02290nas a2200205 4500008004100000245011900041210006900160260000800229300001200237490000800249520153200257100002101789700002401810700002701834700002201861700002401883700002501907700002001932856013201952 2016 eng d00aBudding trends in integrated pest management using advanced micro- and nano-materials: challenges and perspectives0 aBudding trends in integrated pest management using advanced micr cDEC a157-1690 v1843 aOne of the most vital supports to sustain human life on the planet earth is the agriculture system that has been constantly challenged in terms of yield. Crop losses due to insect pest attack even after excessive use of chemical pesticides, are major concerns for humanity and environment protection. By the virtue of unique properties possessed by micro and nano-structures, their implementation in Agri-biotechnology is largely anticipated. Hence, traditional pest management strategies are now forestalling the potential of micro and nanotechnology as an effective and viable approach to alleviate problems pertaining to pest control. These technological innovations hold promise to contribute enhanced productivity by providing novel agrochemical agents and delivery systems. Application of these systems engages to achieve: i) control release of agrochemicals, ii) site-targeted delivery of active ingredients to manage specific pests, iii) reduced pesticide use, iv) detection of chemical residues, v) pesticide degradation, vi) nucleic acid delivery and vii) to mitigate post-harvest damage. Applications of micro and nano-technology are still marginal owing to the perception of low economic returns, stringent regulatory issues involving safety assessment and public awareness over their uses. In this review, we highlight the potential application of micro and nano-materials with a major focus on effective pest management strategies including safe handling of pesticides. (C) 2016 Elsevier Ltd. All rights reserved.1 aKhandelwal, Neha1 aBarbole, Ranjit, S.1 aBanerjee, Shashwat, S.1 aChate, Govind, P.1 aBiradar, Ankush, V.1 aKhandare, Jayant, J.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/budding-trends-integrated-pest-management-using-advanced-micro-and-nano-materials-challenges02304nas a2200193 4500008004100000245009500041210006900136260000800205300001000213490000800223520161200231100002401843700002301867700002401890700002901914700002101943700002001964856012601984 2016 eng d00aRNAi of selected candidate genes interrupts growth and development of Helicoverpa armigera0 aRNAi of selected candidate genes interrupts growth and developme cOCT a44-510 v1333 aHelicoverpa armigera is one of the major crop pests and is less amenable to current pest control approaches. RNA interference (RNAi) is emerging as a potent arsenal for the insect pest control over current methods. Here, we examined the effect on growth and development in H. armigera by targeting various enzymes/proteins such as proteases like trypsins (HaTry2, 3, 4 and 6), chymotrypsin (HaChy4) and cysteine protease like cathepsin (HaCATHL); glutathione S-transferases (HaGST1a, 6 and 8); esterases (HaAce4, HaJHE); catalase (HaCAT); super-oxide-dismutase (HaCu/ZnSOD); fatty acid binding protein (HaFabp) and chitin deacetylase (HaCda5b) through dsRNA approach. Significant downregulation of cognate mRNA expression and reduced activity of trypsin and GST-like enzyme were evident upon feeding candidate dsRNAs to the larvae. Among these, the highest mortality was observed in HaAce4 dsRNA fed larvae followed by HaJHE; HaCAT; HaCuZnSOD; HaFabp and HaTry3 whereas remaining ones showed relatively lower mortality. Furthermore, the dsRNA fed larvae showed significant reduction in the larval mass and abnormalities at the different stages of H. armigera development compared to their control diets. For example, malformed larvae, pupae and moth at a dose of 60 pg/day were evident in high number of individual insects fed on dsRNA containing diets. Moreover, the growth and development of insects and moths were retarded in dsRNA fed larvae. These findings might provide potential new candidates for designing effective dsRNA as pesticide in crop protection. (C) 2016 Elsevier Inc. All rights reserved.1 aChikate, Yojana, R.1 aDawkar, Vishal, V.1 aBarbole, Ranjit, S.1 aTilak, Priyadarshini, V.1 aGupta, Vidya, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/rnai-selected-candidate-genes-interrupts-growth-and-development-helicoverpa-armigera-001937nas a2200205 4500008004100000245014900041210006900190260000800259300001200267490000700279520115700286100002301443700002401466700002301490700002801513700002201541700002001563700002101583856012701604 2017 eng d00aImproved tolerance against helicoverpa armigera in transgenic tomato over-expressing multi-domain proteinase inhibitor gene from capsicum annuum0 aImproved tolerance against helicoverpa armigera in transgenic to cJUL a597-6040 v233 aPlant proteinase inhibitors (PIs) are plant defense proteins and considered as potential candidates for engineering plant resistances against herbivores. Capsicum annuum proteinase inhibitor (CanPI7) is a multi-domain potato type II inhibitor (Pin-II) containing four inhibitory repeat domains (IRD), which target major classes of digestive enzymes in the gut of Helicoverpa armigera larvae. Stable integration and expression of the transgene in T1 transgenic generation, were confirmed by established molecular techniques. Protein extract of transgenic tomato lines showed increased inhibitory activity against H. armigera gut proteinases, supporting those domains of CanPI7 protein to be effective and active. When T1 generation plants were analyzed, they exhibited antibiosis effect against first instar larvae of H. armigera. Further, larvae fed on transgenic tomato leaves showed delayed growth relative to larvae fed on control plants, but did not change mortality rates significantly. Thus, better crop protection can be achieved in transgenic tomato by overexpression of multi-domain proteinase inhibitor CanPI7 gene against H. armigera larvae.1 aTanpure, Rahul, S.1 aBarbole, Ranjit, S.1 aDawkar, Vishal, V.1 aWaichal, Yashashree, A.1 aJoshi, Rakesh, S.1 aGiri, Ashok, P.1 aGupta, Vidya, S. uhttps://library.ncl.res.in/content/improved-tolerance-against-helicoverpa-armigera-transgenic-tomato-over-expressing-multi03076nas a2200265 4500008004100000022001400041245011900055210006900174260000800243300001400251490000600265520217000271100002302441700002202464700002402486700002002510700002002530700001902550700002202569700002102591700003702612700001802649700002002667856012302687 2019 eng d a2470-134300aAzadirachtin-A from azadirachta indica impacts multiple biological targets in cotton bollworm helicoverpa armigera0 aAzadirachtinA from azadirachta indica impacts multiple biologica cMAY a9531-95410 v43 a

