The Drosophila melanogaster homologue of the human histo-blood group P super(k) gene encodes a glycolipid-modifying alpha 1,4-N-acetylgalactosaminyltransferase

Insects express arthro-series glycosphingolipids, which contain an alpha 1,4-linked GaINAc residue. To determine the genetic basis for this linkage, we cloned a cDNA (CG17223) from Drosophila melanogaster encoding a protein with homology to mammalian alpha 1,4-glycosyltransferases and expressed it i...

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Bibliographic Details
Published in:Biochemical journal 2004-08, Vol.382 (1), p.67-74
Main Authors: Mucha, J, Domlatil, J, Lochnit, G, Rendic, D, Paschinger, K, Hinterkoerner, G, Hofinger, A, Kosma, P, Wilson, IBH
Format: Article
Language:English
Subjects:
Drosophila melanogaster
Pichia pastoris
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Summary:Insects express arthro-series glycosphingolipids, which contain an alpha 1,4-linked GaINAc residue. To determine the genetic basis for this linkage, we cloned a cDNA (CG17223) from Drosophila melanogaster encoding a protein with homology to mammalian alpha 1,4-glycosyltransferases and expressed it in the yeast Pichia pastoris. Culture supernatants from the transformed yeast were found to display a novel UDP-GaINAc:GaINAc beta 1,4GIcNAc beta 1-R alpha -N-acetylgalactosaminyltransferase activity when using either a glycolipid, p-nitrophenylglycoside or an N-glycan carrying one or two terminal beta -N-acetylgalactosamine residues. NMR and MS in combination with glycosidase digestion and methylation analysis indicate that the cloned cDNA encodes an alpha 1,4-N-acetylgalactosaminyltransferase. We hypothesize that this enzyme and its orthologues in other insects are required for the biosynthesis of the N5a and subsequent members of the arthro-series of glycolipids as well as of N-glycan receptors for Bacillus thuringiensis crystal toxin Cry1Ac.
ISSN:0264-6021
DOI:10.1042/BJ20040535