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Updated: Mar 22, 2026
Glycan Profiling of Plant Cell Wall Polymers using Microarrays
Published on: December 17, 2012
N-Glycopeptide Profiling in Arabidopsis Inflorescence
Shou-Ling Xu1, Katalin F Medzihradszky2, Zhi-Yong Wang3
1From the ‡Department of Plant Biology, Carnegie Institution for Science, Stanford, California 94305; §Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California 94143.
Abstract:
This study presents the first large-scale analysis of plant intact glycopeptides. Using wheat germ agglutinin lectin weak affinity chromatography to enrich modified peptides, followed by electron transfer dissociation (ETD)(1) fragmentation tandem mass spectrometry, glycan compositions on over 1100 glycopeptides from 270 proteins found in Arabidopsis inflorescence tissue were characterized. While some sites were only detected with a single glycan attached, others displayed up to 16 different glycoforms. Among the identified glycopeptides were four modified in nonconsensus glycosylation motifs. While most of the modified proteins are secreted, membrane, endoplasmic reticulum (ER), or Golgi-localized proteins, surprisingly, N-linked sugars were detected on a protein predicted to be cytosolic or nuclear.
