birk Inhibitors and active against H. armigera gut proteinases (HGP), from chickpea seeds. N-terminal sequencing of this HGP inhibitor revealed a sequence similar to reported pea (Pisum sativum) and chickpea alpha-L-fucosidases and also homologous to legume Kunitz inhibitors. The identity was confirmed by matrix assisted laser desorption ionization - time of flight analysis of tryptic peptides and isolation of DNA sequence coding for the mature protein. Available sequence data showed that this protein forms a distinct phylogenetic cluster with Kunitz inhibitors from Glycine max, Medicago truncatula, P. sativum and Canavalia lineata. The isolated coding sequence was cloned into a yeast expression vector and produced as a recombinant protein in Pichia pastoris. alpha-L-fucosidase activity was not detectable in purified or recombinant protein, by solution assays. The recombinant protein did not inhibit chymotrypsin or subtilisin activity but did exhibit stoichiometric inhibition of trypsin, comparable to soybean Kunitz trypsin inhibitor. The recombinant protein exhibited higher inhibition of total HGP activity as compared to soybean kunitz inhibitor, even though it preferentially inhibited HGP-trypsins. H. armigera larvae fed on inhibitor-incorporated artificial diet showed significant reduction in average larval weight after 18 days of feeding demonstrating potent antimetabolic activity. The over-expression of this gene in chickpea could act as an endogenous source of resistance to H. armigera.

10aChickpea10aCicer arietinum10afucosidase10aHelicoverpa armigera10aKunitz10aProteinase inhibitor1 aSrinivasan, A.1 aGiri, Ashok, P.1 aHarsulkar, Abhay, M.1 aGatehouse, J., A.1 aGupta, Vidya, S. uhttps://library.ncl.res.in/content/kunitz-trypsin-inhibitor-chickpea-cicer-arietinum-l-exerts-anti-metabolic-effect-podborer-002480nas a2200253 4500008004100000022001400041245015100055210006900206260010600275300001400381490000700395520148200402653002001884653002501904653002001929653001501949653002501964100001901989700002802008700002002036700002202056700002102078856012702099 2005 eng d a0022-191000aPodborer (Helicoverpa armigera Hubn.) does not show specific adaptations in gut proteinases to dietary Cicer arietinum Kunitz proteinase inhibitor0 aPodborer Helicoverpa armigera Hubn does not show specific adapta aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcNOV a1268-12760 v513 a

We investigated the response of Helicoverpa armigera larvae towards ingestion of Cicer arietinum Kunitz proteinase inhibitor (CaKPI), which caused antagonistic effects on developing H. armigera larvae. CaKPI-degrading proteinases were not detectable in either control or sensitized larvae. There were negligible increases in total proteinase activity, as well as in trypsin-like and chymotrypsin-like activities of H. armigera gut proteinases (HGPs). Decrease in sensitivity of HGPs to inhibition by CaKPI was not observed when the inhibitor was fed Suggesting that the insect had not shown a specific adaptive response to dietary CaKPI. Semi-quantitative reverse transcriptase polymerase chain reaction (Q RT-PCR) analysis showed a general up-regulation of proteases in larvae that ingested CaKPI and a specific regulation of individual transcripts was not observed. CaKPI had maximum inhibitory activity against HGP derived from fourth instar larvae. CaKPI was equally potent in inhibition of HGPs derived from larvae fed on different host plants, as well as various proteinase inhibitors (Pis) to which larval adaptation was previously reported. The lack of larval response to CaKPI was attributable to the atypical active site sequence and inhibitory activity of CaKPI and/or to the pre-adaptation of H. armigera larvae due to the constant exposure to basal levels of CaKPI in chickpea seeds or a chickpea seed-based diet. (c) 2005 Elsevier Ltd. All rights reserved.

