<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mishra, Manasi</style></author><author><style face="normal" font="default" size="100%">Mahajan, Neha S.</style></author><author><style face="normal" font="default" size="100%">Tamhane, Vaijayanti A.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author><author><style face="normal" font="default" size="100%">Baldwin, Ian T.</style></author><author><style face="normal" font="default" size="100%">Gupta, Vidya S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Stress inducible proteinase inhibitor diversity in capsicum annuum</style></title><secondary-title><style face="normal" font="default" size="100%">BMC Plant Biology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">CanPI</style></keyword><keyword><style  face="normal" font="default" size="100%">Herbivory</style></keyword><keyword><style  face="normal" font="default" size="100%">Oral secretions</style></keyword><keyword><style  face="normal" font="default" size="100%">Pin-II type proteinase inhibitors</style></keyword><keyword><style  face="normal" font="default" size="100%">Plant-insect interaction</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><publisher><style face="normal" font="default" size="100%">BIOMED CENTRAL LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">236 GRAYS INN RD, FLOOR 6, LONDON WC1X 8HL, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">12</style></volume><pages><style face="normal" font="default" size="100%">217</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Background: Wound-inducible Pin-II Proteinase inhibitors (PIs) are one of the important plant serine PIs which have been studied extensively for their structural and functional diversity and relevance in plant defense against insect pests. To explore the functional specialization of an array of Capsicum annuum (L.) proteinase inhibitor (CanPIs) genes, we studied their expression, processing and tissue-specific distribution under steady-state and induced conditions. Inductions were performed by subjecting C. annuum leaves to various treatments, namely aphid infestation or mechanical wounding followed by treatment with either oral secretion (OS) of Helicoverpa armigera or water. Results: The elicitation treatments regulated the accumulation of CanPIs corresponding to 4-, 3-, and 2-inhibitory repeat domains (IRDs). Fourty seven different CanPI genes composed of 28 unique IRDs were identified in total along with those reported earlier. The CanPI gene pool either from uninduced or induced leaves was dominated by 3-IRD PIs and trypsin inhibitory domains. Also a major contribution by 4-IRD CanPI genes possessing trypsin and chymotrypsin inhibitor domains was specifically revealed in wounded leaves treated with OS. Wounding displayed the highest number of unique CanPIs while wounding with OS treatment resulted in the high accumulation of specifically CanPI-4, -7 and -10. Characterization of the PI protein activity through two dimensional gel electrophoresis revealed tissue and induction specific patterns. Consistent with transcript abundance, wound plus OS or water treated C. annuum leaves exhibited significantly higher PI activity and isoform diversity contributed by 3- and 4-IRD CanPIs. CanPI accumulation and activity was weakly elicited by aphid infestation yet resulted in the higher expression of CanPI-26, -41 and -43. Conclusions: Plants can differentially perceive various kinds of insect attacks and respond appropriately through activating plant defenses including regulation of PIs at transcriptional and post-translational levels. Based on the differentially elicited CanPI accumulation patterns, it is intriguing to speculate that generating sequence diversity in the form of multi-IRD PIs is a part of elaborative plant defense strategy to obtain a diverse pool of functional units to confine insect attack.&lt;/p&gt;</style></abstract><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">4.354
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mahajan, Neha S.</style></author><author><style face="normal" font="default" size="100%">Mishra, Manasi</style></author><author><style face="normal" font="default" size="100%">Tamhane, Vaijayanti A.</style></author><author><style face="normal" font="default" size="100%">Gupta, Vidya S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Plasticity of protease gene expression in helicoverpa armigera upon exposure to multi-domain capsicum annuum protease inhibitor</style></title><secondary-title><style face="normal" font="default" size="100%">Biochimica et Biophysica Acta (BBA) - General Subjects</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">1830</style></volume><pages><style face="normal" font="default" size="100%">3414–3420</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Background A multi-domain Pin-II type protease inhibitor from Capsicum annuum (CanPI-7) is known to be effective against the insect pest, Helicoverpa armigera. The present study is an attempt to investigate the optimal dose of recombinant CanPI-7 (rCanPI-7) for effective antibiosis to H. armigera and further to characterize the responses of digestive proteases upon rCanPI-7 ingestion. Methods The gut protease activity was assessed biochemically and transcript accumulation pattern for selected trypsin and chymotrypsin genes was analyzed by quantitative Real-Time PCR. Results The growth retardation upon exposure to rCanPI-7 was more prominent in neonates as compared to third instar larvae. Influence of stage and dosage of rCanPI-7 was conspicuous on the expression and regulation of candidate trypsin and chymotrypsin genes in H. armigera. The transcript accumulation pattern correlated with the protease activity in rCanPI-7 exposed larvae. Conclusions We conclude that early exposure and specific dose of protease inhibitor are essential for effective antibiosis despite the large diversity and plasticity in the expression of protease genes in H. armigera. Moreover, it is also evident that the regulation and expression of H. armigera gut proteases are specific to the stage of PI exposure. General significance These results highlight the requirement of optimal PI concentration for effective growth retardation and for inhibiting the major gut proteases of H. armigera.