Minimal B Cell Extrinsic IgG Glycan Modifications of Pro- and Anti-Inflammatory IgG Preparations
B cells
IVIg
IgG
antibody
glycosylation
sialylation
Journal
Frontiers in immunology
ISSN: 1664-3224
Titre abrégé: Front Immunol
Pays: Switzerland
ID NLM: 101560960
Informations de publication
Date de publication:
2019
2019
Historique:
received:
26
07
2019
accepted:
10
12
2019
entrez:
31
1
2020
pubmed:
31
1
2020
medline:
5
11
2020
Statut:
epublish
Résumé
Select residues in the biantennary sugar moiety attached to the fragment crystallizable of immunoglobulin G (IgG) antibodies can modulate IgG effector functions. Thus, afucosylated IgG glycovariants have enhanced cytotoxic activity, whereas IgG glycovariants rich in terminal sialic acid residues can trigger anti-inflammatory effects. More recent evidence suggests that terminal α2,6 linked sialic acids can be attached to antibodies post IgG secretion. These findings raise concerns for the use of therapeutic antibodies as they may change their glycosylation status in the patient and hence affect their activity. To investigate to what extent B cell extrinsic sialylation processes modify therapeutic IgG preparations
Identifiants
pubmed: 31998308
doi: 10.3389/fimmu.2019.03024
pmc: PMC6970187
doi:
Substances chimiques
Immunoglobulin Fc Fragments
0
Immunoglobulin G
0
Immunoglobulins, Intravenous
0
Polysaccharides
0
Sialic Acids
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3024Informations de copyright
Copyright © 2020 Schaffert, Hanić, Novokmet, Zaytseva, Krištić, Lux, Nitschke, Peipp, Pezer, Hennig, Rapp, Lauc and Nimmerjahn.
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