02058nas a2200229 4500008004100000022001400041245012000055210006900175260010600244300001200350490000700362520113700369653001301506653004101519653002801560653003201588100001901620700002001639700002401659700002101683856012401704 2005 eng d a0022-191000aCharacterization of two midgut proteinases of helicoverpa armigera and their interaction with proteinase inhibitors0 aCharacterization of two midgut proteinases of helicoverpa armige aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcMAY a513-5220 v513 a

Two serine proteinases from the midgut of Helicoverpa armigera have been partially purified and characterized. One proteinase, HGP-1, was capable of hydrolyzing a synthetic substrate of elastase and was inhibited by elastatinal. The second proteinase, HGP-2, was inhibited by a trypsin inhibitor. Molecular weights of HGP-1 and HGP-2 were approximately 26.0 and 29.0 kDa, respectively. Both the proteinases exhibited alkaline pH optima in the range of 10-11. Furthermore, interaction of HGP-1 and HGP-2 with proteinase inhibitors (PIs) from host and non-host plants was studied. HGP-1 was not only insensitive to a PI from chickpea (host) but was also able to degrade it. The same PI from chickpea was able to inhibit over 50% activity of HGP-2. On the contrary, PIs from potato (non-host) showed strong inhibition of both, HGP-1 and HGP-2 and also demonstrated protection of chickpea seed proteins from digestion by both the HGPs. These results could provide important clues in designing strategies for sustainable use of plant PIs in developing insect-tolerant transgenic plants. (C) 2005 Elsevier Ltd. All rights reserved.

10aelastase10aHelicoverpa armigera gut proteinases10ainsect-resistant plants10aplant proteinase inhibitors1 aTelang, M., A.1 aGiri, Ashok, P.1 aSainani, Mohini, N.1 aGupta, Vidya, S. uhttps://library.ncl.res.in/content/characterization-two-midgut-proteinases-helicoverpa-armigera-and-their-interaction-002339nas a2200313 4500008004100000022001400041245009400055210006900149260009800218300001400316490000700330520125300337653001101590653002301601653002101624653001901645653002301664653001001687100002201697700002201719700002501741700002001766700002301786700002501809700002201834700002501856700002101881856012301902 2009 eng d a0022-514200aChanges in volatile composition during fruit development and ripening of `Alphonso' mango0 aChanges in volatile composition during fruit development and rip aTHE ATRIUM, SOUTHERN GATE, CHICHESTER PO19 8SQ, W SUSSEX, ENGLANDbJOHN WILEY & SONS LTDcSEP a2071-20810 v893 a

BACKGROUND: Volatile blends of five developing and five ripening stages of mango (Mangifera indica L. cv. Alphonso) were investigated along with those of flowers and leaves. Raw and ripe fruits of cv. Sabia were also used for comparison. RESULTS: A total of 55 volatiles belonging to various chemical classes such as aldehydes, alcohols, mono- and sesquiterpene hydrocarbons, lactones and furanones were identified. In all Alphonso tissues monoterpenes quantitatively dominated, with 57-99% contribution; in particular, (Z)-ocimene was found in the highest amount. Ripeness was characterized by the de novo appearance of lactones and furanones in the blend of monoterpenes. Sabja was distinguished by the abundance of monoterpene hydrocarbons in the raw fruit, and that of sesquiterpene hydrocarbons and their derivatives in the ripe stage. CONCLUSION: Various stages of the Alphonso fruit during transition from flower to ripe fruit are characterized by unique volatile signatures that are distinguished from each other by the qualitative and quantitative appearance of different volatile compounds. Thus volatiles can be highly informative markers while studying the development and ripening of mango. (C) 2009 Society of Chemical Industry