10aCicer arietinum10aHelicoverpa armigera10ainsect response10aproteinase10aProteinase inhibitor1 aSrinivasan, A.1 aChougule, Nanasaheb, P.1 aGiri, Ashok, P.1 aGatehouse, J., A.1 aGupta, Vidya, S. uhttps://library.ncl.res.in/content/podborer-helicoverpa-armigera-hubn-does-not-show-specific-adaptations-gut-proteinases-002410nas a2200337 4500008004100000022001400041245011600055210006900171260009200240300001200332490000700344520123200351653002701583653002301610653001401633653001601647653002501663653001101688653002701699653001301726100002801739700002201767700002101789700002001810700002401830700002301854700002201877700002001899700002601919856012701945 2008 eng d a0958-315700aComparison of Metarhizium isolates for biocontrol of helicoverpa armigera (Lepidoptera : Noctuidae) in chickpea0 aComparison of Metarhizium isolates for biocontrol of helicoverpa a4 PARK SQUARE, MILTON PARK, ABINGDON OX14 4RN, OXON, ENGLANDbTAYLOR & FRANCIS LTDcFEB a809-8280 v183 a

Metarhizium isolates from soil (53) and insect hosts (10) were evaluated for extracellular production of cuticle degrading enzyme (CDE) activities such as chitinase, chitin deacetylase (CDA), chitosanase, protease and lipase. Regression analysis demonstrated the relation of CDE activities with Helicoverpa armigera mortality. On basis of this relation, ten isolates were selected for further evaluation. Subsequently, based on LT(50) of the 10 isolates towards H. armigera, five isolates were selected. Out of these five isolates, three were selected on the basis of higher conidia production (60-75 g/kg rice), faster sedimentation time (ST(50)) (2.3-2.65 h in 0.1% (w/v) Tween 80) and lower LC(50) (1.4- 5.7 x 10(3) conidia/mL) against H. armigera. Finally, three Metarhizium isolates were selected for the molecular fingerprinting using ITS sequencing and RAPD patterning. All three isolates, M34412, M34311 and M81123, showed comparable RAPD patterns with a 935G primer. These were further evaluated for their field performance against H. armigera in a chickpea crop. The percent efficacies with the three Metarhizium isolates were from 65 to 72%, which was comparable to the chemical insecticide, endosulfan (74%).

10aappressorium formation10achitin deacetylase10achitinase10achitosanase10aHelicoverpa armigera10aLipase10aMetarhizium anisopliae10aProtease1 aKulkarni, Shuklangi, A.1 aGhormade, Vandana1 aKulkarni, Girish1 aKapoor, Manisha1 aChavan, Santosh, B.1 aRajendran, Armugam1 aPatil, Sanjay, K.1 aShouche, Yogesh1 aDeshpande, Mukund, V. uhttps://library.ncl.res.in/content/comparison-metarhizium-isolates-biocontrol-helicoverpa-armigera-lepidoptera-noctuidae-002914nas a2200337 4500008004100000022001400041245014400055210006900199260009200268300001200360490000700372520169100379653002702070653002302097653001402120653002502134653002702159653001102186653002702197653001302224100002302237700002802260700002202288700002402310700002102334700002402355700002102379700002002400700002602420856013002446 2008 eng d a0958-315700aEffect of repeated in vitro sub-culturing on the virulence of metarhizium anisopliae against helicoverpa armigera (Lepidoptera : Noctuidae)0 aEffect of repeated in vitro subculturing on the virulence of met a4 PARK SQUARE, MILTON PARK, ABINGDON OX14 4RN, OXON, ENGLANDbTAYLOR & FRANCIS LTDcMAY a337-3550 v183 a

