01525nas a2200253   4500008004100000022001400041245007200055210006900127260008700196300001200283490000700295520067800302653002500980653001701005653001801022653001601040100002101056700002401077700001901101700002101120700001601141700001801157856009601175       2005                        eng d  a0011-389100aAssessing the role of FecB mutation in productivity of Indian sheep0 aAssessing the role of FecB mutation in productivity of Indian sh  aC V RAMAN AVENUE, PO BOX 8005, BANGALORE 560 080, INDIAbCURRENT SCIENCE ASSNcSEP  a887-8900 v893 a<p>DNA samples from four Indian sheep breeds, viz. Garole, Deccani, Bannur and Madras Red were screened by PCR-RFLP to determine the presence of FecB mutation in these breeds. The Garole was the only breed, which carried the FecB mutation. The FecB mutation was introgressed from Garole sheep into Deccani sheep and Bannur sheep, and the performance of the crossbred sheep is being monitored in subsequent generations. Approximately half of the first backcross ewes (progeny of FecB heterozygote F1 rams) was found to carry one copy of FecB mutation, as expected. The FecB PCR-RFLP test was found to be fast, accurate and useful as a tool for making breeding decisions.</p>10aFecB (Booroola) gene10aGarole sheep10aPCR-RFLP test10aprolificacy1 aPardeshi, V., C.1 aSainani, Mohini, N.1 aMaddox, J., F.1 aGhalsasi, P., M.1 aNimbkar, C.1 aGupta, V., S.  uhttps://library.ncl.res.in/content/assessing-role-fecb-mutation-productivity-indian-sheep-002058nas 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<p>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.</p>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-002159nas a2200241   4500008004100000022001400041245006700055210006700122260010600189300001200295490000700307520131200314653001501626653002001641653002501661653002601686653001101712100002801723700002001751700002401771700002101795856010101816       2005                        eng d  a0965-174800aGene expression patterns of helicoverpa armigera gut proteases0 aGene expression patterns of helicoverpa armigera gut proteases  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcAPR  a355-3670 v353 a<p>Relative quantification of reported gut proteinase cDNAs from Helicoverpa armigera larvae fed on various host plants (cotton, chickpea, pigeonpea, tomato and okra), non-host plant Pis (winged bean, bitter gourd, ground nut, and capsicum) and during larval development has been carried out using semi-quantitative RT-PCR. Five trypsin-like and three chymotrypsin-like proteinases were categorized as insensitive or sensitive to most of the proteinase inhibitors (Pis) and insensitive/sensitive to specific Pis based on their expression analysis. These results were supported by amino acid sequence analysis, where diverged amino acids were observed in the regions, which are reported to be involved in typical trypsin trypsin inhibitor interactions and critical for proteinase inhibitor resistance. Among exopeptidases (five aminopeptidase and three carboxypeptidase), HaAmi4 and HaAmi5 of aminopeptidase and HaCar1 of carboxypeptidase exhibited considerable differential expression. Elastase and cathepsin B-like proteinases were expressed at negligible levels. The proteases identified in the study would be ideal candidates for further interactions studies with protease inhibitors to understand the structural reasons of protease inhibitor insensitivity (c) 2005 Elsevier Ltd. All rights reserved.