10aDeogad10aGas chromatography10aMangifera indica10amango products10aripening indicator10aSabja1 aPandit, Sagar, S.1 aKulkarni, Ram, S.1 aChidley, Hemangi, G.1 aGiri, Ashok, P.1 aPujari, Keshav, H.1 aKoellner, Tobias, G.1 aDegenhardt, Joerg1 aGershenzon, Jonathan1 aGupta, Vidya, S. uhttps://library.ncl.res.in/content/changes-volatile-composition-during-fruit-development-and-ripening-alphonso-mango-002069nas a2200265 4500008004100000022001400041245006900055210006900124260009900193300001200292490000800304520117400312653001201486653001001498653002101508653002601529653001501555100002201570700002501592700002201617700002301639700002001662700002101682856010001703 2009 eng d a0308-814600aCultivar relationships in mango based on fruit volatile profiles0 aCultivar relationships in mango based on fruit volatile profiles aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcMAY a363-3720 v1143 a

Aroma volatiles of mango (Mangifera indica L.) determine consumer acceptability and influence selection, whilst breeding. To assess their variety, composition and possible impact on cultivar relationships, volatile blends of 22 Indian and five non-Indian cultivars were investigated using solvent extraction and gas chromatography. Totally 84 volatiles belonging to various chemical classes were detected. Based on the Cumulative Occurrence of members of these classes, cultivars were grouped as monoterpene or sesquiterpene dominant. a-Pinene, beta-myrcene and beta-caryophyllene were found in all 27 cultivars. For ordination, common compounds with high (relative) concentration provided quantitative characters, whereas the rare and lesser ones provided qualitative (binary) characters; non-Indian cultivars separated from Indian ones but displayed close relations within their groups. In conclusion, mango flavour is dominated qualitatively as well as quantitatively by terpene hydrocarbons; ancient selection of mango cultivars is hinted to be driven by different aroma characters in different parts of the world. (C) 2008 Elsevier Ltd. All rights reserved.

10aFlavour10aGC-MS10aMangifera indica10aMultivariate analysis10aOrdination1 aPandit, Sagar, S.1 aChidley, Hemangi, G.1 aKulkarni, Ram, S.1 aPujari, Keshav, H.1 aGiri, Ashok, P.1 aGupta, Vidya, S. uhttps://library.ncl.res.in/content/cultivar-relationships-mango-based-fruit-volatile-profiles-002840nas a2200241 4500008004100000022001400041245009000055210006900145260008100214300000700295490000700302520195400309653001902263653002402282653002102306653002602327653002902353100002602382700002802408700002002436700002502456856011702481 2013 eng d a1471-209100aCharacterization of a chemostable serine alkaline protease from Periplaneta americana0 aCharacterization of a chemostable serine alkaline protease from  a236 GRAYS INN RD, FLOOR 6, LONDON WC1X 8HL, ENGLANDbBIOMED CENTRAL LTDcNOV a320 v143 a

Background: Proteases are important enzymes involved in numerous essential physiological processes and hold a strong potential for industrial applications. The proteolytic activity of insects' gut is endowed by many isoforms with diverse properties and specificities. Thus, insect proteases can act as a tool in industrial processes. Results: In the present study, purification and properties of a serine alkaline protease from Periplaneta americana and its potential application as an additive in various bio-formulations are reported. The enzyme was purified near to homogeneity by using acetone precipitation and Sephadex G-100 gel filtration chromatography. Enzyme activity was increased up to 4.2 fold after gel filtration chromatography. The purified enzyme appeared as single protein-band with a molecular mass of similar to 27.8 kDa in SDS-PAGE. The optimum pH and temperature for the proteolytic activity for purified protein were found around pH 8.0 and 60 degrees C respectively. Complete inhibition of the purified enzyme by phenylmethylsulfonyl fluoride confirmed that the protease was of serine-type. The purified enzyme revealed high stability and compatibility towards detergents, oxidizing, reducing, and bleaching agents. In addition, enzyme also showed stability towards organic solvents and commercial detergents. Conclusion: Several important properties of a serine protease from P. Americana were revealed. Moreover, insects can serve as excellent and alternative source of industrially important proteases with unique properties, which can be utilized as additives in detergents, stain removers and other bio-formulations. Properties of the P. americana protease accounted in the present investigation can be exploited further in various industrial processes. As an industrial prospective, identification of enzymes with varying essential properties from different insect species might be good approach and bioresource.