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">6</style></issue><custom2><style face="normal" font="default" size="100%">&lt;p&gt;Council of Scientific &amp;amp; Industrial Research (CSIR) - India&lt;/p&gt;</style></custom2><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">4.94
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Lomate, Purushottam R.</style></author><author><style face="normal" font="default" size="100%">Mahajan, Neha S.</style></author><author><style face="normal" font="default" size="100%">Kale, Sandip M.</style></author><author><style face="normal" font="default" size="100%">Gupta, Vidya S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Identification and expression profiling of helicoverpa armigera microRNAs and their possible role in the regulation of digestive protease genes</style></title><secondary-title><style face="normal" font="default" size="100%">Insect Biochemistry and Molecular Biology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Deep sequencing</style></keyword><keyword><style  face="normal" font="default" size="100%">Helicoverpa armigera</style></keyword><keyword><style  face="normal" font="default" size="100%">miRNAs</style></keyword><keyword><style  face="normal" font="default" size="100%">Protease gene regulation</style></keyword><keyword><style  face="normal" font="default" size="100%">Protease inhibitors</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><publisher><style face="normal" font="default" size="100%">PERGAMON-ELSEVIER SCIENCE LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">54</style></volume><pages><style face="normal" font="default" size="100%">129-137</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;3.45&lt;/p&gt;</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mahajan, Neha S.</style></author><author><style face="normal" font="default" size="100%">Mishra, Manasi</style></author><author><style face="normal" font="default" size="100%">Tamhane, Vaijayanti A.</style></author><author><style face="normal" font="default" size="100%">Gupta, Vidya S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Stress inducible proteomic changes in capsicum annuum leaves</style></title><secondary-title><style face="normal" font="default" size="100%">Plant Physiology and Biochemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Capsicum annuum</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidative stress</style></keyword><keyword><style  face="normal" font="default" size="100%">Wounding</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JAN</style></date></pub-dates></dates><publisher><style face="normal" font="default" size="100%">ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER</style></publisher><pub-location><style face="normal" font="default" size="100%">23 RUE LINOIS, 75724 PARIS, FRANCE</style></pub-location><volume><style face="normal" font="default" size="100%">74</style></volume><pages><style face="normal" font="default" size="100%">212-217</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Herbivore attack induces defense responses in plants, activating several signaling cascades. As a result, molecules deterrent to the herbivores are produced and accumulated in plants. Expression of defense mechanism/traits requires reorganization of the plant metabolism, redirecting the resources otherwise meant for growth. In the present work, protein profile of Capsicum annuum leaves was examined after herbivore attack/induction. Majority of proteins identified as differentially accumulated, were having roles in redox metabolism and photosynthesis. For example, superoxide dismutase and NADP oxidoreductase were upregulated by 10- and 6-fold while carbonic anhydrase and fructose-1,6-bisphosphatase were downregulated by 9- and 4-fold, respectively. Also, superoxide dismutase, NADPH quinone oxidoreductase and NADP dependent isocitrate dehydrogenase transcripts showed a higher accumulation in induced leaf tissues at early time points. In general, proteins having role in defense and damage repair were upregulated while those involved in photosynthesis appeared downregulated. Thus metabolic reconfiguration to balance defense and tolerance was evident in the stress-induced leaves. (C) 2013 Elsevier Masson SAS. All rights reserved.&lt;/p&gt;</style></abstract><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.58</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mahajan, Neha S.</style></author><author><style face="normal" font="default" size="100%">Dewangan, Veena</style></author><author><style face="normal" font="default" size="100%">Lomate, Purushottam R.