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- W2903320439 abstract "Abstract The WT1 protein is an ideal cancer antigen, but therapeutically targeting this transcription factor has proven difficult. We have discovered a therapeutic TCR mimic antibody that specifically binds to a WT1-derived peptide (RMFPNAPYL) in the context of the MHC class I haplotype HLA-A2. This high affinity mAb, called ESK, has demonstrated significant anti-cancer activity in animal models of human cancers and leukemias. Studies in vitro and in vivo have shown the dominant role of ADCC in ESK activity. While commercially available mAbs target tens to hundreds of thousands of sites on a cell, ESK binds as few as ~500 epitopes and still promotes cancer cell clearance in vivo. Therefore, we believe ADCC can be a more sensitive mode of killing than currently estimated. To probe this question, we developed a biotinylated RMF peptide that can be pulsed onto HLA-A2 on T2 cells at various concentrations and detected using labeled streptavidin probes. By using 3D confocal microscopy photon scanning, we can detect single molecules of the streptavidin probe on a cell surface. Therefore, using a CFP-DEVD-YFP FRET reporter expressed in the pulsed T2 cells, we can measure the number of peptides bound by ESK in the immunological synapse between a target T2 cell and a human NK cell required to induce T2 cell death. Identifying this number will impact patient selection for ESK clinical trials and will influence the development of therapeutic mAbs against other low-density epitopes." @default.
- W2903320439 created "2018-12-11" @default.
- W2903320439 creator A5006680533 @default.
- W2903320439 creator A5081078558 @default.
- W2903320439 date "2015-05-01" @default.
- W2903320439 modified "2023-09-26" @default.
- W2903320439 title "Quantifying the lower limit of antibody-dependent cell cytotoxicity using a TCRm against a WT1 peptide/MHC epitope (VAC3P.1058)" @default.
- W2903320439 doi "https://doi.org/10.4049/jimmunol.194.supp.71.5" @default.
- W2903320439 hasPublicationYear "2015" @default.
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