</p>10aexpression10agut proteinases10aHelicoverpa armigera10aProteinase inhibitors10aRT-PCR1 aChougule, Nanasaheb, P.1 aGiri, Ashok, P.1 aSainani, Mohini, N.1 aGupta, Vidya, S.  uhttps://library.ncl.res.in/content/gene-expression-patterns-helicoverpa-armigera-gut-proteases-002364nas a2200253   4500008004100000022001400041245022000055210006900275260010600344300001400450490000700464520128900471653002301760653002501783653002801808653002301836653001801859653002601877100001801903700002001921700002401941700002101965856012401986       2005                        eng d  a0031-942200aHigher accumulation of proteinase inhibitors in flowers than leaves and fruits as a possible basis for differential feeding preference of Helicoverpa armigera on tomato (Lycopersicon esculentum Mill, Cv. Dhanashree)0 aHigher accumulation of proteinase inhibitors in flowers than lea  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcNOV  a2659-26670 v663 a<p>Tomato (Lycopersicon esculentum, Mill; cultivar- Dhanashree) proteinase inhibitors (Pis) were tested for their trypsin inhibitory (TT) and Helicoverpa armigera gut proteinases inhibitory (HGPI) activity in different organs of the tomato plants. Analysis of TI and HGPI distribution in various parts of the plant showed that flowers accumulated about 300 and 1000 times higher levels of TI while 700 and 400 times higher levels of HGPI as compared to those in leaves and fruits, respectively. Field observation that H. armigera larvae infest leaves and fruits but not the flowers could be at least partially attributed to the protective role-played by the higher levels of Pis in the flower tissue. Tomato Pis inhibited about 50-80% HGP activity of H. armigera larvae feeding on various host plants including tomato, of larvae exposed to non-host plant Pis and of various larval instars. Tomato Pis were found to be highly stable to insect proteinases wherein incubation of inhibitor with HGP even for 3 h at optimum conditions did not affect inhibitory activity. Bioassay using H. armigera larvae fed on artificial diet containing tomato PIs revealed adverse effect on larval growth, pupae development, adult formation and fecundity. (c) 2005 Elsevier Ltd. All rights reserved.</p>10aaccumulation of PI10aHelicoverpa armigera10aLycopersicon esculentum10aMidgut proteinases10aPlant defense10aProteinase inhibitors1 aDamle, M., S.1 aGiri, Ashok, P.1 aSainani, Mohini, N.1 aGupta, Vidya, S.  uhttps://library.ncl.res.in/content/higher-accumulation-proteinase-inhibitors-flowers-leaves-and-fruits-possible-basis-002418nas a2200265   4500008004100000022001400041245011200055210006900167260007300236300001200309490000900321520145600330653001901786653001901805653002501824653002201849653002501871100002001896700002801916700002001944700001801964700002401982700002102006856012502027       2005                        eng d  a0304-416500aIn vivo and in vitro effect of capsicum annum proteinase inhibitors on helicoverpa armigera gut proteinases0 aIn vivo and in vitro effect of capsicum annum proteinase inhibit  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcMAR  a156-1670 v17223 a<p>Two proteinase inhibitors (PIs), CapA1 and CapA2, were purified from Capsicum annum Linn. Var. Phule Jyoti leaves and assessed for their in vitro and in vivo activity against Helicoverpa armigera gut proteinases (HGPs). Both the inhibitors exhibited molecular weights of about 12 kDa with inhibitory activity against bovine trypsin and chymotrypsin indicating presence of probable two-inhibitor repeats of PIN II family. CapA1 and CapA2 inhibited 60-80% HGP (azocaseinolytic) activity of fourth instar larvae feeding on various host plants while 45-65% inhibition of HGP activity of various instars (II to VI) larvae reared on artificial diet. The partial purification of HGP isoforms, their characterization with synthetic inhibitors and inhibition by C. annum PIs revealed that most of the trypsin-like activity (68-91%) of HGPs was sensitive to C. annum PIs while 39-85% chymotrypsin-like activity of HGPs was insensitive to these inhibitors. The feeding of C. annum leaf extracts and two purified PIs in various doses to H. armigera larvae for two successive generations through artificial diet demonstrated their potential in inhibiting larval growth and development, delay in pupation period and dramatic reduction in fecundity and fertility. This is the first report-demonstrating efficacy of C. annum PIs against insect gut proteinases as well as larval growth and development of H. armigera. (c) 2004 Elsevier B.V. All rights reserved.