Abstract

Monoclonal antibodies are used to block control points of the tumor development of many oncological pathologies. One of the critical control points of tumor development of several oncological pathologies is the receptor for programmed cell death (PD-1) and its ligands. Monoclonal antibodies against the PD-1 receptor are laboratory-derived humanized antibodies. An essential step in the humanization of antibodies is the production of murine hybrid cells producing monoclonal antibodies. This article describes studies of mice monoclonal antibodies against a recombinant human PD-1 receptor (rPD-1) expressed in Escherichia coli. To obtain strains of hybrid cells producing monoclonal antibodies, BALB/c mice were immunized with rPD-1 protein. B-lymphocytes of immunized mice were hybridized with the myeloma cell line of mice. Clones of hybrid cells were identified for productive activity and cloned by limiting dilution method. The properties of monoclonal antibodies were studied by enzyme-linked immunosorbent assay, Western blot and agar gel immunodiffusion. As a result, a hybrid cells producing monoclonal antibodies to a fragment of rPD-1 were obtained. Strains of hybrid cells have high productive activity in vitro and in vivo. Monoclonal antibodies react with rPD-1 protein, belong to the class of IgG1, and have a high binding constant. They efficiently bind to the PD-1 receptor and block the interaction of rPD-1 with the ligand. These monoclonal antibodies to rPD-1 can be used to obtain recombinant humanized monoclonal antibodies to the human PD-1 receptor.

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