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Efficient Expression of Functionally Active Aflibercept with Designed N-glycans.

Tahereh Keshvari1,2, Stanislav Melnik1, Lin Sun1

  • 1Institute of Plant Biotechnology and Cell Biology, Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences BOKU Vienna, 1190 Vienna, Austria.

Antibodies (Basel, Switzerland)
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Summary

Researchers engineered plants to produce aflibercept, a vascular endothelial growth factor receptor (VEGFR) fusion protein, with controlled glycosylation. This plant-based production yielded high amounts of functional aflibercept variants, paving the way for optimized biopharmaceutical development.

Keywords:
Fc fusionafliberceptanti VEGFglycan engineeringglycosylationplant expression

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Area of Science:

  • Biotechnology
  • Molecular Biology
  • Glycobiology

Background:

  • Aflibercept is a crucial therapeutic fusion protein targeting VEGFR.
  • Its production in mammalian cells leads to complex glycosylation heterogeneity, complicating analysis and optimization.
  • N-glycosylation sites on aflibercept can influence its structure and function.

Purpose of the Study:

  • To develop a plant-based system for producing aflibercept with controlled N-glycosylation profiles.
  • To express and characterize aflibercept variants with specific glycan structures (AFLI GnGn and AFLI Sia).
  • To assess the functional activity and binding potency of the glycoengineered aflibercept variants.

Main Methods:

  • Utilized *Nicotiana benthamiana* for transient expression of aflibercept.
  • Employed glycoengineering strategies to introduce terminal GlcNAc and sialic acid residues.
  • Performed mass spectrometry for site-specific glycosylation analysis.
  • Assessed VEGF165 binding potency of the produced variants.

Main Results:

  • Achieved high-level expression of aflibercept variants (2 g/kg fresh leaf material) in plant leaves.
  • Demonstrated proper dimer assembly and consistent site-specific glycosylation patterns.
  • Identified incomplete occupancy at some glycosylation sites.
  • Observed similar binding potency to VEGF165 for both AFLI GnGn and AFLI Sia, with a slight decrease in binding for more sialylated variants.

Conclusions:

  • Successfully produced functionally active aflibercept in significant quantities using a plant-based system.
  • Demonstrated the ability to control and design N-glycosylation profiles in plant-expressed aflibercept.
  • The findings support further research towards optimized biopharmaceutical production with tailored glycosylation.