title: Humanizing glycosylation pathways in eukaryotic expression systems.
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.
authors.affiliation: Department of Medical Biotechnology, School of Advanced Technologies in Medicine, International Campus, Tehran University of Medical Sciences, Tehran, Iran.
authors.forename: Amjad Hayat
authors.initials: AH
authors.lastname: Khan
authors.affiliation: Medical Nano-Technology and Tissue Engineering Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran.|Department of Tissue Engineering and Regenerative Medicine, School of Advanced Technologies in Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
authors.forename: Hadi
authors.initials: H
authors.lastname: Bayat
authors.affiliation: Department of Clinical Biochemistry, Faculty of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran.|Department of Biotechnology, School of Advanced Technologies in Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
authors.forename: Masoumeh
authors.initials: M
authors.lastname: Rajabibazl
authors.affiliation: Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia (UPM), 43400, Serdang, Selangor, Malaysia.
authors.forename: Suriana
authors.initials: S
authors.lastname: Sabri
authors.affiliation: Medical Nano-Technology and Tissue Engineering Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran. rahimpour@sbmu.ac.ir.|Department of Tissue Engineering and Regenerative Medicine, School of Advanced Technologies in Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran. rahimpour@sbmu.ac.ir.
authors.forename: Azam
authors.initials: A
authors.lastname: Rahimpour
mesh_terms: D000818:Animals; D005057:Eukaryotic Cells / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D007891:Leishmania / Q000378:metabolism; D015202:Protein Engineering / Q000379:methods*; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000378:metabolism
chemical_list: D006023:Glycoproteins; D011994:Recombinant Proteins
keywords: Eukaryotic expression systems; Glycoengineering; Glycosylation pattern; LEXSY