Glycosylation Engineering of Human Recombinant Proteins in New S2 System

Authors

  • Jafar Vatandoost1 1- Dept. of Biology, School of Basic Sciences, Hakim Sabzevari University, Sabzevar, Iran.
  • Leila Khalili2 2- Dept. of Biology, School of Basic Sciences, Hakim Sabzevari University, Sabzevar, Iran.

DOI:

https://doi.org/10.22100/jkh.v10i3.714

Keywords:

Drosophila S2 cells, Glycozylation, N-acetylglucosaminidase, Hexosaminidase

Abstract

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.

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Published

2015-06-27

Issue

Section

Original Article(s)

How to Cite

Glycosylation Engineering of Human Recombinant Proteins in New S2 System. (2015). Knowledge and Health in Basic Medical Sciences, 10(3), Page:44-51. https://doi.org/10.22100/jkh.v10i3.714

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