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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.

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.

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

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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