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Variable PD-1 glycosylation modulates the activity of immune checkpoint inhibitors

Chih-Wei Chu1, Tomislav Čaval1, Frederico Alisson-Silva1

  • 1InterVenn Biosciences, South San Francisco, CA, USA.

Life Science Alliance
|January 4, 2024
PubMed

Insights

Camrelizumab and cemiplimab bind to the immune checkpoint PD-1 via its fucosylated glycan. This targeted binding to specific glycosylation variants of PD-1 may lead to more personalized cancer therapies.

Area of Science:

  • Immunology
  • Glycobiology
  • Oncology

Background:

  • Immune checkpoint inhibitors, such as monoclonal antibodies targeting PD-1, offer significant clinical benefits in various solid tumors.
  • Variations in efficacy and toxicity profiles of these antibodies may stem from their distinct molecular properties.

Purpose of the Study:

  • To investigate the molecular interactions between camrelizumab, cemiplimab, and the immune checkpoint PD-1.
  • To explore the role of PD-1 glycosylation in antibody binding and its potential clinical implications.

Main Methods:

  • Utilized protein and cell glycoengineering techniques.
  • Analyzed the binding preferences of camrelizumab and cemiplimab to PD-1.
  • Assessed the concentration of fucosylated PD-1 in non-small-cell lung cancer patients.

Main Results:

  • Camrelizumab and cemiplimab preferentially bind to PD-1 through interactions with its fucosylated glycan, specifically at the asparagine N58 residue.
  • The concentration of fucosylated PD-1 in the blood of non-small-cell lung cancer patients correlates with disease stage.

Conclusions:

  • Glycoprofiling of surface receptors like PD-1 can guide the development of antibodies with enhanced selectivity for glycosylation variants.
  • This approach may enable the creation of differentiated antibodies and facilitate personalized therapeutic strategies in cancer treatment.

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