2. Academic Validation
  3. Comprehensive Glycomic and Glycoproteomic Analyses of Human Programmed Cell Death Protein 1 Extracellular Domain

Comprehensive Glycomic and Glycoproteomic Analyses of Human Programmed Cell Death Protein 1 Extracellular Domain

  • J Proteome Res. 2024 Aug 5. doi: 10.1021/acs.jproteome.4c00292.
Qiushi Chen 1 2,  Zhiwu Tan 3,  Yang Tang 4,  Yi Man Eva Fung 2,  Sheng Chen 5,  Zhiwei Chen 3,  Xuechen Li 1 2
Affiliations

Affiliations

  • 1 Laboratory for Synthetic Chemistry and Chemical Biology Limited, Units 1503-1511, 15/F., Building 17W, Hong Kong Science Park, Shatin, Hong Kong SAR 999077, P. R. China.
  • 2 Department of Chemistry, State Key Laboratory of Synthetic Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong SAR 999077, P. R. China.
  • 3 AIDS Institute and Department of Microbiology, School of Clinical Medicine, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Sassoon Road, Hong Kong SAR 999077, P. R. China.
  • 4 Department of Infectious Diseases and Public Health, Jockey Club College of Veterinary Medicine and Life Sciences, City University of Hong Kong, Tat Chee Avenue, Hong Kong SAR 999077, PR. China.
  • 5 Department of Food Science and Nutrition, Faculty of Science, The Hong Kong Polytechnic University, Yuk Choi Road, Hong Kong SAR 999077, P. R. China.
PMID: 39101792 DOI: 10.1021/acs.jproteome.4c00292
Abstract

Human programmed cell death protein 1 (hPD-1) is an essential receptor in the immune checkpoint pathway. It has played an important role in Cancer therapy. However, not all patients respond positively to the PD-1 antibody treatment, and the underlying mechanism remains unknown. PD-1 is a transmembrane glycoprotein, and its extracellular domain (ECD) is reported to be responsible for interactions and signal transduction. This domain contains 4 N-glycosylation sites and 25 potential O-glycosylation sites, which implicates the importance of glycosylation. The structure of hPD-1 has been intensively studied, but the glycosylation of this protein, especially the glycan on each glycosylation site, has not been comprehensively illustrated. In this study, hPD-1 ECD expressed by human embryonic kidney 293 (HEK 293) and Chinese hamster ovary (CHO) cells was analyzed; not only N- and O-glycosylation sites but also the glycans on these sites were comprehensively analyzed using mass spectrometry. In addition, hPD-1 ECD binding to different anti-hPD-1 Antibodies was tested, and N-glycans were found functioned differently. All of this glycan information will be beneficial for future PD-1 studies.

Keywords

Human programmed cell death protein 1; glycomics; glycoprotein; glycosylation; mass spectrometry.

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