02961nas a2200217 4500008004100000022001400041245017900055210006900234260008000303300001400383490000800397520206000405100002002465700002202485700002602507700002202533700002002555700001702575700002102592856013002613 2006 eng d a0032-088900aMolecular interactions between the specialist herbivore Manduca sexta (Lepidoptera, Sphingidae) and its natural host Nicotiana attenuata. VII. changes in the plant's proteome0 aMolecular interactions between the specialist herbivore Manduca  a15501 MONONA DRIVE, ROCKVILLE, MD 20855 USAbAMER SOC PLANT BIOLOGISTScDEC a1621-16410 v1423 a

When Manduca sexta attacks Nicotiana attenuata, fatty acid-amino acid conjugates (FACs) in the larvae's oral secretions (OS) are introduced into feeding wounds. These FACs trigger a transcriptional response that is similar to the response induced by insect damage. Using two-dimensional gel electrophoresis, matrix-assisted laser desorption ionization-time of flight, and liquid chromatography-tandem mass spectrometry, we characterized the proteins in phenolic extracts and in a nuclear fraction of leaves elicited by larval attack, and/or in leaves wounded and treated with OS, FAC-free OS, and synthetic FACs. Phenolic extracts yielded approximately 600 protein spots, many of which were altered by elicitation, whereas nuclear protein fractions yielded approximately 100 spots, most of which were unchanged by elicitation. Reproducible elicitor-induced changes in 90 spots were characterized. In general, proteins that increased were involved in primary metabolism, defense, and transcriptional and translational regulation; those that decreased were involved in photosynthesis. Like the transcriptional defense responses, proteomic changes were strongly elicited by the FACs in OS. A semiquantitative reverse transcription-PCR approach based on peptide sequences was used to compare transcript and protein accumulation patterns for 17 candidate proteins. In six cases the patterns of elicited transcript accumulation were consistent with those of elicited protein accumulation. Functional analysis of one of the identified proteins involved in photosynthesis, RuBPCase activase, was accomplished by virus-induced gene silencing. Plants with decreased levels of RuBPCase activase protein had reduced photosynthetic rates and RuBPCase activity, and less biomass, responses consistent with those of herbivore-attacked plants. We conclude that the response of the plant's proteome to herbivore elicitation is complex, and integrated transcriptome-proteome-metabolome analysis is required to fully understand this ubiquitous ecological interaction.

1 aGiri, Ashok, P.1 aWuensche, Hendrik1 aMitra, Sirsha, Sribas1 aZavala, Jorge, A.1 aMuck, Alexander1 aSvatos, Ales1 aBaldwin, Ian, T. uhttps://library.ncl.res.in/content/molecular-interactions-between-specialist-herbivore-manduca-sexta-lepidoptera-sphingidae-002593nas a2200277 4500008004100000022001400041245009700055210006900152260007100221300001400292490000700306520162800313653001601941653001701957653001601974653001601990653001502006653002602021100002302047700002402070700002802094700002602122700002102148700002002169856012602189 2013 eng d a1535-389300aMolecular insights into resistance mechanisms of lepidopteran insect pests against toxicants0 aMolecular insights into resistance mechanisms of lepidopteran in a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcNOV a4727-47370 v123 a

Insect pests remain a major reason for crop loss worldwide despite extensive use of chemical insecticides. More than B 50% of all insecticides are organophosphates, followed by synthetic pyrethroids, organochlorines, carbamates, and biopesticides, and their continued use may have many environmental, agricultural, medical, and socioeconomic issues. Importantly, only a countable number of insects have acquired the status of crop pests, mostly due to monoculture of crop plants and polyphagous nature of the insects. We focus on A adaptations of Lepidopteran insects to phytochemicals and synthetic pesticides in native and modern agricultural systems. Because of heavy use of chemical insecticides, a strong selection pressure is imposed on insect populations, resulting in the emergence of resistance against candidate compound(s). Current knowledge suggests that insects generally implement a three-tier system to overcome the effect of toxic compounds at physiological, biochemical, and genetic levels. Furthermore, we have discussed whether the adaptation to phytochemicals provides an advantage to the insect while encountering synthetic insecticide molecules. Specific metabolic pathways employed by insects to convert deterrents into less toxic forms or their removal from the system are highlighted. Using the proteomics approach, insect proteins interacting with insecticides can be identified, and their modification in resistant insects can be characterized. Also, systems biology studies can offer useful cues to decipher the molecular networks participating in the metabolism of detrimental compounds.