The effect of repeated conidial sub-culturing of Metarhizium anisopliae on its virulence against Helicoverpa armigera (Hbner) was studied. The LT(50) observed against third instar larvae of H. armigera for the first sub-culture was 3.4 days; it increased to 4.5 and 5.6 days for the 20th and the 40th sub-cultures, respectively. The LT50 values after passage of the 40th sub-culture on H. armigera decreased to 4.4 and 3.7 days for the 40th (first in vivo) and the 40th (fifth in vivo) passages, respectively. Similarly, the LC(50) of M. anisopliae towards third instar larvae of H. armigera increased from the first sub-culture (0.17x10(4)) to (3.0x10(4)) for the 40th conidial transfers on potato dextrose agar and again decreased to 0.74x10(4) and 0.23x10(4) in the 40th (first in vivo) and the 40th (fifth in vivo) passage, respectively. Similar trends for LC(50) and LT(50) values were seen when sugarcane woolly aphid, Ceratovacuna lanigera Zehntner was used as a host. Significant variation in appressorium formation and cuticle-degrading enzyme production such as chitinase, chitin deacetylase, chitosanase and protease during subsequent sub-culturing and passage through H. armigera was observed. Though there was no effect on internal transcribed spacer (ITS) sequence pattern, interestingly, in randomly amplified polymorphic DNA (RAPD), significant differences in the band intensities and in the banding pattern for different sub-cultures of M. anisopliae were observed. As stable virulence towards the insect pest is desirable for commercialisation of a mycoinsecticide, such changes in virulence due to repeated in vitro transfer need to be monitored and minimised.

10aappressorium formation10achitin deacetylase10achitinase10aHelicoverpa armigera10ain vitro sub-culturing10aLipase10aMetarhizium anisopliae10aProtease1 aNahar, Pallavi, B.1 aKulkarni, Shuklangi, A.1 aKulye, Mahesh, S.1 aChavan, Santosh, B.1 aKulkarni, Girish1 aRajendran, Armugham1 aYadav, Priya, D.1 aShouche, Yogesh1 aDeshpande, Mukund, V. uhttps://library.ncl.res.in/content/effect-repeated-vitro-sub-culturing-virulence-metarhizium-anisopliae-against-helicoverpa-002324nas a2200253 4500008004100000022001400041245010900055210006900164260007100233300001400304490000700318520141500325653001501740653001601755653002001771653002501791653001501816100002301831700002401854700002101878700002101899700002001920856013001940 2011 eng d a1535-389300aAssimilatory potential of helicoverpa armigera reared on host (chickpea) and nonhost (cassia tora) diets0 aAssimilatory potential of helicoverpa armigera reared on host ch a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcNOV a5128-51380 v103 a

Adaptation to plant allelochemicals is a crucial aspect of herbivore chemical ecology. To understand an insect ecology, we studied an effect of nonhost Cassia tora seed-based diet (Ct) on growth, development, and molecular responses in Helicoverpa armigera. We employed a comparative approach to investigate the proteomic differences in gut, hemolymph, and frass of H. armigera reared on a normal (chickpea seed-based, Cp) and Ct diet. In this study, a total of 46 proteins were identified by nano-LC-MS(E). Among them, 17 proteins were up-regulated and 29 proteins were down-regulated when larvae were exposed to the Ct diet. Database searches combined with GO analysis revealed that gut proteases engrossed in digestion, proteins crucial for immunity, adaptive responses to stress, and detoxification were down-regulated in the Ct fed larvae. Proteins identified in H. armigera hemolymph were found to be involved in defense mechanisms. Moreover, proteins found in frass of the Ct fed larvae were observed to participate in energy metabolism. Biochemical and quantitative real-time PCR analysis of selected candidate proteins showed differential gene expression patterns and corroborated with the proteomic data. Our results suggest that the Ct diet could alter expression of proteins related to digestion, absorption of nutrients, adaptation, defense mechanisms, and energy metabolism in H. armigera.

