02341nas a2200265   4500008004100000022001400041245012500055210006900180260005800249300000700307490000700314520143700321653001301758653002301771653001201794653001401806100001901820700002001839700001901859700001901878700001401897700002101911700002001932856012301952       2012                        eng d  a1536-244200aDevelopmental and digestive flexibilities in the midgut of a polyphagous pest, the cotton bollworm, helicoverpa armigera0 aDevelopmental and digestive flexibilities in the midgut of a pol  aLIBRARY C327, TUCSON, AZ 85721 USAbUNIV ARIZONAcMAR  a420 v123 a<p>Developmental patterns and survival of the cotton bollworm, Helicoverpa armigera Hubner (Lepidoptera: Noctuidae), a polyphagous insect pest, have been studied with reference to the effect of diet on major gut digestive enzymes (amylases, proteases, and lipases). Significant correlations between nutritional quality of the diet and larval and pupal mass were observed when H. armigera larvae were fed on various host plants viz. legumes (chickpea and pigeonpea), vegetables (tomato and okra), flowers (rose and marigold), and cereals (sorghum and maize). Larvae fed on diets rich in proteins and/or carbohydrates (pigeonpea, chickpea, maize, and sorghum) showed higher larval mass and developed more rapidly than larvae fed on diets with low protein and carbohydrate content (rose, marigold, okra, and tomato). Low calorific value diets like rose and marigold resulted in higher mortality (25-35%) of H. armigera. Even with highly varying development efficiency and larval/pupal survival rates, H. armigera populations feeding on different diets completed their life cycles. Digestive enzymes of H. armigera displayed variable expression levels and were found to be regulated on the basis of macromolecular composition of the diet. Post-ingestive adaptations operating at the gut level, in the form of controlled release of digestive enzymes, might be a key factor contributing to the physiological plasticity in H. armigera.</p>10aamylases10alarval performance10aLipases10aProteases1 aSarate, P., J.1 aTamhane, V., A.1 aKotkar, H., M.1 aRatnakaran, N.1 aSusan, N.1 aGupta, Vidya, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/developmental-and-digestive-flexibilities-midgut-polyphagous-pest-cotton-bollworm-102205nas a2200229   4500008004100000022001400041245014400055210006900199260010600268300001000374490000800384520127700392653002001669653002501689653002901714653001401743653002601757100002201783700002101805700002001826856012901846       2014                        eng d  a0031-942200aDifferential antibiosis against helicoverpa armigera exerted by distinct inhibitory repeat domains of capsicum annuum proteinase inhibitors0 aDifferential antibiosis against helicoverpa armigera exerted by   aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcMAY  a16-220 v1013 a<p>Plant defensive serine proteinase inhibitors (Pis) are known to have negative impact on digestive physiology of herbivore insects and thus have a crucial role in plant protection. Here, we have assessed the efficacy and specificity of three previously characterized inhibitory repeat domain (IRD) variants from Capsicum annuum PIs viz., IRD-7, -9 and -12 against gut proteinases from Helicoverpa armigera. Comparative study of in silico binding energy revealed that IRD-9 possesses higher affinity towards H. armigera serine proteinases as compared to IRD-7 and -12. H. armigera fed on artificial diet containing 5 TIU/g of recombinant IRD proteins exhibited differential effects on larval growth, survival rate and other nutritional parameters. Major digestive gut trypsin and chymotrypsin genes were down regulated in the IRD fed larvae, while few of them were up-regulated, this indicate alterations in insect digestive physiology. The results corroborated with proteinase activity assays and zymography. These findings suggest that the sequence variations among Pis reflect in their efficacy against proteinases in vitro and in vivo, which also could be used for developing tailor-made multi-domain inhibitor gene(s). (C) 2014 Elsevier Ltd. All rights reserved.</p>10aCapsicum annuum10aHelicoverpa armigera10aInhibitory repeat domain10aProteases10aProteinase inhibitors1 aJoshi, Rakesh, S.1 aGupta, Vidya, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/differential-antibiosis-against-helicoverpa-armigera-exerted-distinct-inhibitory-repeat-002993nas a2200289   4500008004100000022001400041245017700055210006900232260008600301300001000387490000700397520189300404653002002297653002502317653001402342653002502356100002202381700001902403700002802422700001902450700002402469700001902493700002002512700002102532700002002553856013002573       2014                        eng d  a0739-110200aRemarkable efficiency of a pin-II proteinase inhibitor sans two conserved disulfide bonds is due to enhanced flexibility and hydrogen bond density in the reactive site loop0 aRemarkable efficiency of a pinII proteinase inhibitor sans two c  a325 CHESTNUT ST, SUITE 800, PHILADELPHIA, PA 19106 USAbTAYLOR & FRANCIS INCcJAN  a13-260 v323 a<p>Capsicum annuum (L.) expresses diverse potato type II family proteinase inhibitors comprising of inhibitory repeat domain (IRD) as basic functional unit. Most IRDs contain eight conserved cysteines forming four disulfide bonds, which are indispensible for their stability and activity. We investigated the functional significance of evolutionary variations in IRDs and their role in mediating interaction between the inhibitor and cognate proteinase. Among the 18 IRDs encoded by C. annuum, IRD-7, -9, and -12 were selected for further characterization on the basis of variation in their reactive site loop, number of conserved cysteine residues, and higher theoretical G(bind) for interaction with Helicoverpa armigera trypsin. Moreover, inhibition kinetics showed that IRD-9, despite loss of some of the disulfide bonds, was a more potent proteinase inhibitor among the three selected IRDs. Molecular dynamic simulations revealed that serine residues in the place of cysteines at seventh and eighth positions of IRD-9 resulted in an increase in the density of intramolecular hydrogen bonds and reactive site loop flexibility. Results of the serine residues chemical modification also supported this observation and provided a possible explanation for the remarkable inhibitory potential of IRD-9. Furthermore, this natural variant among IRDs showed special attributes like stability to proteolysis and synergistic inhibitory effect on other IRDs. It is likely that IRDs have coevolved selective specialization of their structure and function as a response towards specific insect proteases they encountered. Understanding the molecular mechanism of pest protease-plant proteinaceous inhibitor interaction will help in developing effective pest control strategies.An animated interactive 3D complement (I3DC) is available in Proteopedia at http://proteopedia.org/w/Journal:JBSD:39</p>10aCapsicum annuum10aHelicoverpa armigera10aProteases10aProteinase inhibitor1 aJoshi, Rakesh, S.1 aMishra, Manasi1 aTamhane, Vaijayanti, A.1 aGhosh, Anirban1 aSonavane, Uddhavesh1 aSuresh, C., G.1 aJoshi, Rajendra1 aGupta, Vidya, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/remarkable-efficiency-pin-ii-proteinase-inhibitor-sans-two-conserved-disulfide-bonds-due-0