10afield crops10ainsect-pests10ainsecticide10aLepidoptera10aproteomics10aresistance mechanisms1 aDawkar, Vishal, V.1 aChikate, Yojana, R.1 aLomate, Purushottam, R.1 aDholakia, Bhushan, B.1 aGupta, Vidya, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/molecular-insights-resistance-mechanisms-lepidopteran-insect-pests-against-toxicants-002495nas a2200277 4500008004100000022001400041245012300055210006900178260010600247300001200353490000800365520149500373653001301868653001801881653001001899653001701909653001201926653001601938100002001954700002601974700002602000700002402026700002002050700002102070856012602091 2015 eng d a0031-942200aMetabolic profiling of chickpea-Fusarium interaction identifies differential modulation of disease resistance pathways0 aMetabolic profiling of chickpeaFusarium interaction identifies d aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcAUG a120-1290 v1163 a

Chickpea is the third most widely grown legume in the world and mainly used as a vegetarian source of human dietary protein. Fusarium wilt, caused by Fusarium oxysporum f. sp. ciceri (Foc), is one of the major threats to global chickpea production. Host resistance is the best way to protect crops from diseases; however, in spite of using various approaches, the mechanism of Foc resistance in chickpea remains largely obscure. In the present study, non-targeted metabolic profiling at several time points of resistant and susceptible chickpea cultivars using high-resolution liquid chromatography-mass spectrometry was applied to better understand the mechanistic basis of wilt resistance or susceptibility. Multivariate analysis of the data (OPLS-DA) revealed discriminating metabolites in chickpea root tissue after Foc inoculation such as flavonoids, isoflavonoids, alkaloids, amino acids and sugars. Foc inoculated resistant plants had more flavonoids and isoflavonoids along with their malonyl conjugates. Many antifungal metabolites that were induced after Foc infection viz, aurantion-obstine beta-glucosides and querecitin were elevated in resistant cultivar. Overall, diverse genetic and biochemical mechanisms were operational in the resistant cultivar for Foc defense as compared to the susceptible plant. The resistant chickpea plants employed the above-mentioned metabolic pathways as potential defense strategy against Foc. (C) 2015 Elsevier Ltd. All rights reserved.

10aChickpea10aFusarium wilt10aLC-MS10aMetabolomics10aOPLS-DA10aPhytoalexin1 aKumar, Yashwant1 aDholakia, Bhushan, B.1 aPanigrahi, Priyabrata1 aKadoo, Narendra, Y.1 aGiri, Ashok, P.1 aGupta, Vidya, S. uhttps://library.ncl.res.in/content/metabolic-profiling-chickpea-fusarium-interaction-identifies-differential-modulation-002412nas a2200277 4500008004100000022001400041245011500055210006900170260007900239300001200318490000700330520145300337653001301790653001501803653001201818653001001830653001401840653001301854100002501867700002201892700002601914700002301940700002001963700002101983856013002004 2016 eng d a1073-608500aMolecular cloning and characterization of O-methyltransferase from mango fruit (mangifera indica cv. alphonso)0 aMolecular cloning and characterization of Omethyltransferase fro a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcMAY a340-3500 v583 a

Flavour of ripe Alphonso mango is invariably dominated by the de novo appearance of lactones and furanones during ripening. Of these, furanones comprising furaneol (4-hydroxy-2,5-dimethyl-3(2H)-furanone) and mesifuran (2,5-dimethyl-4-methoxy-3(2H)-furanone) are of particular importance due to their sweet, fruity caramel-like flavour characters and low odour detection thresholds. We isolated a 1056 bp complete open reading frame of a cDNA encoding S-adenosyl-l-methionine-dependent O-methyltransferase from Alphonso mango. The recombinantly expressed enzyme, MiOMTS showed substrate specificity towards furaneol and protocatechuic aldehyde synthesizing mesifuran and vanillin, respectively, in an in vitro assay reaction. A semi-quantitative PCR analysis showed fruit-specific expression of MiOMTS transcripts. Quantitative real-time PCR displayed ripening-related expression pattern of MiOMTS in both pulp and skin of Alphonso mango. Also, early and significantly enhanced accumulation of its transcripts was detected in pulp and skin of ethylene-treated fruits. Ripening-related and fruit-specific expression profile of MiOMTS and substrate specificity towards furaneol is a suggestive of its involvement in the synthesis of mesifuran in Alphonso mango. Moreover, a significant trigger in the expression of MiOMTS transcripts in ethylene-treated fruits point towards the transcriptional regulation of mesifuran biosynthesis by ethylene.