10aadaptation10aCassia tora10aGene expression10aHelicoverpa armigera10aproteomics1 aDawkar, Vishal, V.1 aChikate, Yojana, R.1 aGupta, Vidya, S.1 aSlade, Susan, E.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/assimilatory-potential-helicoverpa-armigera-reared-host-chickpea-and-nonhost-cassia-tora-002280nas a2200241 4500008004100000022001400041245010000055210006900155260007300224300000800297490000800305520142300313653001001736653002201746653002001768653002501788653001401813100002401827700002001851700002101871700002001892856012601912 2012 eng d a0378-111900aAmylase gene expression patterns in Helicoverpa armigera upon feeding on a range of host plants0 aAmylase gene expression patterns in Helicoverpa armigera upon fe aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcJUN a1-70 v5013 a

Expression of two amylase genes (HaAmy1 and HaAmy2) was studied in Helicoverpa armigera (Hubner; Lepidoptera: Noctuidae) feeding on different host plants and during larval development. Alignment of HaAmy1 and HaAmy2 with other insect amylases shows similarities with known Lepidopteran amylase transcripts. H. armigera amylase gene expression is influenced by the availability of reducing sugars, sucrose and starch content of host plants and further correlates to the pool of reducing sugars in the gut and haemolymph of larvae. HaAmy1 and HaAmy2 during larval development on two host plants viz., maize (cereal) and marigold (ornamental) showed their relative difference. Results support the view that when host plants differ in their macronutrients, relationships of enzymes and substrates are flexible. The present work highlights the distribution of HaAmy1 and HaAmy2 (i) during various stages of insect development (second, fourth and sixth instar, pupa, adult and egg), (ii) in various tissues viz., head, haemolymph, fat body, integument and whole larval body of H. armigera feeding on artificial diet and (iii) in three gut regions of larvae fed on various diets. Complexity in expression of amylase genes suggests existence of mechanisms involved to detect nutrient balance required for avoiding fitness costs and focus their importance in insect nutrition. (C) 2012 Elsevier B.V. All rights reserved.

10aDiets10aDigestive amylase10aGene expression10aHelicoverpa armigera10aNutrition1 aKotkar, Hemlata, M.1 aBhide, Amey, J.1 aGupta, Vidya, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/amylase-gene-expression-patterns-helicoverpa-armigera-upon-feeding-range-host-plants-002473nas a2200241 4500008004100000022001400041245013400055210006900189260007400258300001200332490000600344520154200350653002001892653002501912653002301937653002601960653001501986100002502001700002802026700002802054700002102082856012802103 2013 eng d a1872-885500aCompensatory proteolytic responses to dietary proteinase inhibitors from Albizia lebbeck seeds in the helicoverpa armigera larvae0 aCompensatory proteolytic responses to dietary proteinase inhibit aVAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDSbSPRINGERcJUN a259-2660 v73 a

Plant proteinase inhibitors (PIs) have been shown to reduce the growth rates in larvae of numerous insect species. On the other hand, insects can also regulate their proteinases against plant PIs. In the present study, we report the compensatory activities of Helicoverpa armigera (Hubner) (Lepidoptera: Noctuidae) gut proteinases against the PIs of Albizia lebbeck seeds. Total of ten proteinase inhibitor bands were detected in the seed extract of A. lebbeck. Bioassays were conducted by feeding H. armigera larvae on diet containing partially purified PIs from A. lebbeck seeds. Results show that larval growth and survival was significantly reduced by A. lebbeck PIs. We found that higher activity H. armigera gut proteinase (HGP) isoforms observed in the midgut of control larvae were inhibited in the midgut of larvae fed on test diet. Some HGP isoforms were induced in the larvae fed on PI containing test diet; however, these isoforms showed lower activity in the larvae fed on control diet. Aminopeptidase activities were significantly increased in the midgut of larvae fed on test diet. A population of susceptible and resistant enzymes was observed in the midgut of H. armigera, when fed on diet containing PIs from A. lebbeck seeds. Our initial observations indicate that H. armigera can regulate its digestive proteinase activity against non-host plant PIs, too. It is important to study the exact biochemical and molecular mechanisms underlying this phenomenon in order to develop PI-based insect control strategies.

10aAlbizia lebbeck10aHelicoverpa armigera10aMidgut proteinases10aProteinase inhibitors10aregulation1 aHivrale, Vandana, K.1 aLomate, Purushottam, R.1 aBasaiyye, Shriniwas, S.1 aKalve, Neeta, D. uhttps://library.ncl.res.in/content/compensatory-proteolytic-responses-dietary-proteinase-inhibitors-albizia-lebbeck-seeds-002009nas 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

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.

