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Front Plant Sci. 2012 Jul 4;3:150. doi: 10.3389/fpls.2012.00150. eCollection 2012.

Analytical technologies for identification and characterization of the plant N-glycoproteome.

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1
Department of Plant Biology, Cornell University, Ithaca, NY, USA.

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.

KEYWORDS:

N-glycans; glycopeptides; glycoproteins; lectins; mass spectrometry

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