10aChemostability10aIndustrial catalyst10aInsect proteases10aPeriplaneta americana10aSerine alkaline protease1 aSanatan, Prashant, T.1 aLomate, Purushottam, R.1 aGiri, Ashok, P.1 aHivrale, Vandana, K. uhttps://library.ncl.res.in/content/characterization-chemostable-serine-alkaline-protease-periplaneta-americana-002972nas a2200313 4500008004100000022001400041245010400055210006900159260010300228300001200331490000700343520187800350653001302228653002102241653001002262653003502272653002102307653002202328100001802350700001802368700002502386700001902411700001802430700002502448700001902473700002002492700001702512856012902529 2013 eng d a0981-942800aCharacterization of three novel isoprenyl diphosphate synthases from the terpenoid rich mango fruit0 aCharacterization of three novel isoprenyl diphosphate synthases  a23 RUE LINOIS, 75724 PARIS, FRANCEbELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIERcOCT a121-1310 v713 a

Mango (cv. Alphonso) is popular due to its highly attractive, terpenoid-rich flavor. Although Alphonso is clonally propagated, its fruit-flavor composition varies when plants are grown in different geo-climatic zones. Isoprenyl diphosphate synthases catalyze important branch-point reactions in terpenoid biosynthesis, providing precursors for common terpenoids such as volatile terpenes, sterols and carotenoids. Two geranyl diphosphate synthases and a farnesyl diphosphate synthase were isolated from Alphonso fruits, cloned for recombinant expression and found to produce the respective products. Although, one of the geranyl diphosphate synthases showed high sequence similarity to the geranylgeranyl diphosphate synthases, it did not exhibit geranylgeranyl diphosphate synthesizing activity. When modeled, this geranyl diphosphate synthase and farnesyl diphosphate synthase structures were found to be homologous with the reference structures, having all the catalytic side chains appropriately oriented. The optimum temperature for both the geranyl diphosphate synthases was 40 degrees C and that for farnesyl diphosphate synthase was 25 degrees C. This finding correlated well with the dominance of monoterpenes in comparison to sesquiterpenes in the fruits of Alphonso mango in which the mesocarp temperature is higher during ripening than development. The absence of activity of these enzymes with the divalent metal ion other than Mg2+ indicated their adaptation to the Mg2+ rich mesocarp. The typical expression pattern of these genes through the ripening stages of fruits from different cultivation localities depicting the highest transcript levels of these genes in the stage preceding the maximum terpene accumulation indicated the involvement of these genes in the biosynthesis of volatile terpenes. (C) 2013 Elsevier Masson SAS. All rights reserved.

10aAlphonso10aFlavor variation10aFruit10aIsoprenyl diphosphate synthase10aMangifera indica10aTerpene volatiles1 aKulkarni, Ram1 aPandit, Sagar1 aChidley, Hemangi, G.1 aNagel, Raimund1 aSchmidt, Axel1 aGershenzon, Jonathan1 aPujari, Keshav1 aGiri, Ashok, P.1 aGupta, Vidya uhttps://library.ncl.res.in/content/characterization-three-novel-isoprenyl-diphosphate-synthases-terpenoid-rich-mango-fruit-002516nas a2200265 4500008004100000022001400041245012500055210006900180260007300249300001400322490000900336520153000345653001901875653002101894653003601915653001301951653002301964653003201987100002202019700001902041700001902060700002102079700002002100856013002120 2013 eng d a0304-416500aComplementation of intramolecular interactions for structural-functional stability of plant serine proteinase inhibitors0 aComplementation of intramolecular interactions for structuralfun aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcNOV a5087-50940 v18303 a

