Producing Biologics with Defined N-Glycosylation in Plants.
Glycoengineering
Glycosylation
HIV
Monoclonal antibody (mAb)
Plant expression system
Plant-glycoengineering
Plant-made biologics
Plant-made pharmaceutical (PMP)
Sialylation
West Nile virus
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2023
2023
Historique:
entrez:
14
11
2022
pubmed:
15
11
2022
medline:
18
11
2022
Statut:
ppublish
Résumé
The proper glycosylation of glycoproteins is important for their structure and function. This is an especially important consideration when choosing a platform to express recombinant glycoproteins destined for therapeutic use. Chinese hamster ovary (CHO) cells have been the choice expression platform for their ability to produce recombinant glycoproteins with glycosylation profiles similar to those observed in humans. However, consistency with glycosylation has been noted as problematic, and sialylation, an important modification in human glycoproteins, has not been achieved to an acceptable degree in CHO cells. Plant biotechnology and glycoengineering has now made it possible to produce therapeutic recombinant glycoproteins in plants with glycosylation profiles observed in humans, including sialylation. Furthermore, the glycosylation profiles of recombinant therapeutic glycoproteins produced in plants are homogenous and consistently reproducible. Here, entirely via transient expression, two therapeutic monoclonal antibodies are produced in glycoengineered Nicotiana benthamiana plants that carry human glycosylation profiles including sialylation.
Identifiants
pubmed: 36374425
doi: 10.1007/978-1-0716-2835-5_17
doi:
Substances chimiques
Biological Products
0
Recombinant Proteins
0
Glycoproteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
235-250Informations de copyright
© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
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