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

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.

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-002475nas a2200253 4500008004100000022001400041245014800055210006900203260010600272300001200378490000700390520147200397653002001869653002501889653001101914653002901925653002401954100002801978700002202006700002102028700002102049700002002070856013102090 2014 eng d a0965-174800aIdentification and expression profiling of helicoverpa armigera microRNAs and their possible role in the regulation of digestive protease genes0 aIdentification and expression profiling of helicoverpa armigera  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcNOV a129-1370 v543 a

The present investigation is an effort to determine the possible roles of microRNAs (miRNAs) in the regulation of protease gene expression in Helicoverpa armigera upon exposure to plant protease inhibitors (PIs). Using Illumina platform, deep sequencing of 12 small RNA libraries was performed from H. armigera larvae fed on artificial diet (AD) or recombinant Capsicum annuum PI-7 (rCanPI-7) incorporated diet, at various time intervals (0.5, 2, 6, 12, 24, and 48 h). Sequencing data were analyzed with miRDeep2 software; a total of 186 unique miRNAs were identified from all the 12 libraries, out of which 96 were conserved while 90 were novel. These miRNAs showed all the conserved characteristics of insect miRNAs. Homology analysis revealed that most of the identified miRNAs were insect-specific, and more than 50 miRNAs were Lepidoptera-specific. Several candidate miRNAs (conserved and novel) were differentially expressed in rCanPI-7 fed larvae as compared to the larvae fed on AD. H. armigera miRNAs were found to have target sites in several protease genes as well as in protease regulation related genes such as serine PI and immune reactive PI. As expected, negative correlation in the relative abundance miRNAs and their target mRNAs was evident from qualitative real time polymerase chain reaction analysis. The investigation revealed potential roles of miRNAs in H. armigera protease gene regulation. (C) 2014 Elsevier Ltd. All rights reserved.

10aDeep sequencing10aHelicoverpa armigera10amiRNAs10aProtease gene regulation10aProtease inhibitors1 aLomate, Purushottam, R.1 aMahajan, Neha, S.1 aKale, Sandip, M.1 aGupta, Vidya, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/identification-and-expression-profiling-helicoverpa-armigera-micrornas-and-their-possible-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

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

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

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.

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-002746nas a2200265 4500008004100000022001400041245011600055210006900171260007300240300001400313490000900327520177500336653001902111653002302130653002202153653002002175653002502195100002002220700002402240700002302264700002102287700002602308700002002334856012602354 2015 eng d a0304-416500aBiochemical, structural and functional diversity between two digestive alpha-amylases from helicoverpa armigera0 aBiochemical structural and functional diversity between two dige aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcSEP a1719-17280 v18503 a

Background: Helicoverpa armigera (Lepidoptera) feeds on various plants using diverse digestive enzymes as one of the survival tool-kit. The aim of the present study was to understand biochemical properties of recombinant alpha-amylases of H. armigera viz., HaAmy1 and HaAmy2. Methods: The open reading frames of HaAmy1 and HaAmy2 were cloned in Pichia pastoris and expressed heterologously. Purified recombinant enzymes were characterized for their biochemical and biophysical attributes using established methods. Results: Sequence alignment and homology modeling showed that HaAmy1 and HaAmy2 were conserved in their amino acid sequences and structures. HaAmy1 and HaAmy2 showed optimum activity at 60 degrees C; however, they differed in their optimum pH. Furthermore, HaAmy2 showed higher affinity for starch and amylopectin whereas HaAmy1 had higher catalytic efficiency. HaAmy1 and HaAmy2 were inhibited to the same magnitude by a synthetic amylase inhibitor (acarbose) while wheat amylase inhibitor showed about 2-fold higher inhibition of HaAmy1 than HaAmy2 at pH 7 while 6-fold difference at pH 11. Interactions of HaAmy1 and HaAmy2 with wheat amylase inhibitor revealed 2:1 stoichiometric ratio and much more complex interaction with HaAmy1. Conclusions: The diversity of amylases in perspective of their biochemical and biophysical properties, and their differential interactions with amylase inhibitors signify the potential role of these enzymes in adaptation of H. armigera on diverse plant diets. General significance: Characterization of digestive enzymes of H. armigera provides the molecular basis for the polyphagous nature and thus could assist in designing future strategies for the insect control. (C) 2015 Elsevier B.V. All rights reserved.

