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- W2034458624 abstract "The Bacillus thuringiensis Cry1Ac toxin specifically binds to a 120 kDa aminopeptidase N (APN) receptor in Manduca sexta. The binding interaction is mediated by GalNAc, presumably covalently attached to the APN as part of an undefined glycan structure. Here we detail a simple, rapid and specific chemical deglycosylation technique, applicable to glycoproteins immobilized on Western blots. We used the technique to directly and unambiguously demonstrate that carbohydrates attached to 120 kDA APN are in fact binding epitopes for Cry1Ac toxin. This technique is generally applicable to all putative Cry toxin/receptor combinations. We analyzed the various glycans on the 120 kDA APN using carbohydrate compositional analysis and lectin binding. The data indicate that in the average APN molecule, 2 of 4 possible N-glycosylation sites are occupied with fucosylated paucimannose [Man(2-3)(Fuc(1-2)GlcNAc(2)-peptide] type N-glycans. Additionally, we identified 13 probable O-glycosylation sites, 10 of which are located in the Thr/Pro rich C-terminal stalk region of the protein. It is likely that 5-6 of the 13 sites are occupied, probably with simple [GalNAc-peptide] type O-glycans. This O-glycosylated C-terminal stalk, being GalNAc-rich, is the most likely binding site for Cry1Ac." @default.
- W2034458624 created "2016-06-24" @default.
- W2034458624 creator A5028687753 @default.
- W2034458624 creator A5029211607 @default.
- W2034458624 creator A5076474690 @default.
- W2034458624 date "2004-01-01" @default.
- W2034458624 modified "2023-09-26" @default.
- W2034458624 title "Analysis of glycan structures on the 120 kDa aminopeptidase N of Manduca sexta and their interactions with Bacillus thuringiensis Cry1Ac toxin" @default.
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- W2034458624 doi "https://doi.org/10.1016/j.ibmb.2003.09.007" @default.
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- W2034458624 hasPublicationYear "2004" @default.
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