Glycan-protein cross-linking mass spectrometry reveals sialic acid-mediated protein networks on cell surfaces.
Journal
Chemical science
ISSN: 2041-6520
Titre abrégé: Chem Sci
Pays: England
ID NLM: 101545951
Informations de publication
Date de publication:
01 Jul 2021
01 Jul 2021
Historique:
received:
08
02
2021
accepted:
17
05
2021
entrez:
14
7
2021
pubmed:
15
7
2021
medline:
15
7
2021
Statut:
epublish
Résumé
A cross-linking method is developed to elucidate glycan-mediated interactions between membrane proteins through sialic acids. The method provides information on previously unknown extensive glycomic interactions on cell membranes. The vast majority of membrane proteins are glycosylated with complicated glycan structures attached to the polypeptide backbone. Glycan-protein interactions are fundamental elements in many cellular events. Although significant advances have been made to identify protein-protein interactions in living cells, only modest advances have been made on glycan-protein interactions. Mechanistic elucidation of glycan-protein interactions has thus far remained elusive. Therefore, we developed a cross-linking mass spectrometry (XL-MS) workflow to directly identify glycan-protein interactions on the cell membrane using liquid chromatography-mass spectrometry (LC-MS). This method involved incorporating azido groups on cell surface glycans through biosynthetic pathways, followed by treatment of cell cultures with a synthesized reagent,
Identifiants
pubmed: 34257876
doi: 10.1039/d1sc00814e
pii: d1sc00814e
pmc: PMC8246274
doi:
Types de publication
Journal Article
Langues
eng
Pagination
8767-8777Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM049077
Pays : United States
Informations de copyright
This journal is © The Royal Society of Chemistry.
Déclaration de conflit d'intérêts
There are no conflicts with this report.
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