02246nas a2200265   4500008004100000022001400041245007900055210006900134260000800203300001200211490000700223520141000230653002101640653000701661653002701668653001601695653002201711100002301733700002601756700002501782700002201807700002001829700002401849856010701873       2022                        eng d  a0022-284400aFunctional diversity of the lepidopteran ATP-binding cassette transporters0 aFunctional diversity of the lepidopteran ATPbinding cassette tra  cAUG  a258-2700 v903 a<p>
	The ATP-binding cassette (ABC) transporter gene family is ubiquitous in the living world. ABC proteins bind and hydrolyze ATP to transport a myriad of molecules across various lipid-containing membrane systems. They have been studied well in plants for transport of a variety of compounds and particularly, in vertebrates due to their direct involvement in resistance mechanisms against several toxic molecules/metabolites. ABC transporters in insects are found within large multigene families involved in the efflux of chemical insecticides and toxic/undesired metabolites originating from food and endogenous metabolism. This review deals with ABC transporter subfamilies of few agronomically important Lepidopteran pests. The transcriptional dynamics and regulation of ABC transporters during insect development emphasizes their functional diversity against insecticides, Cry toxins, and plant specialized metabolites. To generate insights about molecular function and physiological roles of ABCs, functional and structural characterization is necessary. Also, expansion and divergence of ABC transporter gene subfamilies in Lepidopteran insects needs more systematic investigation. We anticipate that newer methods of insect control in agriculture can benefit from an understanding of ABC transporter interactions with a vast range of natural specialized molecules and synthetic compounds.</p>
10aABC transporters10aBt10ainsecticide resistance10aLepidoptera10aPlant metabolites1 aBarve, Pranoti, R.1 aTellis, Meenakshi, B.1 aBarvkar, Vitthal, T.1 aJoshi, Rakesh, S.1 aGiri, Ashok, P.1 aKotkar, Hemlata, M.  uhttps://library.ncl.res.in/content/functional-diversity-lepidopteran-atp-binding-cassette-transporters02816nas a2200265   4500008004100000022001400041245008900055210006900144260000800213300001100221490000700232520198500239653002002224653001202244653002002256653001502276653002402291653001302315653001802328100002302346700002502369700002002394700002402414856011202438       2025                        eng d  a1744-117X00aHigh levels of sinigrin trigger synthesis of fatty acids in Plutella xylostella (L.)0 aHigh levels of sinigrin trigger synthesis of fatty acids in Plut  cJUN  a1014240 v543 a<p>
	Diamondback moth (Lepidoptera: Plutellidae; Plutella xylostella L.) is a specialist insect of the Brassicaceae family, damaging economically important crops, such as cabbage and cauliflower. Glucosinolates, also known as `mustard oil bombs' are present in all Brassicaceae members, of which sinigrin (allyl-glucosinolate or 2-propenylglucosinolate) is a major aliphatic compound. During herbivory, glucosinolates are converted to toxic isothiocyanates that deter insect pests. P. xylostella possesses glucosinolate sulfatases that desulfate them. Such a conversion renders them unfit for degradation to toxic products. Changes in the larval performance prompted us for RNA sequencing to understand probable adaptation mechanism under sinigrin stress. Differentially expressed genes were found to be related to larval cuticle proteins. Further, gene ontology and KEGG (Kyoto Encyclopedia of Genes and Genomes) analyses depict genes belonging to the categories, integral component of membrane, cellular processes and those involved in biosynthesis of fatty acids. Upregulation of cuticular genes viz. larval cuticle protein-17 (LCP-17), cuticular protein-19 (2CP-19) and ATP binding cassette transporter C7 (ABCC7), ABCC16 was validated by qRT-PCR. Liquid chromatography quadrupole time of flight mass spectrometry analysis of whole larvae feeding on sinigrin and their separated cuticle, depicted abundance of fatty acids. Changes in the topography of the larval cuticle were evident by scanning electron microscopy. Expression of PxABCH1 was corroborated to its role in the transport of cuticular lipids. Notably, molecular docking of PxABCH1 with cuticular fatty acids showed favorable binding interactions. To summarize, integrated transcriptomic and metabolomic analyses suggest that in response to a diet containing a high dose of sinigrin, P. xylostella re-programs metabolic pathways related to fatty acid biosynthesis that directly influence insect development.</p>
10aABC transporter10aCuticle10aHost metabolite10aMetabolome10aPlutella xylostella10aSinigrin10aTranscriptome1 aBarve, Pranoti, R.1 aBarvkar, Vitthal, T.1 aGiri, Ashok, P.1 aKotkar, Hemlata, M.  uhttps://library.ncl.res.in/content/high-levels-sinigrin-trigger-synthesis-fatty-acids-plutella-xylostella-l