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Identification of a monoclonal antibody that targets PD-1 in a manner requiring PD-1 Asn58 glycosylation
Programmed cell death 1 (PD-1) is inhibitory receptor and immune checkpoint protein. Blocking the interaction of PD-1 and its ligands PD-L1/ L2 is able to active T-cell-mediated antitumor response. Monoclonal antibody-based drugs targeting PD-1 pathway have exhibited great promise in cancer therapy....
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6814707/ https://www.ncbi.nlm.nih.gov/pubmed/31667366 http://dx.doi.org/10.1038/s42003-019-0642-9 |
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author | Wang, Mingzhu Wang, Junchao Wang, Rongjuan Jiao, Shasha Wang, Shuang Zhang, Jinchao Zhang, Min |
author_facet | Wang, Mingzhu Wang, Junchao Wang, Rongjuan Jiao, Shasha Wang, Shuang Zhang, Jinchao Zhang, Min |
author_sort | Wang, Mingzhu |
collection | PubMed |
description | Programmed cell death 1 (PD-1) is inhibitory receptor and immune checkpoint protein. Blocking the interaction of PD-1 and its ligands PD-L1/ L2 is able to active T-cell-mediated antitumor response. Monoclonal antibody-based drugs targeting PD-1 pathway have exhibited great promise in cancer therapy. Here we show that MW11-h317, an anti-PD-1 monoclonal antibody, displays high affinity for PD-1 and blocks PD-1 interactions with PD-L1/L2. MW11-h317 can effectively induce T-cell-mediated immune response and inhibit tumor growth in mouse model. Crystal structure of PD-1/MW11-h317 Fab complex reveals that both the loops and glycosylation of PD-1 are involved in recognition and binding, in which Asn58 glycosylation plays a critical role. The unique glycan epitope in PD-1 to MW11-h317 is different from the first two approved clinical PD-1 antibodies, nivolumab and pembrolizumab. These results suggest MW11-h317 as a therapeutic monoclonal antibody of PD-1 glycosylation-targeting which may become efficient alternative for cancer therapy. |
format | Online Article Text |
id | pubmed-6814707 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-68147072019-10-30 Identification of a monoclonal antibody that targets PD-1 in a manner requiring PD-1 Asn58 glycosylation Wang, Mingzhu Wang, Junchao Wang, Rongjuan Jiao, Shasha Wang, Shuang Zhang, Jinchao Zhang, Min Commun Biol Article Programmed cell death 1 (PD-1) is inhibitory receptor and immune checkpoint protein. Blocking the interaction of PD-1 and its ligands PD-L1/ L2 is able to active T-cell-mediated antitumor response. Monoclonal antibody-based drugs targeting PD-1 pathway have exhibited great promise in cancer therapy. Here we show that MW11-h317, an anti-PD-1 monoclonal antibody, displays high affinity for PD-1 and blocks PD-1 interactions with PD-L1/L2. MW11-h317 can effectively induce T-cell-mediated immune response and inhibit tumor growth in mouse model. Crystal structure of PD-1/MW11-h317 Fab complex reveals that both the loops and glycosylation of PD-1 are involved in recognition and binding, in which Asn58 glycosylation plays a critical role. The unique glycan epitope in PD-1 to MW11-h317 is different from the first two approved clinical PD-1 antibodies, nivolumab and pembrolizumab. These results suggest MW11-h317 as a therapeutic monoclonal antibody of PD-1 glycosylation-targeting which may become efficient alternative for cancer therapy. Nature Publishing Group UK 2019-10-25 /pmc/articles/PMC6814707/ /pubmed/31667366 http://dx.doi.org/10.1038/s42003-019-0642-9 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Wang, Mingzhu Wang, Junchao Wang, Rongjuan Jiao, Shasha Wang, Shuang Zhang, Jinchao Zhang, Min Identification of a monoclonal antibody that targets PD-1 in a manner requiring PD-1 Asn58 glycosylation |
title | Identification of a monoclonal antibody that targets PD-1 in a manner requiring PD-1 Asn58 glycosylation |
title_full | Identification of a monoclonal antibody that targets PD-1 in a manner requiring PD-1 Asn58 glycosylation |
title_fullStr | Identification of a monoclonal antibody that targets PD-1 in a manner requiring PD-1 Asn58 glycosylation |
title_full_unstemmed | Identification of a monoclonal antibody that targets PD-1 in a manner requiring PD-1 Asn58 glycosylation |
title_short | Identification of a monoclonal antibody that targets PD-1 in a manner requiring PD-1 Asn58 glycosylation |
title_sort | identification of a monoclonal antibody that targets pd-1 in a manner requiring pd-1 asn58 glycosylation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6814707/ https://www.ncbi.nlm.nih.gov/pubmed/31667366 http://dx.doi.org/10.1038/s42003-019-0642-9 |
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