![]() ![]() Cell-Free Synthetic Glycobiology: Designing and Engineering Glycomolecules Outside of Living Cells. Taw, Mingji Li, Alicia Aquino, Ninad Agashe, Sean Chung, Michael C. International Journal of Molecular Sciences 2020, 21 Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments. Homogeneous production and characterization of recombinant N-GlcNAc-protein in Pichia pastoris. Shengjun Wang, Yongheng Rong, Yaoguang Wang, Decai Kong, Peng George Wang, Min Chen, Yun Kong.Genetic and process engineering strategies for enhanced recombinant N-glycoprotein production in bacteria. Fenryco Pratama, Dennis Linton, Neil Dixon.Shubham Deshmukh, Rucha Kulkarni, Kakoli Bose.Covalent and Oriented Immobilization of scFv Antibody Fragments via an Engineered Glycan Moiety. Hortigüela, Sylvain Robin, Heng Lin, Yajie Li, Anthony P. This article is cited by 55 publications. The process of bacterial N-linked glycosylation offers the possibility to specifically address and alter the biophysical properties of proteins. The analysis revealed the presence of a homogeneous N-glycan that significantly increased the stability and the solubility of the 3D5 antibody fragment. We describe a new strategy for glycoengineering and production of quantitative amounts of glycosylated scFv 3D5 at high purity. Toward this goal, we elucidated whether antibody fragments, a potential class of therapeutic proteins, are amenable to bacterial N-linked glycosylation, thereby improving their biophysical properties. However, the major challenges in studying the consequences of protein glycosylation on a molecular level are caused by glycan heterogeneities of currently used eukaryotic expression systems, but the discovery of the N-linked protein glycosylation system in the ε-proteobacterium Campylobacter jejuni and its functional transfer to Escherichia coli opened up the possibility to produce glycoproteins in bacteria. In particular, N-linked protein glycosylation can increase the biophysical and pharmacokinetic properties of therapeutic proteins. Glycosylation is the predominant protein modification to diversify the functionality of proteins. ![]()
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