GlycoFly: A database of Drosophila N-linked Glycoproteins identified using SPEG-MS techniques

Deniz Baycin-Hizal, Yuan Tian, Ilhan Akan, Elena Jacobson, Dean Clark, Jeffrey Chu, Karen Palter, Hui Zhang, Michael J. Betenbaugh

Research output: Contribution to journalArticlepeer-review

Abstract

Protein glycosylation affects cellular functions of the central nervous system (CNS). Its deficiency leads to neurological disorders such as ataxia, paralysis, learning disability, mental retardation, and memory loss. However, the glycoproteins that are responsible for these diseases are not well characterized. In this study, Drosophila melanogaster was used as a model organism to identify the N-glycosylated proteins and N-glycosylation sites of its CNS by means of proteomics. Adult fly heads were digested with chymotrypsin or trypsin and the N-linked glycopeptides were captured using solid phase extraction of N-linked glycopeptides (SPEG) technique followed by mass spectrometry (MS) analysis using LTQ OrbiTrap Velos. Three hundred and thirty new and 147 previously known glycoproteins were identified from 721 uniquely detected peptides that have 740 NXS/T glycosylation sites. The N-glycosylation sites were highly abundant in cell adhesion, ion channel, and ion binding molecules, which are important for nerve maturation, organ development, axon guidance, learning, and memory. Identification of the N-glycosylated sites of these proteins will enhance our knowledge of these proteins and serve as a basis for future studies to address the roles of these proteins in neurological function and disorders. A database for Drosophila N-linked glycopeptides (http://betenbaugh.jhu.edu/GlycoFly) has been established in this study as a resource for study of neurological disorders.

Original languageEnglish (US)
Pages (from-to)2777-2784
Number of pages8
JournalJournal of proteome research
Volume10
Issue number6
DOIs
StatePublished - Jun 3 2011

Keywords

  • Drosophila melanogaster
  • GlycoFly
  • Glycoproteins
  • central nervous system
  • glycoproteomics
  • glycosylation site
  • solid phase extraction of N-linked glycopeptides (SPEG) method

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

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