10aalpha-amylases10aAmylase inhibitors10aDigestive enzymes10aEnzyme activity10aHelicoverpa armigera1 aBhide, Amey, J.1 aChannale, Sonal, M.1 aPatil, Sucheta, S.1 aGupta, Vidya, S.1 aRamasamy, Sureshkumar1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/biochemical-structural-and-functional-diversity-between-two-digestive-alpha-amylases-002747nas a2200253 4500008004100000022001400041245014700055210006900202260006700271300001000338490000700348520180200355653001702157653002502174653002702199653001502226653001802241100002302259700002402282700002102306700002102327700002002348856012502368 2016 eng d a1672-960900aExpression of proteins involved in digestion and detoxification are regulated in helicoverpa armigera to cope up with chlorpyrifos insecticide0 aExpression of proteins involved in digestion and detoxification  a111 RIVER ST, HOBOKEN 07030-5774, NJ USAbWILEY-BLACKWELLcFEB a68-770 v233 a

Helicoverpa armigera is a key pest in many vital crops, which is mainly controlled by chemical strategies. To manage this pest is becoming challenging due to its ability and evolution of resistance against insecticides. Further, its subsequent spread on nonhost plant is remarkable in recent times. Hence, decoding resistance mechanism against phytochemicals and synthetic insecticides is a major challenge. The present work describes that the digestion, defense and immunity related enzymes are associated with chlorpyrifos resistance in H. armigera. Proteomic analysis of H. armigera gut tissue upon feeding on chlorpyrifos containing diet (CH) and artificial diet (AD) using nano-liquid chromatography-mass spectrometry identified upregulated 23-proteins in CH fed larvae. Database searches combined with gene ontology analysis revealed that the identified gut proteins engrossed in digestion, proteins crucial for immunity, adaptive responses to stress, and detoxification. Biochemical and quantitative real-time polymerase chain reaction analysis of candidate proteins indicated that insects were struggling to get nutrients and energy in presence of CH, while at the same time endeavoring to metabolize chlorpyrifos. Moreover, we proposed a potential processing pathway of chlorpyrifos in H. armigera gut by examining the metabolites using gas chromatography-mass spectrometry. H. armigera exhibit a range of intriguing behavioral, morphological adaptations and resistance to insecticides by regulating expression of proteins involved in digestion and detoxification mechanisms to cope up with chlorpyrifos. In these contexts, as gut is a rich repository of biological information; profound analysis of gut tissues can give clues of detoxification and resistance mechanism in insects.

10achlorpyrifos10aHelicoverpa armigera10ainsecticide resistance10aproteomics10areal-time PCR1 aDawkar, Vishal, V.1 aChikate, Yojana, R.1 aMore, Tushar, H.1 aGupta, Vidya, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/expression-proteins-involved-digestion-and-detoxification-are-regulated-helicoverpa-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

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.

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

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

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-inhibitor02402nas a2200265 4500008004100000022001400041245011800055210006900173260000800242300001200250490000700262520150500269653002001774653001501794653001401809653001901823653002501842653002901867653002601896653001601922653002701938100002101965700002601986856012402012 2019 eng d a0233-111X00aPuzzle of highly virulent Metarhizium anisopliae strains from Annona squamosa fields against Helicoverpa armigera0 aPuzzle of highly virulent Metarhizium anisopliae strains from An cAPR a392-4010 v593 a

