ArticleFrontiers in immunology2022
PD-1 N58-Glycosylation-Dependent Binding of Monoclonal Antibody Cemiplimab for Immune Checkpoint Therapy.
Article in Frontiers in immunology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 43 citations in OpenAlex.
- Humanized Anti-PD-1 Antibodies Generated Using The Conditional Kernel-Elastic Autoencoder.bioRxiv : the preprint server for biology · 2026Article
- Review
- Engineering strategies and binding mechanisms of therapeutic anti-PD-1 antibodies approved by regulatory agencies globally.Frontiers in immunology · 2026Review
- Transarterial chemoembolization combined with PD-1 inhibitors for unresectable hepatocellular carcinoma: efficacy and hepatic safety at 4-week versus 6-week treatment intervals.American journal of translational research · 2026Article
- Article
- Pyroglutamation of cell surface proteins CD47 and TRP1 by glutaminyl cyclase modulates therapeutic antibody binding.Communications biology · 2025Article
- Cemiplimab in the treatment of metastatic basal cell carcinoma.Future oncology (London, England) · 2025Review
- Targeting PD-1 post-translational modifications for improving cancer immunotherapy.Cell insight · 2025Review
- An engineered PD1-Fc fusion produced in N. benthamiana plants efficiently blocks PD1/PDL1 interaction.Plant cell reports · 2025Article
- Article
- E-selectin affinity glycoproteomics reveals neuroendocrine proteins and the secretin receptor as a poor-prognosis signature in colorectal cancer.Molecular oncology · 2025Article
- Residue-Specific Epitope Mapping of the PD-1/Nivolumab Interaction Using X-ray Footprinting Mass Spectrometry.Antibodies (Basel, Switzerland) · 2024Article
- N-linked glycosylation of PD-L1/PD-1: an emerging target for cancer diagnosis and treatment.Journal of translational medicine · 2024Review
- Glycosylation and Its Role in Immune Checkpoint Proteins: From Molecular Mechanisms to Clinical Implications.Biomedicines · 2024Review
- Emerging therapeutic frontiers in cancer: insights into posttranslational modifications of PD-1/PD-L1 and regulatory pathways.Experimental hematology & oncology · 2024Review
- Post-translational Modification of PD-1: Potential Targets for Cancer Immunotherapy.Cancer research · 2024Review
- Anti-Tumor Potential of Post-Translational Modifications of PD-1.Current issues in molecular biology · 2024Review
- Variable PD-1 glycosylation modulates the activity of immune checkpoint inhibitors.Life science alliance · 2024Article
- Combinatory glycoengineering of monoclonal antibodies and its application in cancer therapy: a narrative review.Translational cancer research · 2024Review
- Navigating the landscape of PD-1/PD-L1 imaging tracers: from challenges to opportunities.Frontiers in medicine · 2024Review
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Immune checkpoint therapy (ICT) with a monoclonal antibody (MAb) against programmed cell death protein 1 (PD-1) is a powerful clinical treatment for tumors. Cemiplimab is a human IgG4 antibody approved in 2018 and is the first MAb proven to be effective for locally advanced basal cell carcinoma. Here, we report the crystal structure of cemiplimab bound to PD-1 and the effects of PD-1 N-glycosylation on the interactions with cemiplimab. The structure of the cemiplimab/PD-1 complex shows that cemiplimab mainly binds to PD-1 with its heavy chain, whereas the light chain serves as the predominant region to compete with the binding of PD-L1 to PD-1. The interaction network of cemiplimab to PD-1 resembles that of camrelizumab (another PD-1-binding MAb), and the N58 glycan on the BC loop of PD-1 may be involved in the interaction with cemiplimab. The binding affinity of cemiplimab with PD-1 was substantially decreased with N58-glycan-deficient PD-1, whereas the PD-1/PD-L1 blocking efficiency of cemiplimab was attenuated upon binding to the N58-glycosylation-deficient PD-1. These results indicate that both the binding and blocking efficacy of cemiplimab require the N58 glycosylation of PD-1. Taken together, these findings expand our understanding of the significance of PD-1 glycosylation in the interaction with cemiplimab.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.