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With increasing commercial opportunities for biotherapeutics across global markets, demands are as high as ever for technologies that can support production of complex glycoproteins. N-linked glycosylation is a common post-translational modification to many proteins that may influence biological activity, protein conformation, stability, solubility, secretion, pharmacokinetics, and antigenicity.

Consequently, the ability to control and tailor N-glycosylation is critical for today’s antibody engineering. With iBio’s new Glycaneering Development Service, we can provide the power, speed and control needed to develop next-gen monoclonal antibodies, biobetters, and fast-follower products.

Glycaneering is supported by iBio’s multi-attribute analytical methods, which uses mass spectrometry to elucidate and quantify precise glycoforms on recombinant proteins.

computer generated representation of cells involved in the glycosylation process

Development Services

Why Glycaneering?

Consistency

iBio’s Nbenthamiana expression system delivers products with inherently greater N-linked glycosylation homogeneity versus competing platforms:

  • Bacteria do not glycosylate. Yeast hyperglycosylate. Chinese hamster ovary [CHO] cell lines do not precisely mimic human glycosylation patterns and intellectual property barriers limit access to glycosylation controls in CHO.
  • Nbenthamiana does not attach α1,6-fucose, terminal β1,4-galactose residues or any sialic acid residues, leading to simpler, more homogeneous N-linked glycosylation patterns than other eukaryotic expression platforms.  N. benthamiana adds α1,3-fucose.
Chart showing the results of using Glycaneering, Glycan Engineering, technology indicating its consistency

Afucosylation

Alternate N. benthiamiana hosts generate afucosylated N-linked glycans with enhanced antibody-dependent cell-mediated cytotoxicity [ADCC] activity. iBio has rights to this plant-specific afucosylation technology. Plant hosts generate G0, G1 and G2 N-linked side chains without fucose. A different host generates afucosylated antibodies with terminal β1,4-galactose residues that may further enhance effector functions, especially ADCC.2,3

Chart showing afucosylation of glycans - plotting ADCC activity vs Rituximab concentration (ng/ml)
Diagram displaying the interaction of an effector cell with a target cell during glycan engineering
Chart showing the increased amount of oligomannose residues when using Glycaneering technology which can be useful for various antibody optimization applications.
References: https://www.mdpi.com/1422-0067/20/1/194

Oligomannose Modification

Glycaneering enables the production of glycoproteins with exclusively oligomannose residues. Oligomannose can be useful for the development of lysosomal enzymes, proteins with a high clearance rate, or to promote certain effector functions.

iBio Offers Customized N-Glycosylation to Meet Your Target Product Profile

Standard Plant N-Glycans

In wild-type plants
  • More homogenous
  • No sialylation
  • No galactose capping

Afucosylated N-Glycans

Using knock-out N. benthamiana
  • Increased ADCC*
  • No sialylation
  • No galactose capping

Afucosylated Humanized N-Glycans

Using knock-out / knock-in N. benthamiana
  • Increased ADCC*
  • Galactose capping (G2)
  • No sialylation

Oligomannose N-Glycans

Use of a mannosidase inhibitor treatment
  • Increased cellular drug uptake
  • Lower serum half-life
  • Increased ADCC*
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