Background: Plant protease inhibitors (PIs) constitute a diverse group of proteins capable of inhibiting proteases. Among Pls, serine Pls (SPIs) display stability and conformational restrictions of the reactive site loop by virtue of their compact size, and by the presence of disulfide bonds, hydrogen bonds, and other weak interactions. Scope of review: The significance of various intramolecular interactions contributing to protein folding mechanism and their role in overall stability and activity of SPIs is discussed here. Furthermore, we have reviewed the effect of variation or manipulation of these interactions on the activity/stability of SPIs. Major conclusions: The selective gain or loss of disulfide bond(s) in SPIs can be associated with their functional differentiation, which is likely to be compensated by non-covalent interactions (hydrogen bonding or electrostatic interactions). Thus, these intramolecular interactions are collectively responsible for the functional activity of SPIs, through the maintenance of scaffold framework, conformational rigidity and shape complementarities of reactive site loop. General significance: Structural insight of these interactions will provide an in-depth understanding of kinetic and thermodynamic parameters involved in the folding and stability mechanisms of SPIs. These features can be explored for engineering canonical SPIs for optimizing their overall stability and functionality for various applications. (C) 2013 Elsevier B.V. All rights reserved.

10aDisulfide bond10ahydrogen bonding10aIntramolecular weak interaction10aProtease10aReactive site loop10aSerine proteinase inhibitor1 aJoshi, Rakesh, S.1 aMishra, Manasi1 aSuresh, C., G.1 aGupta, Vidya, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/complementation-intramolecular-interactions-structural-functional-stability-plant-serine-001985nas a2200265 4500008004100000022001400041245006200055210006100117260010600178300001000284490000700294520110800301653001401409653001401423653003201437653001601469653001601485653001701501653002001518100002201538700002201560700002201582700002001604856009501624 2015 eng d a0965-174800aCathepsins of lepidopteran insects: aspects and prospects0 aCathepsins of lepidopteran insects aspects and prospects aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcSEP a51-590 v643 a

Molecular understanding of lepidopteran physiology has revealed that proteases consist of one of the central regulatory/reacting system for insect growth and survival. Among the various proteases, cathepsins are the most crucial cellular proteases, which play vital roles during insect development. In the present review, we have discussed various aspects of the lepidopteran insect cathepsins, emphasizing their roles in processes like development, growth, metamorphosis, apoptosis and immunity. Cathepsins are categorized into different types on the basis of their sequence diversification, leading to variation in structure and catalytic function. Cathepsins exhibit tissue and stage specific expression pattern which is fine-tuned by a delicate balance of expression, compartmentalization, zymogen activation, inhibition by protein inhibitors and degradation. The indispensability of cathepsins as cellular proteases in the above mentioned processes proposes them as novel targets for designing effective and specific insect controlling strategies. (C) 2015 Elsevier Ltd. All rights reserved.

10aApoptosis10aCathepsin10aCysteine/aspartate protease10aDevelopment10aLepidoptera10aPest control10aStress response1 aSaikhedkar, Nidhi1 aSummanwar, Aarohi1 aJoshi, Rakesh, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/cathepsins-lepidopteran-insects-aspects-and-prospects-002071nas a2200181 4500008004100000245008400041210006900125260000800194300001200202490000800214520144300222100002201665700002401687700002601711700002001737700002101757856011101778 2016 eng d00aCharacterization of roseomonas and nocardioides spp. for arsenic transformation0 aCharacterization of roseomonas and nocardioides spp for arsenic  cNOV a742-7500 v3183 aThe metalloid arsenic predominantly exists in the arsenite [As(III)] and arsenate [As(V)]. These two forms are respectively oxidized and reduced by microbial redox processes. This study was designed to bioprospect arsenic tolerating bacteria from Lonar lake and to characterize their arsenic redoxing ability. Screening of sixty-nine bacterial species isolated from Lonar lake led to identification of three arsenic oxidizing and seven arsenic-reducing species. Arsenite oxidizing isolate Roseomonas sp. L-159a being closely related to Roseomonas cervicalis ATCC 49957 oxidized 2 mM As(III) in 60 h. Gene expression of large and small subunits of arsenite oxidase respectively showed 15- and 17-fold higher expression. Another isolate Nocardioides sp. L-37a formed a clade with Nocardioides ghangwensis JC2055, exhibited normal growth with different carbon sources and pH ranges. It reduced 2 mM As(V) in 36 h and showed constitutive expression of arsenate reductase which increased over 4-fold upon As(V) exposure. Genetic markers related to arsenic transformation were identified and characterized from the two isolates. Moderate resistance against the arsenicals was exhibited by the two isolates in the range of 1-5 mM for As(III) and 1-200 mM for As(V). Altogether we provide multiple evidences to indicate that Roseomonas sp. and Nocardioides sp. exhibited arsenic transformation ability. (C) 2016 Elsevier B.V. All rights reserved.1 aBagade, Aditi, V.1 aBachate, Sachin, P.1 aDholakia, Bhushan, B.1 aGiri, Ashok, P.1 aKodam, Kisan, M. uhttps://library.ncl.res.in/content/characterization-roseomonas-and-nocardioides-spp-arsenic-transformation02696nas a2200301 4500008004100000022001400041245016000055210006900215260010600284300000900390490000700399520155800406653001301964653001801977653002801995653002902023653001502052653002402067100002402091700002002115700001902135700002002154700002202174700002302196700002602219700002002245856012902265 2016 eng d a0965-174800aCharacterization of two coleopteran alpha-amylases and molecular insights into their differential inhibition by synthetic alpha-amylase inhibitor, acarbose0 aCharacterization of two coleopteran alphaamylases and molecular  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcJUL a1-110 v743 a