Azadirachtin-A (AzaA) from the Indian neem tree (Azadirachta indica) has insecticidal properties; however, its molecular mechanism remains elusive. The ``targeted and nontargeted proteomic profiling'', metabolomics, matrix-assisted laser desorption/ionization time of flight (MALDI-TOF) imaging, gene expression, and in silico analysis provided clues about its action on Helicoverpa armigera. Fourth instar H. armigera larvae fed on AzaA-based diet (AzaD) suffered from significant mortality, growth retardation, reduced larval mass, complications in molting, and prolonged development. Furthermore, death of AzaD-fed larvae was observed with various phenotypes like bursting, blackening, and half-molting. Liquid chromatography-mass spectrometry (LC-MS) data showed limited catabolic processing of ingested AzaA and dramatic alternations of primary metabolism in H. armigera. MALDI-TOF imaging indicated the presence of AzaA in midgut of H. armigera. In the gut, out of 79 proteins identified, 34 were upregulated, which were related to digestion, immunity, energy production, and apoptosis mechanism. On the other hand, 45 proteins were downregulated, including those from carbohydrate metabolism, lipid metabolism, and energy transfer. In the hemolymph, 21 upregulated proteins were reported to be involved in immunity, RNA processing, and mRNA-directed protein synthesis, while 7 downregulated proteins were implicated in energy transfer, hydrolysis, lipid metabolism, defense mechanisms, and amino acid storage-related functions. Subsequently, six target proteins were identified using labeled AzaA that interacted with whole insect proteins. In silico analysis suggests that AzaA could be efficiently accommodated in the hydrophobic pocket of juvenile hormone esterase and showed strong interaction with active site residues, indicating plausible targets of AzaA in H. armigera. Quantitative polymerase chain reaction analysis suggested differential gene expression patterns and partly corroborated the proteomic results. Overall, data suggest that AzaA generally targets more than one protein in H. armigera and hence could be a potent biopesticide.

1 aDawkar, Vishal, V.1 aBarage, Sagar, H.1 aBarbole, Ranjit, S.1 aFatangare, Amol1 aGrimalt, Susana1 aHaldar, Saikat1 aHeckel, David, G.1 aGupta, Vidya, S.1 aThulasiram, Hirekodathakallu, V.1 aSvatos, Ales.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/azadirachtin-azadirachta-indica-impacts-multiple-biological-targets-cotton-bollworm02347nas a2200289 4500008004100000245011900041210006900160260000800229300001100237490000800248520141100256100002101667700001701688700001601705700001801721700002001739700002301759700001901782700001601801700001801817700001401835700002001849700002401869700001901893700001501912856013001927 2022 eng d00aIdentification and characterization of the key enzyme in the biosynthesis of the neurotoxin beta-ODAP in grass pea0 aIdentification and characterization of the key enzyme in the bio cMAY a1018060 v2983 a

Grass pea (Lathyrus sativus L.) is a grain legume commonly grown in Asia and Africa for food and forage. It is a highly nutritious and robust crop, capable of surviving both droughts and floods. However, it produces a neurotoxic compound, beta-N- oxalyl-L-alpha,beta-diaminopropionic acid (beta-ODAP), which can cause a severe neurological disorder when consumed as a primary diet component. While the catalytic activity associated with beta-ODAP formation was demonstrated more than 50 years ago, the enzyme responsible for this activity has not been identified. Here, we report on the identity, activity, 3D structure, and phylogenesis of this enzyme-beta-ODAP synthase (BOS). We show that BOS belongs to the benzylalcohol O-acetyltransfer-ase, anthocyanin O-hydroxycinnamoyltransferase, anthranilate N-hydroxycinnamoyl/benzoyltransferase, deacetylvindoline 4-O-acetyltransferase superfamily of acyltransferases and is structurally similar to hydroxycinnamoyl transferase. Using molecular docking, we propose a mechanism for its catalytic activity, and using heterologous expression in tobacco leaves (Nicotiana benthamiana), we demonstrate that expression of BOS in the presence of its substrates is sufficient for beta-ODAP production in vivo. The identification of BOS may pave the way toward engineering beta-ODAP-free grass pea cultivars, which are safe for human and animal consumption.