10aEthylene10aexpression10aFlavour10aMango10aMesifuran10aRipening1 aChidley, Hemangi, G.1 aOak, Pranjali, S.1 aDeshpande, Ashish, B.1 aPujari, Keshav, H.1 aGiri, Ashok, P.1 aGupta, Vidya, S. uhttps://library.ncl.res.in/content/molecular-cloning-and-characterization-o-methyltransferase-mango-fruit-mangifera-indica-cv02635nas a2200229 4500008004100000022001400041245012200055210006900177260000800246300001100254490000900265520184800274653001602122653001802138653002802156653001102184653002702195100002202222700002202244700002002266856011902286 2020 eng d a0304-416500aMolecular determinant for specificity: differential interaction of alpha-amylases with their proteinaceous inhibitors0 aMolecular determinant for specificity differential interaction o cDEC a1297030 v18643 a

Background: alpha-Amylase inhibitors (alpha-AIs) belong to the discrete classes, and exhibited differential specificities against alpha-amylases from various sources. Several alpha-amylases and their complexes with inhibitors at the molecular level have been studied in detail. Interestingly, some alpha-AIs depict specific and selective interactions amid different insect alpha-amylases. Scope of review: There are studies to understand evolutionary variability and functional differentiation of insect alpha-amylases and their cognate inhibitors. We have examined sequence, structural, and interaction diversity between various alpha-amylases and alpha-AIs. Based on these analyses, we are providing a potential basis for the functional differentiation among certain insect a-amylases concerning mammalian counterparts and their interactions with different proteinaceous alpha-AIs. Major conclusions: Insect alpha-amylases have conserved domain architecture with differences in length, number of disulfide bonds, and secondary structure. Furthermore, few of them exhibit variable characteristics like chloride dependent activity, the presence of N-terminal glutamine residue to protect against proteolytic degradation, and loop variations near the enzyme active site. Conformation of alpha-AI protein could be an essential factor for their specificity and binding affinities towards target alpha-amylase(s). Furthermore, variation into the enzyme binding pocket residues might contribute to differential interactions with inhibitors. General significance: Molecular insights in the interactions between insect alpha-amylases and plant alpha-AI will provide the details of mechanisms assisting the inhibitor specificity. Furthermore, this information will help to design potent and effective alpha-AIs against specific alpha-amylase.

10aActive site10aalpha-amylase10aalpha-amylase inhibitor10aInsect10amolecular interactions1 aRane, Ashwini, S.1 aJoshi, Rakesh, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/molecular-determinant-specificity-differential-interaction-alpha-amylases-their02489nas a2200241 4500008004100000022001400041245010400055210006900159260000800228300001400236490000800250520167700258653001801935653002801953653001801981653001501999653001702014100002202031700002102053700002202074700002002096856013102116 2020 eng d a0141-813000aMolecular investigation of coleopteran specific alpha-amylase inhibitors from amaranthaceae members0 aMolecular investigation of coleopteran specific alphaamylase inh cNOV a1444-14500 v1633 a

alpha-Amylase inhibitors (alpha-AIs) target alpha-amylases and interfere with the carbohydrate digestion of insects. Among different classes of alpha-AIs, a knottin-type inhibitor from Amaranthus hypochondriacus (AhAI) was found to be specific against coleopteran storage pests. In this report, we have characterized three previously unidentified knottin-type alpha-AIs from various Amaranthaceae plants namely, Amaranthus hypochondriacus (AhAI2), Alternanthera sessilis (AsAI) and Chenopodium quinoa (CqAI). They contain a signal peptide, pro-peptide, and mature peptide. The mature peptides of the new alpha-AIs shared 68 to 78% identity with AhAI and have highly variable pro-peptide regions. Along with the cystine-knot fold, they showed conservation of reactive site residues. All recombinant alpha-AIs were successfully expressed in their active form and native state using an oxidative cytoplasmic environment. Inhibition studies against various amylases revealed that these inhibitors showed selective inhibition of coleopteran recombinant insect alpha-amylases viz., Tribolium castaneum, and Callosobruchus chinensis. Tribolium castaneum alpha-amylase inhibition potency was highest for AhAI2 (Ki similar to 15 mu M) followed by AsAI (Ki similar to 43 mu M) and CqAI (Ki similar to 61 mu M). Interaction analysis of these inhibitors illustrated that the reactive site of inhibitors make several non-covalent interactions with the substrate-binding pocket of coleopteran alpha-amylases. The selectivity of these inhibitors against coleopteran a-amylases highlights their potential in storage grain pest control. (C) 2020 Elsevier B.V. All rights reserved.

