N-glycosylation of PD-L1 modulates the efficacy of immune checkpoint blockades targeting PD-L1 and PD-1
The N-glycosylation of PD-L1 at all four sites interferes with the ability of anti-PD-L1 and anti-PD-1 ICBs to block PD-L1 interactions with PD-1; in contrast, glycosylation at the N35 site enhances ICB blocking efficacy. These effects are connected to the ability of sPD-L1 to compete with ICB binding to PD-L1 or PD-1. Thus, assessing PD-L1 glycosylation, beyond expression levels, could improve patient stratification and outcomes.
Authors
- Baisali Bhattacharya (ORCID: https://orcid.org/0000-0003-3399-7399)
- Tomer Cooks (ORCID: https://orcid.org/0000-0003-0853-3437)
- Adit Ben‐Baruch (ORCID: https://orcid.org/0000-0001-9260-8686)
- Olga Radinsky (ORCID: https://orcid.org/0009-0001-7282-0257)
- Tsipi Meshel
- Angel Porgador (ORCID: https://orcid.org/0000-0003-1540-4449)
- Tal Manko
- Bar Kaufman (ORCID: https://orcid.org/0000-0001-7740-0473)
- Nofar Erlichman
- Daniela Gologan (ORCID: https://orcid.org/0000-0003-0861-6857)
- Moshe Elkabets
- Yoav Nuta
- Muhammad Abu-Ahmad
- Eman Gharra
Institutions
- Ben-Gurion University of the Negev (IL)
- Tel Aviv University (IL)
Publication Details
- Journal
- Molecular Cancer
- Published
- 2025-05-10
- DOI
- https://doi.org/10.1186/s12943-025-02330-w
- Citations
- 6
- Primary Topic
- Cancer Immunotherapy and Biomarkers
- Type
- article
- Field-Weighted Citation Impact
- 6.27
Funders
- Israel Cancer Research Fund
- United States - Israel Binational Science Foundation
- Deutsches Krebsforschungszentrum
- Rosetrees Trust
- Ministry of Science, Technology and Space
- United States-Israel Binational Science Foundation
- Israel Science Foundation