Post-harvest insect infestation of stored grains makes them unfit for human consumption and leads to severe economic loss. Here, we report functional and structural characterization of two coleopteran alpha-amylases viz. Callosobruchus chinensis alpha-amylase (CcAmy) and Tribolium castaneum alpha-amylase (TcAmy) along with their interactions with proteinaceous and non-proteinaceous alpha-amylase inhibitors. Secondary structural alignment of CcAmy and TcAmy with other coleopteran alpha-amylases revealed conserved motifs, active sites, di-sulfide bonds and two point mutations at spatially conserved substrate or inhibitor binding sites. Homology modeling and molecular docking showed structural differences between these two enzymes. Both the enzymes had similar optimum pH values but differed in their optimum temperature. Overall, pattern of enzyme stabilities were similar under various temperature and pH conditions. Further, CcAmy and TcAmy differed in their substrate affinity and catalytic efficiency towards starch and amylopectin. HPLC analysis detected common amylolytic products like maltose and maltotriose while glucose and malto-tetrose were unique in CcAmy and TcAmy catalyzed reactions respectively. At very low concentrations, wheat alpha-amylase inhibitor was found to be superior over the acarbose as far as complete inhibition of amylolytic activities of CcAmy and TcAmy was concerned. Mechanism underlying differential amylolytic reaction inhibition by acarbose was discussed. (C) 2016 Elsevier Ltd. All rights reserved.

10aAcarbose10aalpha-amylase10aalpha-amylase inhibitor10aCallosobruchus chinensis10aColeoptera10aTribolium castaneum1 aChannale, Sonal, M.1 aBhide, Amey, J.1 aYadav, Yashpal1 aKashyap, Garima1 aPawar, Pankaj, K.1 aMaheshwari, V., L.1 aRamasamy, Sureshkumar1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/characterization-two-coleopteran-alpha-amylases-and-molecular-insights-their-differential02690nas a2200253 4500008004100000245013700041210006900178260000800247300001400255490000900269520176500278100001602043700002902059700002502088700002402113700002202137700002202159700002602181700002402207700002202231700003702253700002002290856012602310 2016 eng d00aComparative functional characterization of eugenol synthase from four different ocimum species: implications on eugenol accumulation0 aComparative functional characterization of eugenol synthase from cNOV a1539-15470 v18643 a

