Articles written in Journal of Biosciences
Volume 36 Issue 3 August 2011 pp 545-553 Articles
The process of uptake of hexamerins during metamorphosis from insect haemolymph by fat body cells is reminiscent of receptor-mediated endocytosis. Previously, we had identified a hexamerin-binding protein (HBP) and reported for the first time that uptake of hexamerins is dependent on the phosphorylation of HBP partly by a tyrosine kinase, which is, in turn, activated by 20-hydroxyecdysone (20E). However, the exact nature of HBP and the mechanism of interaction are still unknown. Here we report the possibility of HBP being a GPI-anchored protein in the fat body of
Volume 46 All articles Published: 19 March 2021 Article ID 0029 Article
The midgut of lepidopteran larvae is a multifunctional tissue that performs roles in digestion, absorption,immunity, transmission of pathogens and interaction with ingested various molecules. The proteins localized atthe inner apical brush border membrane are primarily digestive proteases, but some of them, likeaminopeptidase N, alkaline phosphatase, cadherins, ABC transporter C2, etc., interact with Crystal (Cry) toxinsproduced by Bacillus thuringiensis (Bt). In the present study, aminopeptidase N (APN) was characterized asCry-toxin-interacting protein in the larval midgut of castor semilooper, Achaea janata. Transcriptomic andproteomic analyses revealed the presence of multiple isoforms of APNs (APN1, 2, 4, 6 and 9) which have lessthan 40% sequence similarity but show the presence of characteristic ‘GAMENEG’ and zinc-binding motifs.Feeding a sublethal dose of Cry toxin caused differential expression of various APN isoform. Further, 6thgenerationCry-toxin-exposed larvae showed reduced expression of APN2. This report suggests that A. janatalarvae exploit altered expression of APNs to overcome the deleterious effects of Cry toxicity, which mightfacilitate toxin tolerance in the long run.
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