In Vivo Glycan Engineering via the Mannosidase I Inhibitor (Kifunensine) Improves Efficacy of Rituximab Manufactured in
Alkaloids
/ pharmacology
Antibody-Dependent Cell Cytotoxicity
/ drug effects
Antigens, CD20
/ metabolism
Fucose
/ metabolism
Glycosylation
/ drug effects
Mannose
/ metabolism
Mannosidases
/ antagonists & inhibitors
Metabolic Engineering
/ methods
Polysaccharides
/ metabolism
Rituximab
/ pharmacology
Nicotiana
/ drug effects
ADCC
glycosylation
kifunensine
monoclonal antibody
plant made pharmaceuticals
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
07 Jan 2019
07 Jan 2019
Historique:
received:
15
11
2018
revised:
20
12
2018
accepted:
02
01
2019
entrez:
10
1
2019
pubmed:
10
1
2019
medline:
2
5
2019
Statut:
epublish
Résumé
N-glycosylation has been shown to affect the pharmacokinetic properties of several classes of biologics, including monoclonal antibodies, blood factors, and lysosomal enzymes. In the last two decades, N-glycan engineering has been employed to achieve a N-glycosylation profile that is either more consistent or aligned with a specific improved activity (i.e., effector function or serum half-life). In particular, attention has focused on engineering processes in vivo or in vitro to alter the structure of the N-glycosylation of the Fc region of anti-cancer monoclonal antibodies in order to increase antibody-dependent cell-mediated cytotoxicity (ADCC). Here, we applied the mannosidase I inhibitor kifunensine to the
Identifiants
pubmed: 30621113
pii: ijms20010194
doi: 10.3390/ijms20010194
pmc: PMC6337617
pii:
doi:
Substances chimiques
Alkaloids
0
Antigens, CD20
0
Polysaccharides
0
kifunensine
0NI8960271
Fucose
28RYY2IV3F
Rituximab
4F4X42SYQ6
Mannosidases
EC 3.2.1.-
mannosyl-oligosaccharide 1,2-alpha-mannosidase
EC 3.2.1.113
Mannose
PHA4727WTP
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
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