Isoprenoids and phenylpropanoids are the major secondary metabolite constituents in Ocimum genus. Though enzymes from phenylpropanoid pathway have been characterized from few plants, limited information exists on how they modulate levels of secondary metabolites. Here, we performed phenylpropanoid profiling in different tissues from five Ocimum species, which revealed significant variations in secondary metabolites including eugenol, eugenol methyl ether, estragole and methyl cinnamate levels. Expression analysis of eugenol synthase (EGS) gene showed higher transcript levels especially in young leaves and inflorescence; and were positively correlated with eugenol contents. Additionally, transcript levels of coniferyl alcohol acyl transferase, a key enzyme diverting pool of substrate to phenylpropanoids, were in accordance with their abundance in respective species. In particular, eugenol methyl transferase expression positively correlated with higher levels of eugenol methyl ether in Ocimum tenuiflorum. Further, EGSs were functionally characterized from four Ocimum species varying in their eugenol contents. Kinetic and expression analyses indicated, higher enzyme turnover and transcripts levels, in species accumulating more eugenol. Moreover, biochemical and bioinformatics studies demonstrated that coniferyl acetate was the preferred substrate over coumaryl acetate when used, individually or together, in the enzyme assay. Overall, this study revealed the preliminary evidence for varied accumulation of eugenol and its abundance over chavicol in these Ocimum species. Current findings could potentially provide novel insights for metabolic modulations in medicinal and aromatic plants. (C) 2016 Elsevier B.V. All rights reserved.

1 aAnand, Atul1 aJayaramaiah, Ramesha, H.1 aBeedkar, Supriya, D.1 aSingh, Priyanka, A.1 aJoshi, Rakesh, S.1 aMulani, Fayaj, A.1 aDholakia, Bhushan, B.1 aPunekar, Sachin, A.1 aGade, Wasudeo, N.1 aThulasiram, Hirekodathakallu, V.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/comparative-functional-characterization-eugenol-synthase-four-different-ocimum-species02661nas a2200241 4500008004100000022001400041245022700055210006900282260000900351520169200360653002002052653001002072653002202082653002602104653001902130653002602149100001802175700002602193700002902219700002402248700002002272856012702292 2020 eng d a0721-759500aCombinatorial approach through in vitro regeneration and phytochemical profiling of ceropegia media (huber) ans.: a potential way forward in the conservation of an endangered medicinal plant from the western ghats in India0 aCombinatorial approach through in vitro regeneration and phytoch cJUN 3 a

Ceropegia mediais an endemic and endangered plant as its propagation through seeds is unreliable due to low germination, slow growth and seedling decay under natural conditions. Also, tubers of this plant are edible serving as carbohydrate source with medicinal values leading to severe population decline in the natural habitat. To provide a sustainable solution, an efficient in vitro propagation protocol along with phytochemical profiling was developed forC. media. Callus cultures were induced from seedling and wild leaf tissues using the most effective Murashige and Skoog's (MS) medium with 2,4-dichlorophenoxyacetic acid (2,4-D; 2 mu M) and sucrose (3%). Somatic embryos were acquired on MS medium with 1 mu M 6-Benzylaminopurine (BAP) and 1 mu M 2,4-D. Conversion into plantlets was attained only from tissue culture-derived seedling leaf (TCDSL) explant. Further, in vitro tuberization was achieved from TCDSL callus with BAP and Naphthalene acetic acid (NAA). AgNO(3)as an elicitor had a positive effect on both fresh and dry weights of callus. Successful acclimatization (58%) was attained after two months resulting in normal phenotype in pots. Further, metabolite profiles of ten different tissues from wild and in vitro plants were compared. Total 82 compounds comprising alkaloids, fatty acids, fatty acid ester, steroids, terpenes and hydrocarbons were identified. Overall, results suggested enhanced production of selected metabolites with in vitro propagation and AgNO3, alleviating the problem of unavailability of planting materials. Thus, the current study might offer potential ways for the conservation of such RED enlisted species asC. media. [GRAHICS]

