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Glycosylation profiles determine extravasation and disease-targeting properties of armed antibodies

Dario Venetz1, Christian Hess1, Chia-wei Lin2

  • 1Institute of Pharmaceutical Sciences, Department of Chemistry and Applied Biosciences, and.

Proceedings of the National Academy of Sciences of the United States of America
|February 4, 2015
PubMed

Insights

Antibody extravasation is key for cancer therapy. This study found that specific N-linked glycan structures on antibodies significantly impact tumor targeting efficiency, emphasizing glycosylation control in drug development.

Area of Science:

  • Biotechnology
  • Immunology
  • Glycobiology

Background:

  • Antibody extravasation is crucial for reaching molecular targets in diseases, as these targets are often located outside blood vessels.
  • Understanding the factors influencing antibody biodistribution is essential for developing effective antibody-based therapeutics.

Purpose of the Study:

  • To investigate the correlation between N-linked glycan structures and the tumor-targeting efficiency of a novel IL9-armed cancer-specific antibody.
  • To analyze the glycan microheterogeneity on the IL9 portion of the recombinant antibody.
  • To determine the impact of specific glycan structures on antibody homing activity.

Main Methods:

  • Detailed biodistribution studies were performed using a novel IL9-armed cancer-specific antibody.
  • Site-specific glycan analysis was employed to characterize the N-linked glycan structures.
  • Correlation analysis was conducted between glycan structures and tumor-targeting efficiencies.

Main Results:

  • A clear correlation was identified between N-linked glycan structures and tumor-targeting efficiencies.
  • Site-specific glycan analysis revealed significant glycan microheterogeneity on the IL9 portion of the antibody.
  • Nonsialylated glycan structures were found to negatively impact disease-homing activity.

Conclusions:

  • N-linked glycan structure is a critical determinant of antibody tumor-targeting efficiency.
  • Glycosylation control and thorough characterization are vital during the process development of antibody-based therapeutics.
  • Minimizing nonsialylated glycans may enhance the therapeutic efficacy of antibodies by improving disease homing.
Keywords:
armed antibodyglycosylationinterleukin-9site-specific glycan analysistumor targeting

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