| Literature DB >> 27837408 |
Amjad Hayat Khan1, Hadi Bayat2,3, Masoumeh Rajabibazl4,5, Suriana Sabri6, Azam Rahimpour7,8.
Abstract
Glycosylation represents the most widespread posttranslational modifications, found in a broad spectrum of natural and therapeutic recombinant proteins. It highly affects bioactivity, site-specificity, stability, solubility, immunogenicity, and serum half-life of glycoproteins. Numerous expression hosts including yeasts, insect cells, transgenic plants, and mammalian cells have been explored for synthesizing therapeutic glycoproteins. However, glycosylation profile of eukaryotic expression systems differs from human. Glycosylation strategies have been proposed for humanizing the glycosylation pathways in expression hosts which is the main theme of this review. Besides, we also highlighted the glycosylation potential of protozoan parasites by emphasizing on the mammalian-like glycosylation potential of Leishmania tarentolae known as Leishmania expression system.Entities:
Keywords: Eukaryotic expression systems; Glycoengineering; Glycosylation pattern; LEXSY
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Year: 2016 PMID: 27837408 DOI: 10.1007/s11274-016-2172-7
Source DB: PubMed Journal: World J Microbiol Biotechnol ISSN: 0959-3993 Impact factor: 3.312