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Glycomic studies of Drosophila melanogaster embryos

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Abstract

With the complete genome sequence of Drosophila melanogaster defined a systematic approach towards understanding the function of glycosylation has become possible. Structural assignment of the entire Drosophila glycome during specific developmental stages could provide information that would shed further light on the specific roles of different glycans during development and pinpoint the activity of certain glycosyltransferases and other glycan biosynthetic genes that otherwise might be missed through genetic analyses. In this paper the major glycoprotein N- and O-glycans of Drosophila embryos are described as part of our initial undertaking to characterize the glycome of Drosophila melanogaster. The N-glycans are dominated by high mannose and paucimannose structures. Minor amounts of mono-, bi- and tri-antennary complex glycans were observed with GlcNAc and Galβ1–4GlcNAc non-reducing end termini. O-glycans were restricted to the mucin-type core 1 Galβ1-3GalNAc sequence.

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Abbreviations

PNGase F:

peptide N-glycosidase F

PNGase A:

peptide N-glycosidase A

MALDI-:

Matrix assisted laser desorption ionisation

CAD:

collision activated decomposition

GC:

gas chromatography

Hex:

hexose

HexNAc:

N-acetylhexosamine

Fuc:

fucose

Gal:

galactose

GlcNAc:

N-acetylglucosamine

Man:

mannose

NeuAc:

N-acetylneuraminic acid

NeuGc:

N-glycolylneuraminic acid

MS:

mass spectrometry

MS/MS:

tandem mass spectrometry

CNS:

central nervous system

GFP:

green fluorescent protein

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Correspondence to Stuart M. Haslam.

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North, S.J., Koles, K., Hembd, C. et al. Glycomic studies of Drosophila melanogaster embryos. Glycoconj J 23, 345–354 (2006). https://doi.org/10.1007/s10719-006-6693-4

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  • DOI: https://doi.org/10.1007/s10719-006-6693-4

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