Dataset Information

Profiling the level of N-glycan structural heterogeneity in Arabidopsis N-glycoproteins

ABSTRACT: In this study, we use hydrophilic enrichment, high-resolution tandem mass spectrometry with complimentary and triggered fragmentation to profile Arabidopsis N-glycopeptides. A total of 492 N-glycosites were identified from 324 Arabidopsis proteins with extensive N-glycan structural heterogeneity revealed through 1099 N-glycopeptides. To demonstrate the precision of the approach, we also profiled N-glycopeptides from the β-1,2-xylosyltransferase mutant (xylt), an enzyme in the N-glycan biosynthetic pathway.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Floret, Whole Membrane, Rosette, Stem

SUBMITTER: Kris Ford

LAB HEAD: Joshua L. Heazlewood

PROVIDER: PXD006270 | Pride | 2017-12-18

REPOSITORIES: pride

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Dataset's files

Source:

			Action	DRS
	160601_Wei1.byspec2	Other
	160601_Wei1.byspec2_20160607_Byonic.byrslt	Other
	160601_Wei1.pdResult	Other
	160601_Wei1.pep.xml	Pepxml
	160601_Wei1.raw	Raw

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Publications

N-linked Glycan Micro-heterogeneity in Glycoproteins of Arabidopsis.

Zeng Wei W Ford Kristina L KL Bacic Antony A Heazlewood Joshua L JL

Molecular & cellular proteomics : MCP 20171213 3

N-glycosylation is one of the most common protein post-translational modifications in eukaryotes and has a relatively conserved core structure between fungi, animals and plants. In plants, the biosynthesis of N-glycans has been extensively studied with all the major biosynthetic enzymes characterized. However, few studies have applied advanced mass spectrometry to profile intact plant N-glycopeptides. In this study, we use hydrophilic enrichment, high-resolution tandem mass ...[more]

PMID: 29237727

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Project description:Neutrophils are short-lived yet vital innate immune cells equipped with bioactive glycoproteins packed in cytosolic granules that can readily be mobilised to elicit an effective and timely response against invading pathogens. Since the dynamic glycosylation processes underpinning the dramatic metamorphosis associated with myeloid progenitor-to-neutrophil differentiation remain unmapped, we here perform a comprehensive spatiotemporal profiling of the complex N-glycoproteome of isolated granule populations from blood-derived neutrophils and during maturation of bone marrow-derived progenitors using glycomics-assisted glycoproteomics. Firstly, glycomics indicated that the granule populations of mature (resting) neutrophils exhibit distinctive glycophenotypes including, most strikingly, unusual paucimannosidic- and monoantennary complex-type N-glycans in azurophilic granules. The granule-specific N-glycosylation features were recapitulated by glycoproteomics, which also uncovered extensive site- and protein-specific N-glycosylation decorating 4,772 N-glycopeptides from 352 N-glycoproteins across the neutrophil granules. Excitingly, comprehensive mining of proteomics and transcriptomics data collected from discrete myeloid progenitor stages for glycopeptide and glyco-enzyme expression revealed that dramatic glycoproteome remodelling underpins the promyelocytic-to-metamyelocyte transition and that remodelling is driven predominantly by proteome expression changes rather than modulation of the glycosylation machinery. Notable exceptions were the oligosaccharyltransferase subunits responsible for initiation of N-glycoprotein biosynthesis that were strongly reduced with myeloid differentiation leading to reduced N-glycosylation efficiency in late-stage neutrophil maturation and in corresponding granules. Our study provides new spatiotemporal insights into the dynamic neutrophil N-glycoproteome, which exhibits intriguingly complex site-, protein- and granule-specific N-glycosylation features and which undergoes strong remodelling during myeloid progenitor-to-neutrophil metamorphosis.

Dataset Information

Profiling the level of N-glycan structural heterogeneity in Arabidopsis N-glycoproteins

Dataset's files

Publications

<i>N</i>-linked Glycan Micro-heterogeneity in Glycoproteins of Arabidopsis.

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