CD Biosynsis provides a variety of exogenous protein expression systems that can produce glycoproteins using genetic engineering and protein engineering strategies combined with genomics and proteomics analysis.
Advantages of Synthetic Biology-Driven Glycoprotein Production
Glycoproteins are formed by covalently linking carbohydrates to proteins, and about half of the proteins discovered so far are glycoproteins, which are diverse and have different properties and functions. Glycoproteins play an important role in various physiological and pathological functions in animals and plants. The common methods used to synthesize glycoproteins consist of chemical synthesis, chemoenzymatic synthesis, and enzymatic synthesis. Due to the great structural differences and complexity of glycoproteins, the general chemical synthesis methods are cumbersome and costly to prepare. The production of glycoproteins driven by synthetic biology based on techniques such as molecular biology and metabolic engineering is important for the production and application of high-value glycoproteins.
Figure 1. Glycosylation within E. coli and major modifications leading to enhanced glycosylation efficiency. (Jaffé SR, et al., 2014)
What We Provide
CD Biosynsis has extensive experience in glycoprotein synthesis and, based on our established synthetic biology platform, we are able to provide custom glycoprotein synthesis services of high quality.
Featured Services
- We are able to modify the amino acid sequences of recombinant proteins associated with glycosylation using genetic engineering strategies to alter the number and type of protein glycosylation sites.
- We offer custom synthesis services for glycoproteins.
- We are able to modify various exogenous protein expression systems.
Deliverables
- Exogenous protein expression system that can be used for glycoprotein production.
- Customized glycoproteins
How We Can Help
De Novo Synthesis of Key Glycopeptides with Biological Activity
Glycoproteins are large in molecular weight and complex in structure. Therefore, our scientists focus on the synthesis of key glycopeptide fragments with biological activity. We can automate the synthesis of glycopeptides up to 50 amino acid residue fragments using solid-phase synthesis technology.
Producing Recombinant Glycoproteins in Mammalian Cells
Mammalian cells are capable of expressing glycosylated proteins similar to those of humans. We can provide recombinant glycoprotein production services using mammalian cells as host cells. The mammalian cells that we have successfully applied for recombinant glycoprotein production are listed below.
| Chinese hamster ovary cells |
Baby hamster kidney cells |
Murine myeloma cells |
Producing Recombinant Glycoproteins in Prokaryotic Expression Systems
With the discovery of glycoproteins in prokaryotes, our scientists are dedicated to developing engineered bacteria with the ability to glycosylate modified proteins, thus helping our customers to reduce the cost of glycoprotein production. We have successfully transferred the N-linked glycosylation mechanism from Campylobacter jejuni to Escherichia coli, developing prokaryotic systems capable of producing glycoproteins.
Producing Recombinant Glycoproteins in Yeast
Yeast has the advantages of being both a prokaryotic organism that can be easily cultured, reproduce quickly, and secrete exogenous proteins and a eukaryotic expression system that is capable of glycosylation modification of post-translational exogenous proteins. We offer exogenous glycoprotein production services using yeast expression systems as host cells.
Producing Recombinant Glycoproteins in Insect cells
Based on the study of glycosylation modifications of insect proteins, we are able to produce recombinant glycoproteins using an insect baculovirus expression system.
Producing Recombinant Glycoproteins in Plant cells
With the development of plant transgenic technology, we have successfully established plant cell expression systems. Our scientists are committed to using plant cells to achieve large-scale production of various recombinant glycoproteins.
Glycosylation of Recombinant Proteins
Protein glycosylation modifications have a significant impact on protein structure and function. We are able to modify the glycan chains on the surface of proteins, thus changing the structure and function of the protein to meet the individual needs of our clients. For protein glycosylation engineering, we can provide the following specific services.
- We can alter the glycosylation of the protein in the cell culture medium by changing the concentration of sugars, hormones, and ammonia ions.
- We can use site-directed mutagenesis to increase or decrease the amino acid sequence associated with the protein glycosylation site.
- We can use genetic engineering to alter the expression of glycosidases or glycosyltransferases in the glycosylation pathway in the host cell.
Applications of Glycoprotein
Globular proteins are functional proteins that are essential for almost all biochemical reactions in organisms and can be applied in a wide range of fields such as biomedicine, pharmaceuticals, and the food industry. Several applications of globular proteins in related fields are listed below.
- Used in biological washing.
- Used in the field of brewing.
- Used in laboratory research.
- Used in disease treatment and diagnosis.
- Used in food processing.
- Used in the textile industry.
- Used in CAR-T therapy development.
- Used in laboratory research.
- Used in antibody drug development.
- Used in biochemical reagent development.
Want to Learn More?
CD Biosynsis provides the most comprehensive and efficient solutions for synthetic biology workflows. We are committed to helping our customers solve all problems encountered in protein and peptide production to advance their applications in a wide range of fields. Each of our deliverables will undergo a rigorous quality inspection test to ensure the reliability and accuracy of the results. If you are interested in our services or have any further questions, please do not hesitate to contact us.
References
- Tytgat HLP, et al. Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies. Nat Commun. 2019 Nov 27; 10(1): 5403.
- Jaffé SR, et al. Escherichia coli as a glycoprotein production host: recent developments and challenges. Curr Opin Biotechnol. 2014 Dec; 30: 205-10.
Home
