Journal
PROTEIN EXPRESSION AND PURIFICATION
Volume 177, Issue -, Pages -Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2020.105766
Keywords
Molecular cloning; Purification of an scFv that binds to PD-1; Molecular modeling; Determining the IC50 for the anti-PD-1 scFv; Mechanism by which the anti-PD-1 scFv blocks binding of PD-L1
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Funding
- RepVir
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The study describes the purification and tight binding of an anti-PD-1 scFv from E. coli to human PD-1, and demonstrates its ability to disrupt the interaction between PD-1 and PD-L1. The properties of this scFv, including its small size, stability, and high affinity for human PD-1, suggest its potential utility in immunotherapeutic, diagnostic, and anti-viral applications.
Activated T-cells express Programmed cell Death protein 1 (PD-1), a key immune checkpoint receptor. PD-1 functions primarily in peripheral tissues, where T cells may encounter tumor-derived immunosuppressive ligands. Monoclonal antibodies that disrupt the interaction between T-cell derived PD-1 and immunosuppressive ligands, such as PD-L1, have revolutionized approaches to cancer therapy. For instance, Nivolumab is a monoclonal Ab that targets human PD-1 and has played an important role in immune checkpoint therapy. Herein we report the purification and initial characterization of a similar to 27 kDa single chain variable fragment (scFv) of Nivolumab that targets human PD-1 and blocks binding by PD-L1. The possibility that the anti-PD-1 scFv can serve as both an anti-tumor agent and as an anti-viral agent is discussed. Importance: The clinical significance of anti-PD-1 antibodies for treatment of a range of solid tumors is well documented (reviewed in [1-4]). In this report, we describe the results of studies that establish that an anti-PD-1 scFv purified from E. coli binds tightly to human PD-1. Furthermore, we demonstrate that upon binding, the antiPD-1 scFv disrupts the interaction between PD-1 and PD-L1. Thus, the properties of this scFv, including its small size, stability and affinity for human PD-1, suggest that it has the potential to be a useful reagent in subsequent immunotherapeutic, diagnostic and anti-viral applications.
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