With many years of experience in glycoengineering, CD BioGlyco has solved various shortcomings of the expression systems and brought customers high-quality cell lines to produce glycoproteins. We have confidence to be your essential research assistant in the field of glycobiology.

Background

Most secreted proteins in eukaryotes are glycosylated, and after many common biosynthetic steps, glycan structures mature in a species-dependent manner. Therefore, human therapeutic proteins produced in plants usually contain plant-like rather than human-like glycans, which will affect the biological function, stability and immunogenicity of the protein. The glycoengineering of plant-based expression systems started as a strategy to eliminate plant-like glycans and produce human proteins with compatible glycan structures. Since there are no pathways to synthesize sialylated proteins and the necessary precursors, the precise replication of human glycans is relatively difficult in plants, but it can now be achieved through the cooperative expression of multiple human enzymes.

Although many studies have been devoted to removing plant glycans and replacing them with human counterparts, the presence of plant glycans on proteins can also bring advantages, such as enhancing the immunogenicity of certain vaccines and promoting the interactions between therapeutic proteins and their receptors. At present, the bio-manufacturing of plant-based proteins is still a relatively new method, with only a small number of commercial-scale facilities. But compared with mammalian cell expression systems, it can reduce capital investment and commodity costs by about 50%, and relatively simple plant expression systems are more likely to produce homogenous glycoform, while mammalian expression hosts are more difficult to achieve this goal due to their complex endogenous glycosylation mechanisms.

Fig 1. Typical structures of native mammalian and plant glycans (Fischer, R.; et al. 2018)

Services

CD BioGlyco has put great efforts into exploring the glycoengineered N. benthamiana-based expression system to express different proteins. The services we provide include but are not limited to the following aspects.

• The presence of core β(1,2) xylose, core α(1,3) fucose and Levisa residues on recombinant proteins produced in plants is undesirable because of their potential immunogenicity. By inhibiting β(1,2) xylosyltransferase and α(1,3) fucosyltransferase, the N. benthamiana ΔXF was created, thereby removing the plant-specific N-glycans.
• Additional enzymes are introduced to allow the synthesis of non-natural glycans in plants. The specific implementation mechanism varies according to the most practical and effective process in each host species.

Applications

• Biopharmaceutical research
• Improve the biological activity of recombinant proteins
• Genetic engineering drug production
• Glycoprotein structure and function research

Advantages of Us

• Efficient expression vector, optimized protein expression strategies
• Fast production speed and high safety
• Customize experimental programs according to different research needs
• Cost-effective
• One-stop service, 24 hours after-sales service

CD BioGlyco can customize plant-based glycoprotein expression solutions for customers according to their needs, which not only saves you time, but also saves costs while maintaining high efficiency.

Customers can contact our employees directly and we will respond promptly. If you are interested in our services, please contact us for more detailed information.

References:

1. Fischer, R.; et al. Glycoengineering of Plant-Based Expression Systems. Advances in Biochemical Engineering/Biotechnology. 2018.
2. Montero-Morales, L.; Steinkellner, H. Advanced Plant-Based Glycan Engineering. Frontiers in Bioengineering and Biotechnology. 2018, 6.