10aalpha-amylase10aalpha-amylase inhibitor10aAmaranthaceae10aColeoptera10aKnottin-type1 aRane, Ashwini, S.1 aVenkatesh, Varun1 aJoshi, Rakesh, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/molecular-investigation-coleopteran-specific-alpha-amylase-inhibitors-amaranthaceae-members02333nas a2200289 4500008004100000022001400041245007800055210006900133260000800202300001100210490000800221520142300229653001401652653002401666653002401690653002201714653003301736653002201769100001801791700001601809700002401825700002201849700002001871700002501891700002001916856010701936 2024 eng d a0141-813000aMulti-dimensional impact of captopril modification on human serum albumin0 aMultidimensional impact of captopril modification on human serum cAUG a1332890 v2743 a

Captopril is a thiol drug, widely used for the management of hypertension and cardiovascular diseases. Reactive thiols are found to covalently modify the cysteines of plasma proteins and affect their structure and function. Human serum albumin (HSA) is prone to undergo modification by various low molecular weight compounds, including drugs. Cysteine34 (Cys34) in HSA has a free thiol group with antioxidant properties, considered to be the most redox-sensitive amino acid in plasma. Through mass-spectrometric analysis, we demonstrate for the first time that captopril forms a disulfide adduct at Cys34 residue and increases the protease susceptibility of HSA to trypsin. As evidenced by our biophysical and electron microscopy studies, HSA undergoes structural alteration, aggregation and morphological changes when treated with different captopril concentrations. Molecular dynamics studies further revealed the regions of secondary structural changes in HSA due to disulfide adduct formation by captopril at Cys34. It also elucidated the residues involved in the noncovalent interactions with captopril. It is envisaged that structural change in HSA may influence the efficacy of drug delivery as well as its own biological function. These findings may thus provide significant insights into the field of pharmacology intriguing further investigation into the effects of long-term captopril treatment.

10aCaptopril10aElectron microscopy10aHuman serum albumin10aMass spectrometry10aMolecular dynamic simulation10aSpectrophotometry1 aGhosh, Amrita1 aJani, Vinod1 aSonavane, Uddhavesh1 aNaphade, Anvi, N.1 aJoshi, Rajendra1 aKulkarni, Mahesh, J.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/multi-dimensional-impact-captopril-modification-human-serum-albumin02001nas a2200253 4500008004100000022001400041245012600055210006900181260000800250300001100258490000800269520115500277653001401432653001201446653001601458653001601474653001401490653002601504100002401530700002201554700002901576700002001605856012201625 2025 eng d a0141-813000aMYB proteins: Versatile regulators of plant development, stress responses, and secondary metabolite biosynthetic pathways0 aMYB proteins Versatile regulators of plant development stress re cFEB a1385880 v2883 a

MYB proteins are ubiquitous in nature, regulating key aspects of plant growth and development. Although MYB proteins are known for regulating genes involved in secondary metabolite biosynthesis, particularly phenylpropanoids, their roles in terpenoid, glucosinolate, and alkaloid biosynthesis remain less understood. This review explores the structural and functional differences between activator and repressor MYB proteins along with their roles in plant growth, development, stress responses, and secondary metabolite production. MYB proteins serve as central hubs in protein-protein interaction networks that regulate expression of numerous genes involved in the adaptation of plants to varying environmental conditions. Thus, we also highlight key interacting partners of MYB proteins and their roles in these adaptation mechanisms. We further discuss the mechanisms regulating MYB proteins, including autoregulation, epigenetics, and post-transcriptional and post-translational modifications. Overall, we propose MYB proteins as versatile regulators for improving plant traits, stress responses, and secondary metabolite production.

10aActivator10adefense10aDevelopment10aMYB protein10aRepressor10aSecondary metabolites1 aBhatt, Preshita, A.1 aGurav, Tanuja, P.1 aKondhare, Kirtikumar, R.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/myb-proteins-versatile-regulators-plant-development-stress-responses-and-secondary