Identification of N-linked glycosylation sites on plant glycoproteins — ASN Events
  1. Schedule
  2. Symposium Three: Plant Proteomics
  3. Identification of N-linked glycosylation sites on plant glycoproteins

Identification of N-linked glycosylation sites on plant glycoproteins (#12)

Kris Ford 1 , Yin Ying Ho 1 , Wei Zeng 1 , Monika S Doblin 1 , Antony Bacic 1 2
  1. Adelaide Proteomics Centre, School of Biological Sciences, University of Adelaide, Adelaide, SA, Australia
  2. ARC Centre of Excellence in Plant Cell Walls, School of Biosciences, University of Melbourne, Vic, Australia

N-glycosylation of plant proteins has been shown to be important for catalytic activity, folding, subcellular location and secretion, as well as in plant pathogen interactions1. At the modification site there is (micro)heterogeneity of the glycans attached, making it difficult to detect in routine proteomics studies and the labile nature of the glycan hinders the analysis by mass spectrometry.
We describe a method for the enrichment of N-linked glycopeptides from plants, followed by LC-MS/MS analysis using higher-energy collisional dissociation (HCD) and electron transfer dissociation (ETD) for peptide identification, glycan site attachment and the type of glycans attached.