</p>10aCapsicum annum10agut proteinase10aHelicoverpa armigera10ainsect resistance10aProteinase inhibitor1 aTamhane, V., A.1 aChougule, Nanasaheb, P.1 aGiri, Ashok, P.1 aDixit, A., R.1 aSainani, Mohini, N.1 aGupta, Vidya, S.  uhttps://library.ncl.res.in/content/vivo-and-vitro-effect-capsicum-annum-proteinase-inhibitors-helicoverpa-armigera-gut-002480nas a2200277   4500008004100000022001400041245015400055210006900209260008900278300001200367490000700379520142000386653001401806653001301820653002001833653003501853653002301888653001801911100002501929700002501954700002001979700002401999700002802023700002102051856013002072       2006                        eng d  a0885-576500aDifferentially expressed gene transcripts in roots of resistant and susceptible chickpea plant (Cicer arietinum L.) upon Fusarium oxysporum infection0 aDifferentially expressed gene transcripts in roots of resistant   a24-28 OVAL RD, LONDON NW1 7DX, ENGLANDbACADEMIC PRESS LTD ELSEVIER SCIENCE LTDcAPR  a176-1880 v683 a<p>Differentially expressed genes in chickpea, (Cicer arietinum L.) during root infection by Fusarium oxysportan f sp. ciceri Racel, were identified using cDNA-RAPD and cDNA-AFLP approaches. The former employed decamer primers on cDNA template and revealed nine differentially expressed transcripts in the resistant-infected chickpea variety. Among the 2000 transcript-derived fragments (TDFs) screened by cDNA-AFLP, 273 were differentially expressed in chickpea roots during Fusaritan infection. Only 13.65% of the TDFs were differentially regulated during pathogen challenge, while the other 86% were expressed non-differentially during the process of pathogen infection in chickpea roots. Nineteen TDFs, which expressed differentially in the resistant-infected chickpea variety were cloned and sequenced. Two of these TDFs were similar to transcription factors like WRKY proteins and 14-3-3 proteins, while three TDFs represented the NBS-LRR-type gene sequences. Two TDFs had sequence identity to genes known to have function in defense. The RAPID TDF CaFRi60 showed sequence identity to gamma-glutamyl-cysteine synthetase. Among the TDFs examined by cDNA-AFLP, 19 were confirmed by Reverse Northern blot to be differentially expressed. The data confirms the effectiveness of the cDNA-AFLP technique in detecting differentially expressed genes during pathogenesis. (c) 2006 Elsevier Ltd. All rights reserved.</p>10acDNA-AFLP10aChickpea10aCicer arietinum10adifferentially expressed genes10afusarium oxysporum10aTranscriptome1 aNimbalkar, Suhas, B.1 aHarsulkar, Abhay, M.1 aGiri, Ashok, P.1 aSainani, Mohini, N.1 aFranceschi, Vincent, R.1 aGupta, Vidya, S.  uhttps://library.ncl.res.in/content/differentially-expressed-gene-transcripts-roots-resistant-and-susceptible-chickpea-plant-002554nas a2200253   4500008004100000022001400041245014600055210006900201260007300270300001000343490000800353520157900361653002201940653001501962653002601977653002002003653003802023653001502061100002802076700002002104700002402124700002102148856013102169       2007                        eng d  a0378-111900aDiverse forms of pin-II family proteinase inhibitors from capsicum annuum adversely affect the growth and development of helicoverpa armigera0 aDiverse forms of pinII family proteinase inhibitors from capsicu  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcNOV  a29-380 v4033 a<p>Novel forms of Pin-II type proteinase inhibitor (PIs) cDNAs (CanPIs) having three or four inhibitory repeat domains (IRD) were isolated from the developing green fruits of Capsicum annuum. Deduced amino acid (aa) sequences of the CanPIs showed up to 15% sequence divergence among each other or reported inhibitors (CanPI-1 AF039398, CanPI-2 AF221097). Amino acid sequence analysis of these CanPIs revealed that three IRD Pls have trypsin