| Literature DB >> 35087313 |
Ratna Sariyatun1, Hiroyuki Kajiura1,2, Juthamard Limkul1, Ryo Misaki1,2, Kazuhito Fujiyama1,2,3.
Abstract
N-Glycosylation is essential for protein stability, activity and characteristics, and is often needed to deliver pharmaceutical glycoproteins to target cells. A paucimannosidic structure, Man3GlcNAc2 (M3), has been reported to enable cellular uptake of glycoproteins through the mannose receptor (MR) in humans, and such uptake has been exploited for the treatment of certain diseases. However, M3 is generally produced at a very low level in plants. In this study, a cell culture was established from an Arabidopsis alg3 mutant plant lacking asparagine-linked glycosylation 3 (ALG3) enzyme activity. Arabidopsis alg3 cell culture produced glycoproteins with predominantly M3 and GlcNAc-terminal structures, while the amount of plant-specific N-glycans was very low. Pharmaceutical glycoproteins with these characteristics would be valuable for cellular delivery through the MR, and safe for human therapy.Entities:
Keywords: Arabidopsis; N-glycosylation; alg3; paucimannose
Year: 2021 PMID: 35087313 PMCID: PMC8761587 DOI: 10.5511/plantbiotechnology.21.1025a
Source DB: PubMed Journal: Plant Biotechnol (Tokyo) ISSN: 1342-4580 Impact factor: 1.133