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<p>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.</p>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-002352nas a2200181   4500008004100000022001400041245015300055210006900208260008500277300001000362490000600372520157500378100002201953700002001975700002501995700002102020856012902041       2008                        eng d  a1932-620300aDigestive duet: midgut digestive proteinases of manduca sexta ingesting nicotiana attenuata with manipulated trypsin proteinase inhibitor expression0 aDigestive duet midgut digestive proteinases of manduca sexta ing  a185 BERRY ST, STE 1300, SAN FRANCISCO, CA 94107 USAbPUBLIC LIBRARY SCIENCEcAPR  ae20080 v33 a<p>Background: The defensive effect of endogenous trypsin proteinase inhibitors (NaTPIs) on the herbivore Manduca sexta was demonstrated by genetically altering NaTPI production in M. sexta's host plant, Nicotiana attenuata. To understand how this defense works, we studied the effects of NaTPI on M. sexta gut proteinase activity levels in different larval instars of caterpillars feeding freely on untransformed and transformed plants. Methodology/Principal Findings: Second and third instars larvae that fed on NaTPI-producing (WT) genotypes were lighter and had less gut proteinase activity compared to those that fed on genotypes with either little or no NaTPI activity. Unexpectedly, NaTPI activity in vitro assays not only inhibited the trypsin sensitive fraction of gut proteinase activity but also halved the NaTPI-insensitive fraction in third-instar larvae. Unable to degrade NaTPI, larvae apparently lacked the means to adapt to NaTPI in their diet. However, caterpillars recovered at least part of their gut proteinase activity when they were transferred from NaTPI-producing host plants to NaTPI-free host plants. In addition extracts of basal leaves inhibited more gut proteinase activity than did extracts of middle stem leaves with the same protein content. Conclusions/Significance: Although larvae can minimize the effects of high NaTPI levels by feeding on leaves with high protein and low NaTPI activity, the host plant's endogenous NaTPIs remain an effective defense against M. sexta, inhibiting gut proteinase and affecting larval performance.</p>1 aZavala, Jorge, A.1 aGiri, Ashok, P.1 aJongsma, Maarten, A.1 aBaldwin, Ian, T.  uhttps://library.ncl.res.in/content/digestive-duet-midgut-digestive-proteinases-manduca-sexta-ingesting-nicotiana-attenuata-0