</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author><author><style face="normal" font="default" size="100%">Mishra, Manasi</style></author><author><style face="normal" font="default" size="100%">Gupta, Vidya S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structural features of diverse Pin-II proteinase inhibitor genes from capsicum annuum</style></title><secondary-title><style face="normal" font="default" size="100%">Planta</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">CanPI</style></keyword><keyword><style  face="normal" font="default" size="100%">Capsicum</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene architecture</style></keyword><keyword><style  face="normal" font="default" size="100%">Promoter</style></keyword><keyword><style  face="normal" font="default" size="100%">Proteinase inhibitor</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">2</style></number><publisher><style face="normal" font="default" size="100%">SPRINGER</style></publisher><pub-location><style face="normal" font="default" size="100%">233 SPRING ST, NEW YORK, NY 10013 USA</style></pub-location><volume><style face="normal" font="default" size="100%">241</style></volume><pages><style face="normal" font="default" size="100%">319-331</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The proteinase inhibitor (PI) genes from Capsicum annuum were characterized with respect to their UTR, introns and promoter elements. The occurrence of PIs with circularly permuted domain organization was evident. Several potato inhibitor II (Pin-II) type proteinase inhibitor (PI) genes have been analyzed from Capsicum annuum (L.) with respect to their differential expression during plant defense response. However, complete gene characterization of any of these C. annuum PIs (CanPIs) has not been carried out so far. Complete gene architectures of a previously identified CanPI-7 (Beads-on-string, Type A) and a member of newly isolated Bracelet type B, CanPI-69 are reported in this study. The 5' UTR (untranslated region), 3'UTR, and intronic sequences of both the CanPI genes were obtained. The genomic sequence of CanPI-7 exhibited, exon 1 (49 base pair, bp) and exon 2 (740 bp) interrupted by a 294-bp long type I intron. We noted the occurrence of three multi-domain PIs (CanPI-69, 70, 71) with circularly permuted domain organization. CanPI-69 was found to possess exon 1 (49 bp), exon 2 (551 bp) and a 584-bp long type I intron. The upstream sequence analysis of CanPI-7 and CanPI-69 predicted various transcription factor-binding sites including TATA and CAAT boxes, hormone-responsive elements (ABRELATERD1, DOFCOREZM, ERELEE4), and a defense-responsive element (WRKY71OS). Binding of transcription factors such as zinc finger motif MADS-box and MYB to the promoter regions was confirmed using electrophoretic mobility shift assay followed by mass spectrometric identification. The 3' UTR analysis for 25 CanPI genes revealed unique/distinct 3' UTR sequence for each gene. Structures of three domain CanPIs of type A and B were predicted and further analyzed for their attributes. This investigation of CanPI gene architecture will enable the better understanding of the genetic elements present in CanPIs.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">3.239</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Lomate, Purushottam R.</style></author><author><style face="normal" font="default" size="100%">Dewangan, Veena</style></author><author><style face="normal" font="default" size="100%">Mahajan, Neha S.</style></author><author><style face="normal" font="default" size="100%">Kumar, Yashwant</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Abhijeet</style></author><author><style face="normal" font="default" size="100%">Wang, Li</style></author><author><style face="normal" font="default" size="100%">Saxena, Smita</style></author><author><style face="normal" font="default" size="100%">Gupta, Vidya S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Integrated transcriptomic and proteomic analyses suggest the participation of endogenous protease inhibitors in the regulation of protease gene expression in helicoverpa armigera</style></title><secondary-title><style face="normal" font="default" size="100%">Molecular &amp; Cellular Proteomics</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUL</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">17</style></volume><pages><style face="normal" font="default" size="100%">1324-1336</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Insects adapt to plant protease inhibitors (PIs) present in their diet by differentially regulating multiple digestive proteases. However, mechanisms regulating protease gene expression in insects are largely enigmatic. Ingestion of multi-domain recombinant Capsicum annuum protease inhibitor-7 (CanPI-7) arrests growth and development of Helicoverpa armigera (Lepidoptera: Noctuidae). Using de novo RNA sequencing and proteomic analysis, we examined the response of H. armigera larvae fed on recombinant CanPI-7 at different time intervals. Here, we present evidence supporting a dynamic transition in H. armigera protease expression on CanPI-7 feeding with general down-regulation of protease genes at early time points (0.5 to 6 h) and significant up-regulation of specific trypsin, chymotrypsin and aminopeptidase genes at later time points (12 to 48 h). Further, coexpression of H. armigera endogenous PIs with several digestive protease genes were apparent. In addition to the differential expression of endogenous H. armigera PIs, we also observed a distinct novel isoform of endogenous PI in CanPI-7 fed H. armigera larvae. Based on present and earlier studies, we propose potential mechanism of protease regulation in H. armigera and subsequent adaptation strategy to cope with anti-nutritional components of plants.</style></abstract><issue><style face="normal" font="default" size="100%">7</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">6.540</style></custom4></record></records></xml>