01937nas a2200205   4500008004100000245014900041210006900190260000800259300001200267490000700279520115700286100002301443700002401466700002301490700002801513700002201541700002001563700002101583856012701604       2017                        eng d00aImproved tolerance against helicoverpa armigera in transgenic tomato over-expressing multi-domain proteinase inhibitor gene from capsicum annuum0 aImproved tolerance against helicoverpa armigera in transgenic to  cJUL  a597-6040 v233 aPlant proteinase inhibitors (PIs) are plant defense proteins and considered as potential candidates for engineering plant resistances against herbivores. Capsicum annuum proteinase inhibitor (CanPI7) is a multi-domain potato type II inhibitor (Pin-II) containing four inhibitory repeat domains (IRD), which target major classes of digestive enzymes in the gut of Helicoverpa armigera larvae. Stable integration and expression of the transgene in T1 transgenic generation, were confirmed by established molecular techniques. Protein extract of transgenic tomato lines showed increased inhibitory activity against H. armigera gut proteinases, supporting those domains of CanPI7 protein to be effective and active. When T1 generation plants were analyzed, they exhibited antibiosis effect against first instar larvae of H. armigera. Further, larvae fed on transgenic tomato leaves showed delayed growth relative to larvae fed on control plants, but did not change mortality rates significantly. Thus, better crop protection can be achieved in transgenic tomato by overexpression of multi-domain proteinase inhibitor CanPI7 gene against H. armigera larvae.1 aTanpure, Rahul, S.1 aBarbole, Ranjit, S.1 aDawkar, Vishal, V.1 aWaichal, Yashashree, A.1 aJoshi, Rakesh, S.1 aGiri, Ashok, P.1 aGupta, Vidya, S.  uhttps://library.ncl.res.in/content/improved-tolerance-against-helicoverpa-armigera-transgenic-tomato-over-expressing-multi02668nas a2200253   4500008004100000022001400041245007600055210006900131260000800200490000600208520183100214653001602045653002602061653001402087653003802101100002602139700002402165700002602189700003002215700001802245700002402263700002202287856010502309       2024                        eng d  a2701-019800aInhibition of trehalose synthesis in lepidoptera reduces larval fitness0 aInhibition of trehalose synthesis in lepidoptera reduces larval   cFEB0 v83 a<p>
	Trehalose is synthesized in insects through the trehalose 6-phosphate synthase and phosphatase (TPS/TPP) pathway. TPP dephosphorylates trehalose 6-phosphate to release trehalose. Trehalose is involved in metamorphosis, but its relation with body weight, size, and developmental timing is unexplored. The expression and activity of TPS/TPP fluctuate depending on trehalose demand. Thus, TPS/TPP inhibition can highlight the significance of trehalose in insect physiology. TPS/TPP transcript levels are elevated in the pre-pupal and pupal stages in Helicoverpa armigera. The inhibition of recombinantly expressed TPP by N-(phenylthio)phthalimide (NPP), is validated by in vitro assays. In vivo inhibition of trehalose synthesis reduces larval weight and size, hampers metamorphosis, and reduces its overall fitness. Insufficient trehalose leads to a shift in glucose flux, reduced energy, and dysregulated fatty acid oxidation. Metabolomics reaffirms the depletion of trehalose, glucose, glucose 6-phosphate, and suppressed tricarboxylic acid cycle. Reduced trehalose hampers the energy level affecting larval vitality. Through trehalose synthesis inhibition, the importance of trehalose in insect physiology and development is investigated. Also, in two other lepidopterans, TPP inhibition impedes physiology and survival. NPP is also found to be effective as an insecticidal formulation. Overall, trehalose levels affect the larval size, weight, and metabolic homeostasis for larval-pupal transition in lepidoptera. Inhibition of trehalose synthesis enzyme TPS/TPP is a good model to study the contribution of trehalose in attaining body weight and in larval-pupal transition. Transcriptomics and metabolomics studies reveal overall reduced energy and dysregulated glucose, protein, and fatty acid metabolism.image</p>
10aLepidoptera10ametabolic homeostasis10atrehalose10atrehalose 6-phosphate phosphatase1 aTellis, Meenakshi, B.1 aMohite, Sharada, D.1 aNair, Vineetkumar, S.1 aChaudhari, Bhagyashri, Y.1 aAhmed, Shadab1 aKotkar, Hemlata, M.1 aJoshi, Rakesh, S.  uhttps://library.ncl.res.in/content/inhibition-trehalose-synthesis-lepidoptera-reduces-larval-fitness