inhibitory sites, while four IRD CanPIs have both trypsin and chymotrypsin inhibitory sites. Four CanPIs, two having three IRD (CanPI-3 AY986465 and CanPI-5 DQ005912) and two having four IRD (CanPI-7 DQ005913 and CanPI-9 DQ005915), were cloned in Pichia pastoris to express recombinant CanPIs. Recombinant CanPIs inhibited 90% of bovine trypsin (TI), while chymotrypsin inhibition (0) varied with the number of chymotrypsin inhibitory sites in the CanPIs. Recombinant inhibitors inhibited over 70% of the gut proteinase activity of Helicoverpa armigera. H. armigera larvae fed on recombinant CanPIs individually incorporated into artificial diet, showed 35% mortality; in addition, weight gain in H. armigera larvae and pupae was severely reduced compared to controls. Of the four CanPIs, CanPI-7, which has two sites for TI and CI, was the only one to have a consistently antagonistic effect on H. armigera growth and development. We conclude that among the four recombinant Pls tested, CanPIs containing diverse IRDs are best suited for developing insect-resistant transgenic plants. (c) 2007 Elsevier B.V. All rights reserved.</p>10ainsect resistance10aIP repeats10aPI-insect interaction10aPichia pastoris10apotato type 2 inhibitors (Pot-II)10aSolanaceae1 aTamhane, Vaijayantl, A.1 aGiri, Ashok, P.1 aSainani, Mohini, N.1 aGupta, Vidya, S.  uhttps://library.ncl.res.in/content/diverse-forms-pin-ii-family-proteinase-inhibitors-capsicum-annuum-adversely-affect-growth-002531nas a2200277   4500008004100000022001400041245009300055210006900148260008100217300001200298490000700310520153700317653002201854653001701876653002201893653002601915653003301941653002401974100002101998700002402019700002402043700002302067700001802090700002102108856012402129       2007                        eng d  a0268-914600aMitochondrial haplotypes reveal a strong genetic structure for three Indian sheep breeds0 aMitochondrial haplotypes reveal a strong genetic structure for t  a9600 GARSINGTON RD, OXFORD OX4 2DQ, OXON, ENGLANDbBLACKWELL PUBLISHINGcOCT  a460-4660 v383 a<p>This survey represents the first characterization of mitochondrial DNA diversity within three breeds of Indian sheep (two strains of the Deccani breed, as well as the Bannur and Garole breeds) from different geographic regions and with divergent phenotypic characteristics. A 1061-bp fragment of the mitochondrial genome spanning the control region, a portion of the 12S rRNA gene and the complete phenyl tRNA gene, was sequenced from 73 animals and compared with the corresponding published sequence from European and Asian breeds and the European Mouflon (Ovis musimon). Analysis of all 156 sequences revealed 73 haplotypes, 52 of which belonged to the Indian breeds. The three Indian breeds had no haplotypes in common, but one Indian haplotype was shared with European and other Asian breeds. The highest nucleotide and haplotype diversity was observed in the Bannur breed (0.00355 and 0.981 respectively), while the minimum was in the Sangamneri strain of the Deccani breed (0.00167 and 0.882 respectively). All 52 Indian haplotypes belonged to mitochondrial lineage A. Therefore, these Indian sheep are distinct from other Asian and European breeds studied so far. The relationships among the haplotypes showed strong breed structure and almost no introgression among these Indian breeds, consistent with Indian sheep husbandry, which discourages genetic exchange between breeds. These results have implications for the conservation of India's ovine biodiversity and suggest a common origin for the breeds investigated.</p>10aGenetic diversity10aIndian sheep10amitochondrial DNA10amitochondrial lineage10aphylogeographic distribution10asheep domestication1 aPardeshi, V., C.1 aKadoo, Narendra, Y.1 aSainani, Mohini, N.1 aMeadows, J., R. S.1 aKijas, J., W.1 aGupta, Vidya, S.  uhttps://library.ncl.res.in/content/mitochondrial-haplotypes-reveal-strong-genetic-structure-three-indian-sheep-breeds-0