In our search for indigenous virulent strains of the entomopathogenic fungi, we observed that Metarhizium isolates from soils associated with Annona squamosa (custard apple) have higher virulence (>90% mortality of Helicoverpa armigera larvae at 1/10(th) spore concentration) than strains isolated from Solanum lycopersicum (tomato) fields. Proteomic analysis revealed two insecticidal cyclopeptides of A. squamosa origin in the M. anisopliae strains that led to higher virulence against H. armigera. Transcriptomic and genomic data indicated that M. anisopliae strains and A. squamosa had more than 20 genes in common, including those for cyclic hexapeptide synthase, non-ribosomal peptide synthetase, and plant cyclotide genes, which are involved in the biosynthesis of insecticidal cyclopeptides. These genes were absent in M. anisopliae strains isolated from the S. lycopersicum fields. Further, these strains can establish an endophytic relationship with A. squamosa suggesting that these rhizospheric strains originally could be endophytes, which were eventually released into the soil. Further, Metarhizium strains associated with Capsicum annuum (chili), Azadirachta indica (neem), and Carica papaya (papaya) - plants with insecticidal properties - also had higher virulence against H. armigera. Thus exploration of rhizospheres of plants producing insecticidal metabolites to isolate entomopathogenic fungi, per se, could be a viable strategy in agricultural for crop protection.

10aAnnona squamosa10aBiocontrol10aendophyte10aentomopathogen10aHelicoverpa armigera10ahorizontal gene transfer10ainsecticidal peptides10aMetarhizium10anatural transformation1 aPathan, Ejaj, K.1 aDeshpande, Mukund, V. uhttps://library.ncl.res.in/content/puzzle-highly-virulent-metarhizium-anisopliae-strains-annona-squamosa-fields-against02262nas 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

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.

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

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-recovery02322nas a2200253 4500008004100000022001400041245014300055210006900198260000800267490000800275520140100283653001701684653003701701653001401738653002501752653001901777100002301796700003201819700002101851700002501872700002201897700002001919856012901939 2024 eng d a0965-174800aAminoacylase efficiently hydrolyses fatty acid amino acid conjugates of Helicoverpa armigera potentially to increase the pool of glutamine0 aAminoacylase efficiently hydrolyses fatty acid amino acid conjug cFEB0 v1653 a

One of the most prevalent bioactive molecules present in the oral secretion (OS) of lepidopteran insects is fatty acid amino acid conjugates (FACs). Insect dietary components have influence on the synthesis and retaining the pool of FACs in the OS. We noted differential and diet-specific accumulation of FACs in the OS of Helicoverpa armigera by using Liquid Chromatography-Quadrupole Time of Flight Mass Spectrometry. Interestingly, we identified FACs hydrolyzing enzyme aminoacylase (HaACY) in the OS of H. armigera through proteomic analysis. Next, we have cloned, expressed, and purified active recombinant HaACY in the bacterial system. Recombinant HaACY hydrolyzes all the six identified FACs in the OS of H. armigera larvae fed on host and non-host plants and releases respective fatty acid and glutamine. In these six FACs, fatty acid moieties vary while amino acid glutamine was common. Glutamine obtained upon hydrolysis of FACs by HaACY might serve as an amino acid pool for insect growth and development. To understand the substrate choices of HaACY, we chemically synthesized, purified, and characterized all the six FACs. Interestingly, rHaACY also shows hydrolysis of synthetic FACs into respective fatty acid and glutamine. Our results underline the importance of diet on accumulation of FACs and role of aminoacylase(s) in regulating the level of FACs and glutamine.

10aAminoacylase10aFatty acid amino acid conjugates10aGlutamine10aHelicoverpa armigera10aOral secretion1 aKallure, Gopal, S.1 aSahoo, Shubhranshu, Shekhar1 aKale, Rutuja, S.1 aBarvkar, Vitthal, T.1 aKontham, Ravindar1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/aminoacylase-efficiently-hydrolyses-fatty-acid-amino-acid-conjugates-helicoverpa-armigera02422nas 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

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.

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

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 >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.

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

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