Tailored glycosylation
With increasing commercial opportunities for biotherapeutics in global markets, demand for technologies that can support the production of complex glycoproteins is as high as it has ever been. N-linked glycosylation is a common post-translational modification that can affect biological activity, protein conformation, stability, solubility, secretion, pharmacokinetics, and antigenicity.
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As a result, the ability to control and tailor N-glycosylation is critical for antibody engineering today. We can provide the power, speed, and control required to develop next-generation monoclonal antibodies, biobetters, and fast-follower products with our glycan engineering service.
It's all about consistency
SwiftPharma’s N. benthamiana expression system delivers products with inherently greater N-linked glycosylation homogeneity versus competing platforms:
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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.
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N. benthamiana 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 and a typical mammalian O-glycosylation pathway is not present at all.
SwiftPharma has an extended tool-box for glyco-engineering in the tobacco related species Nicotiana benthamiana toward the production of N-defined and tailored mucin-type O-glycans on recombinant proteins. This guarantees exceptionally reliable and stable modifications, and ticks another box for regulatory approval.
Our proteins
SwiftPharma offers customized N- and O-Glycosylation to meet your target product profile
Standard plant
N-glycans
In wild-type plants
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More homogenous
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No sialylation
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No galactose capping
Afucosylated
N-glycans
Using knock-out N. benthamiana
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Increased ADCC
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No sialylation
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No galactose capping
Afucosylated "humanized"
N- and O-glycans
Using knock-out / knock-in N. benthamiana
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Increased ADCC
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Galactose capping (G2)
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No sialylation
Oligomannose
N-glycans
Use of one or more mannosidase inhibitors
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Increased cellular drug uptake
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Lower serum half-life
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Increased ADCC
