Glycosylation Engineering of Human Recombinant Proteins in New S2 System
DOI:
https://doi.org/10.22100/jkh.v10i3.714Keywords:
Drosophila S2 cells, Glycozylation, N-acetylglucosaminidase, HexosaminidaseAbstract
Insect expression systems have been used to achieve high expression of recombinant and complex proteins, but disability of insects in the synthesis of N-Glycan products similar to mammals has been a controversial conflict debate in recent years. Glycosylation products in insects contain high or low end of mannose units. The main reason for this inability is the low level of activity of a number of enzymes including β-N - (1 and 2) acetyl glucosamine transferase I and II, β- (1 and 4) galactosyl transferase, α-(2, 3) and α-(2, 6) sialyl transferase. In addittion, a hexoaminidase that remove N-acetyl glucosamine at the end of glycan products and prevents binding of galactose and Sialic acid to glycan products have been discovered in insects. So the insect cells can be engineered to produce glycan products similar with mammalians and remove blocking agents of synthesis of sialyl and galactose products. In this systematic review, the glycosylation pathways in mammals and insects and engineering of possible glycosylation pathways in S2 cells have been investigated.
References
Bernard AR, Kost TA, Overton L, Cavegn C, Young J, Bertrand M, et al. Recombinant protein expression in a drosophila cell-line - comparison with the baculovirus system. Cytotechnology 1994;15:139-44.
Vatandoost J, ZomorodipourA, Sadeghizadeh M, Aliyari R, Bos M. Expression of biologically active human clotting factor IX in Drosophila S2 cells: gamma-carboxylation of a human vitamin K-dependent protein by the insect enzyme. Biotechnology Progress 2012;28:45-51.
Kim KR, Kim YK, Cha HJ. Recombinant baculovirus-based multiple protein expression platform for Drosophila S2 cell culture. J Biotechnol 2008;133:116-22.
Vatandoost J. Cloning and study of expression γ-carboxylated human factor IX in Drosophila S2 cells, 2012, Ph.D Thesis, Tarbiat Modares University, Tehran.
Vatandoost J, Zomorodipour A. Optimization of transfection and stable expression of human factor IX in Drosophila S2 cells. Iranian Journal of Biology 2014;26.
Arruda VR, Hagstrom JN, Deitch J, Heiman-Patterson T, Camire RM, Chu K, et al. Posttranslational modifications of recombinant myotube-synthesized human factor IX. Blood 2001;97:130-8.
Tomiya N, Narang S, Lee YC, Betenbaugh MJ. Comparing N-glycan processing in mammalian cell lines to native and engineered lepidopteran insect cell lines. Glycoconjugate Journal 2004;21: 343-60.
Jarvis DL, Kawar ZS, Hollister JR. Engineering N-glycosylation pathways inthe baculovirus-insect cell system. Current Opinion in Biotechnology 1998;9:528-33.
Viswanathan K, Betenbaugh M, yarema K. Glycosylation in native and engineered insect cells, Handbook of carbohydrate engineering, 2005.p.407-30.
Klipp E, Liebermeister W, Wierling C, Kowald A, Lehrach H, Herwig R. Systems biology. 2013: John Wiley & Sons. p. 112-115.
Tabish S, Raza A, Nasir A, Zafar S, Bokhari H. Analysis of glycosylation motifs and glycosyltransferases in Bacteria and Archaea. Bioinformation 2011;6:191.
Emmanuel T. Kinetics of protein modification reactions. Biochem Biophys Res Commun J 1984; 217:341-51.
Apweiler R, Hermjakob H, Sharon N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta 1999;1473:4-8.
Mann M, Jensen ON. Proteomic analysis of post-translational modifications. Nature Biotechnology 2003;21:255-61.
Beevers L. Post-translationalmodifications, Nucleic Acids and Proteins in Plants I. 1982, Springer. p. 136-168.
Rendić D, Wilson IB, Paschinger K. The glycosylation capacity of insect cells. Croatica Chemica Acta 2008;81:7-21.
Easton R, Leader T. Glycosylation of proteins–structure, function and analysis. Life Science 2011(48):1-5.
Behzad LR, Rezaei zarchi S. Proteins and Nucleic Acids. 2010, Payam Noor. p. 45-52.
Seppo A, Tiemeyer M. Function and structure of drosophila glycans. Glycobiology 2000;10:751-60.
Chang GD, Chen CJ, Lin CY, Chen HC, Chen H. Improvement of glycosylation in insect cells with mammalian glycosyltransferases. J Biotechnol 2003;102:61-71.
Berninsone PM. Carbohydrates and glycosylation, in WormBook: The online review of C. elegans biology 2005, WormBook: Pasadena.
Johanson K, Appelbaum E, Doyle M, Hensley P, Zhao B, Abdelmeguid SS, et al. Binding interactions of human interleukin-5 with its receptor-alpha subunit - large-scale production, structural, and functional, studies of drosophila-expressed recombinant proteins. J Biol Chem 1995;270:9459-71.
Aumiller JJ, Mabashi-Asazuma H, Hillar A, Shi X, Jarvis DL. A new glycoengineered insect cell line with an inducibly mammalianized protein N-glycosylation pathway. Glycobiology 2012;22:417-28.
Kost TA, Patrick Condreay J, Jarvis DL. Baculovirus as versatile vector for protein expression in insect and mammalian cells. National Center for Biotecnology Information 2005;23:567-75.
Downloads
Published
Issue
Section
License
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
