Dataset Information

Cell surface-specific N-glycoproteomics

ABSTRACT: To understand the cellular functions of glycans and to exploit them as clinical targets it is essential to acquire information on their cell surface exposure. Here, we developed a sensitive and specific mass spectrometry method to globally study the N-glycoforms displayed at individual protein sites on the cell surface. This offers a valuable tool to discriminate between functionally relevant glycans and biosynthetic intermediates for future cellular glycoproteomic analyses.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Keratinocyte, Skin

SUBMITTER: Noortje de Haan

LAB HEAD: Hans Wandall

PROVIDER: PXD042172 | Pride | 2024-01-26

REPOSITORIES: Pride

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Publications

Sensitive and Specific Global Cell Surface <i>N</i>-Glycoproteomics Shows Profound Differences Between Glycosylation Sites and Subcellular Components.

de Haan Noortje N Song Ming M Grant Oliver C OC Ye Zilu Z Khoder Agha Fawzi F Koed Møller Aasted Mikkel M Woods Robert J RJ Vakhrushev Sergey Y SY Wandall Hans H HH

Analytical chemistry 20231113 47

Cell surface glycans are essential for establishing cell communication, adhesion, and migration. However, it remains challenging to obtain cell surface-specific information about glycoconjugate structures. Acquiring this information is essential for unraveling the functional role of glycans and for exploiting them as clinical targets. To specifically analyze the <i>N</i>-glycoprotein forms expressed at the cell surface, we developed a C18 liquid chromatography (LC)-mass spectrometry (MS)-based g ...[more]

PMID: 37956981

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Project description:The phylum Bacteroidetes is a major component of the human gut microbiota which has a broad impact on the development and physiology of its host, and a potential role in a wide range of disease syndromes1-3. The predominance of Bacteroidetes and the genus Bacteroides in the distal gut is due in large part to the expansion of paralogous gene clusters, termed Polysaccharide Utilization Loci (PULs), dedicated to the uptake and catabolism of host derived and dietary polysaccharides4,5. It is generally thought that the diversity of PULs is key to Bacteroides successful competition for nutrients in the gut environment6. The nutritive value of the available polysaccharides varies greatly and thus their utilization is hierarchical and strictly controlled. A typical PUL includes regulatory genes that control expression in response to the presence of specific glycan substrates. However the existence of additional regulatory mechanisms has been predicted to explain phenomena such as the hierarchical control, catabolite repression, and the fine tuning of gene expression to match catabolic activity7-9. Using Bacteroides fragilis as a model organism, this report describes a previously unknown layer of regulatory control in which cis-encoded antisense small RNAs (sRNA) act as repressors of the PULsâ catabolic genes. Nearly 30% of B. fragilis PULs are subject to this type of sRNA control and these PULs tend to be more closely linked to the utilization of host-derived glycans than dietary polysaccharides. The findings described here indicate the presence of a global control mechanism that underlies the known regulatory circuits which modulate PUL expression in response to substrate availability, and hence provide novel insight into regulation of the gut Bacteroidetes physiology. This is a 4 chip study with 8 technical replicates on each chip. This was an in vitro, exploratory study to determine if mutation or overexpression of a sRNA associated with the Don locus would affect gene expression. In vitro cultures were grown in defined media with mucin glycans as the sole carbon source. The two chips representing growth of the wild type strain (638R) on mucin glycans were also used in a related study GSE53883 (GSM1303101 and GSM1303102).

Dataset Information

Cell surface-specific N-glycoproteomics

Publications

Sensitive and Specific Global Cell Surface <i>N</i>-Glycoproteomics Shows Profound Differences Between Glycosylation Sites and Subcellular Components.

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