10aCeropegia media10aGC-MS10aMicrotuberization10aSecondary metabolites10aSilver nitrate10asomatic embryogenesis1 aPandey, Meena1 aDholakia, Bhushan, B.1 aJayaramaiah, Ramesha, H.1 aPunekar, Sachin, A.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/combinatorial-approach-through-vitro-regeneration-and-phytochemical-profiling-ceropegia02181nas a2200253 4500008004100000022001400041245012300055210006900178260000800247300001100255490000800266520133300274653001301607653001301620653002201633653001901655653001801674653001501692100002301707700002001730700002701750700002001777856013001797 2022 eng d a0031-942200aCharacterized constituents of insect herbivore oral secretions and their influence on the regulation of plant defenses0 aCharacterized constituents of insect herbivore oral secretions a cJAN a1130080 v1933 aFor more than 350 million years, there have been ongoing dynamic interactions between plants and insects. In several cases, insects cause-specific feeding damage with ensuing herbivore-associated molecular patterns that invoke characteristic defense responses. During feeding on plant tissue, insects release oral secretions (OSs) containing a repertoire of molecules affecting plant defense (effectors). Some of these OS components might elicit a defense response to combat insect attacks (elicitors), while some might curb the plant defenses (suppressors). Few reports suggest that the synthesis and function of OS components might depend on the host plant and associated microorganisms. We review these intricate plant-insect interactions, during which there is a continuous exchange of molecules between plants and feeding insects along with the associated microorganisms. We further provide a list of commonly identified inducible plant produced defensive molecules released upon insect attack as well as in response to OS treatments of the plants. Thus, we describe how plants specialized and defense-related metabolism is modulated at innumerable phases by OS during plant-insect interactions. A molecular understanding of these complex interactions will provide a means to design eco-friendly crop protection strategies.10aEffector10aElicitor10aHerbivore insects10aOral secretion10aPlant defense10aSuppressor1 aKallure, Gopal, S.1 aKumari, Archana1 aShinde, Balkrishna, A.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/characterized-constituents-insect-herbivore-oral-secretions-and-their-influence-regulation02451nas a2200253 4500008004100000022001400041245014700055210006900202260000900271300000800280490000700288520156100295653002801856653002701884653001001911653002501921653001701946100001801963700002601981700002102007700002402028700002002052856012502072 2025 eng d a2190-572X00aComprehensive tissue specific analysis of antioxidant potential and metabolite profiling of a vulnerable therapeutic herb Ceropegia sahyadrica0 aComprehensive tissue specific analysis of antioxidant potential  cNOV  a4340 v153 a

This study investigated tissue-culture of an endangered medicinal herb, Ceropegia sahyadrica, along with tissue-specific variation in antioxidant activity and GC-MS based phytochemical profiling using wild and in vitro explants. In vitro leaf explants exhibited callus induction rate of 100% in Murashige and Skoog media containing 6-benzylaminopurine (4 mu M) and 2,4-dichlorophenoxyacetic acid (2 mu M) with 5% sucrose, whereas in vitro root explant achieved 66.7% with the combination of 2 mu M 6-benzylaminopurine and 1 mu M 2,4-dichlorophenoxyacetic acid in Murashige and Skoog medium. Microtuberization was most pronounced in in vitro root explants with a maximum response of 73.3% in 1 mu M indole-3-acetic acid, 2 mu M 6-benzylaminopurine and 5% sucrose. Scanning electron microscopy imaging revealed distinct cellular organization among tissues. Further, antioxidant potential assessed through 1,1-diphenyl-2-picrylhydrazyl radical scavenging assays and estimated total phenolic content showed metabolic variation and commonality between in vitro and wild tissues. Additionally, phytochemical profiling by gas chromatography-mass spectrometry identified 201 compounds, including alkaloids, fatty acid methyl esters, flavonoids, phytosterols and other bioactive molecules with alterations in metabolite profiles between in vitro and wild tissues. These findings demonstrated that explant origin and culture condition might significantly influence metabolic responses for conservation and ensures a reliable source of bioactive compound.

10aCeropegia- Conservation10aEndemic medicinal herb10aGC-MS10aMetabolite profiling10aTuberization1 aPandey, Meena1 aDholakia, Bhushan, B.1 aSaraf, Purva, S.1 aPunekar, Sachin, A.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/comprehensive-tissue-specific-analysis-antioxidant-potential-and-metabolite-profiling