In-depth site-specific O-Glycosylation analysis of therapeutic Fc-fusion protein by electron-transfer/higher-energy collisional dissociation mass spectrometry.

Chromatography, Liquid / methods Glucagon-Like Peptide 1 / analysis Glycosylation Humans Immunoglobulin Fc Fragments / analysis Recombinant Fusion Proteins / analysis Tandem Mass Spectrometry
Electron-transfer/higher-energy collisional dissociation Glucagon-like peptide-1 Liquid chromatography/mass spectrometry O-Glycosylation Therapeutic Fc-fusion protein

Journal

Biologicals : journal of the International Association of Biological Standardization
ISSN: 1095-8320
Titre abrégé: Biologicals
Pays: England
ID NLM: 9004494

Informations de publication

Date de publication:
Mar 2019
Historique:
received: 30 10 2018
revised: 11 01 2019
accepted: 12 01 2019
pubmed: 2 2 2019
medline: 16 7 2019
entrez: 2 2 2019
Statut: ppublish

Résumé

Unexpected O-glycosylations, including O-xylosylations and mucin-type O-glycosylations, have been reported in recent glycosylation analyses of Fc-fusion proteins produced in mammalian cell expression systems. This observation suggests that therapeutic proteins with novel structures can undergo unintended O-glycosylations, having implications regarding their efficacy and safety. Therefore, the implementation of O-glycosylation analysis during product developmental is essential. However, detail site-specific O-glycosylation analysis is difficult because no consensus sequence for mucin-type O-glycosylations is known, and O-glycopeptides often contain multiple or continuous glycosylation sites. Recently, a new mass spectrometric fragmentation method called electron-transfer/higher-energy collisional dissociation (EThcD) has been used for site-specific glycosylation analysis. In this study, we conducted site-specific O-glycosylation analysis of commercially available GLP1-Fc fusion protein with (G4S)

Identifiants

DOI: 10.1016/j.biologicals.2019.01.005 PMID: 30704904
pubmed: 30704904
pii: S1045-1056(19)30009-0
doi: 10.1016/j.biologicals.2019.01.005
pii:
doi:

Substances chimiques

Immunoglobulin Fc Fragments 0
Recombinant Fusion Proteins 0
Glucagon-Like Peptide 1 89750-14-1

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

35-43

Informations de copyright

Copyright © 2019 International Alliance for Biological Standardization. Published by Elsevier Ltd. All rights reserved.

Auteurs

Noritaka Hashii (N)

Division of Biological Chemistry and Biologicals, National Institute of Health Sciences, 3-25-26 Tonomachi, Kawasaki-ku, Kawasaki, Kanagawa, 210-9501, Japan. Electronic address: hashii@nihs.go.jp.

Junya Suzuki (J)

Division of Biological Chemistry and Biologicals, National Institute of Health Sciences, 3-25-26 Tonomachi, Kawasaki-ku, Kawasaki, Kanagawa, 210-9501, Japan.

Hisatoshi Hanamatsu (H)

Department of Advanced Clinical Glycobiology, Faculty of Medicine and Graduate School of Medicine, Hokkaido University, Kita-21, Nishi-11, Kita-ku, Sapporo, 001-0021, Japan.

Jun-Ichi Furukawa (JI)

Department of Advanced Clinical Glycobiology, Faculty of Medicine and Graduate School of Medicine, Hokkaido University, Kita-21, Nishi-11, Kita-ku, Sapporo, 001-0021, Japan.

Akiko Ishii-Watabe (A)

Division of Biological Chemistry and Biologicals, National Institute of Health Sciences, 3-25-26 Tonomachi, Kawasaki-ku, Kawasaki, Kanagawa, 210-9501, Japan.

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Classifications MeSH

questionsmedicales.fr › Techniques d'investigation › Techniques de chimie analytique › Chromatographie › Chromatographie en phase liquide › In-depth site-specific O-Glycosylation...
questionsmedicales.fr › Hormones gastrointestinales › Peptides glucagon-like › Glucagon-like peptide 1 › In-depth site-specific O-Glycosylation...
questionsmedicales.fr › Métabolisme › Métabolisme glucidique › Glycosylation › In-depth site-specific O-Glycosylation...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › In-depth site-specific O-Glycosylation...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Globulines › Sérum-globulines › Immunoglobulines › Fragments d'immunoglobuline › Fragments Fc des immunoglobulines › In-depth site-specific O-Glycosylation...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines recombinantes › Protéines de fusion recombinantes › In-depth site-specific O-Glycosylation...
questionsmedicales.fr › Techniques d'investigation › Techniques de chimie analytique › Spectrométrie de masse › Spectrométrie de masse en tandem › In-depth site-specific O-Glycosylation...