Abstract
N-glycosylation is one of the most common and complex post-translational modifications of eukaryotic proteins and one that has numerous roles, such as modulating protein stability, sorting, folding, enzyme activity, and ligand interactions. In plants, the functional significance of N-glycosylation is typically obscure, although it is a feature of most secreted proteins and so is potentially of considerable interest to plant cell wall biologists. While analytical pipelines have been established to characterize yeast, mammalian, and bacterial N-glycoproteomes, such large-scale approaches for the study of plant glycoproteins have yet to be reported. Indeed, the N-glycans that decorate plant and mammalian or yeast proteins are structurally distinct and so modification of existing analytical approaches are needed to tackle plant N-glycoproteomes. In this review, we summarize a range of existing technologies for large-scale N-glycoprotein analysis and highlight promising future approaches that may provide a better understanding of the plant N-glycoproteome, and therefore the cell wall proteome and other proteins associated with the secretory pathway.
Highlights
Characterization of the detailed structures of N-glycoproteins can provide valuable insights into basics aspects of cell and organismal biology and is becoming increasingly important for pharmaceutical development and production (De Marchis et al, 2011; Xu et al, 2011; Yang et al, 2012)
In this review we present some of the analytical platforms or strategies, including new developments in mass spectrometry (MS) instrumentation, which can be used for the systematic characterization of N -glycoproteins, with particular reference to the challenges of studying those from plants, as well as a perspective of future developments in the field
As described above, the characterization of the plant N glycoproteome is methodologically challenging due to the extreme structural heterogeneity and the often low concentration of several glycoforms attached to each glycopeptide residing in the total peptide pool
Summary
Characterization of the detailed structures of N-glycoproteins can provide valuable insights into basics aspects of cell and organismal biology and is becoming increasingly important for pharmaceutical development and production (De Marchis et al, 2011; Xu et al, 2011; Yang et al, 2012). A comprehensive analysis of a plant glycoprotein involves the identification of glycosylated peptides, determination of the location of the glycosylation sites, and elucidation of the glycan structure (Fitchette et al, 2007), each of which presents a specific set of technical challenges.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