1 aGoldsmith, Moshe1 aBarad, Shiri1 aKnafo, Maor1 aSavidor, Alon1 aBen-Dor, Shifra1 aBrandis, Alexander1 aMehlman, Tevie1 aPeleg, Yoav1 aAlbeck, Shira1 aDym, Orly1 aBen-Zeev, Efrat1 aBarbole, Ranjit, S.1 aAharoni, Asaph1 aReich, Ziv uhttps://library.ncl.res.in/content/identification-and-characterization-key-enzyme-biosynthesis-neurotoxin-beta-odap-grass-pea01182nas a2200169 4500008004100000245014600041210006900187260000900256490000700265520050900272100002400781700002000805700001800825700002000843700002200863856012700885 2024 eng d00aArticle chitinase inhibition induces transcriptional dysregulation altering ecdysteroid-mediated control of spodoptera frugiperda development0 aArticle chitinase inhibition induces transcriptional dysregulati cMAR 0 v273 a

Chitinases and ecdysteroid hormones are vital for insect development. Crosstalk between chitin and ecdysteroid metabolism regulation is enigmatic. Here, we examined chitinase inhibition effect on Spodopsilencing and overexpression resulted in ecdysone receptor deregulation. Transcription factors, like Neverland, and other ecdysteroid biosynthesis genes might lead to their upregulation in berberine-fed chitinase activity's impact on ecdysone biosynthesis and its transcriptional crosstalk.

1 aBarbole, Ranjit, S.1 aSharma, Shivani1 aPatil, Yogita1 aGiri, Ashok, P.1 aJoshi, Rakesh, S. uhttps://library.ncl.res.in/content/article-chitinase-inhibition-induces-transcriptional-dysregulation-altering-ecdysteroid02460nas a2200241 4500008004100000022001400041245014600055210006900201260000900270300001100279490000800290520157900298653001901877653002901896653002301925653003201948653001401980653002701994100002402021700002202045700002002067856013102087 2024 eng d a0006-291X00aEngineering inhibitory repeat domains of Pin-II type proteinase inhibitors indicate their high structural-functional tolerance to mutagenesis0 aEngineering inhibitory repeat domains of PinII type proteinase i cNOV  a1508080 v7353 a

Plant proteinase inhibitors (PIs) are critical in defending against biotic stress. Most PIs contain an inhibitory repeat domain (IRD), which serves as the functional component, displaying a high degree of sequence and structural conservation. In this study, we examined the structural and functional resilience of IRDs using a combination of computational modeling and experimental validation. We have taken an evolution-based approach to enhance the PIs effectiveness of two previously identified Capsicum annuum IRDs, IRD4 and IRD10. Through in silico site-saturation mutagenesis of IRD4 and IRD10, we identified key sites associated with enhanced PI activity for targeted mutagenesis. Binding energy predictions for a mutant IRD library, tested against target proteases, suggested that positions R11 and N32 in IRD4 and N32 and H33 in IRD10 were promising candidates for further modification to improve inhibitory potential. Subsequent experimental validation revealed that the mutant proteins IRD4_R11K and IRD4_N32S exhibited stronger chymotrypsin inhibition than the wild-type (WT) IRD4. Similarly, the mutants IRD10_N32S and IRD10_H33 N demonstrated improved trypsin inhibition relative to the WT IRD10. These findings indicate that engineered IRD variants can tolerate structural changes while maintaining or enhancing their inhibitory activity against target proteases. Overall, this study demonstrates the potential of engineering PIs to increase their structural and functional resilience, offering new opportunities for biotechnological applications.

10aCapsicum annum10aInhibitory repeat domain10amolecular modeling10aplant proteinase inhibitors10aProteases10aSaturation mutagenesis1 aBarbole, Ranjit, S.1 aJoshi, Rakesh, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/engineering-inhibitory-repeat-domains-pin-ii-type-proteinase-inhibitors-indicate-their-high00725nas a2200217 4500008004100000245008400041210007000125260000800195300000900203490000700212100002100219700001600240700002300256700001900279700002000298700001600318700002000334700002400354700001500378856011400393 2024 eng d00aLsBOS utilizes oxalyl-CoA produced by LsAAE3 to synthesize β-ODAP in grass pea0 aLsBOS utilizes oxalylCoA produced by LsAAE3 to synthesize βODAP  cAUG a67150 v151 aGoldsmith, Moshe1 aAvram, Liat1 aBrandis, Alexander1 aMehlman, Tevie1 aBen-Dor, Shifra1 aPeleg, Yoav1 aBen-Zeev, Efrat1 aBarbole, Ranjit, S.1 aReich, Ziv uhttps://library.ncl.res.in/content/lsbos-utilizes-oxalyl-coa-produced-lsaae3-synthesize-%CE%B2-odap-grass-pea