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Fig. 1 | Molecular Cancer

Fig. 1

From: Safety and efficacy of a novel anti-CD19 chimeric antigen receptor T cell product targeting a membrane-proximal domain of CD19 with fast on- and off-rates against non-Hodgkin lymphoma: a first-in-human study

Fig. 1

The h1218 antibody is specific for CD19 and recognizes a non-FMC63 membrane proximal epitope. A Schematic of FMC63 and h1218 antibodies binding sites on CD19. B Binding of h1218 to FMC63 bound-human CD19 complex. Sensor chips were coated with FMC63 Fc and CD19-ECD-Ck from 1700 to 2300 s. Additional FMC63 or h1218 antibody was added to the FMC63-bound sensor chip at 2300 s and monitored for further binding activities. C h1218 antibody binding test on wild-type HEK293T (CD19 negative), HEK293T cell expressing human CD19 (huCD19, HHH), and HEK293T cells expressing one of the three chimeric CD19 forms that had cynomolgus residues replacement at different region of CD19, respectively (CHH, HCH, and HHC). D Mutagenesis study to identify key residues corresponding to the h1218 CD19 epitope. E Quantification of IFNγ release on HEK293T cells expressing WT or mutant CD19 to identify additional key residues corresponding to the h1218 CD19 epitope. F Binding affinity of FMC63 and h1218 scFv to recombinant human CD19-ECD-Ck (M1-P278). Each line represents affinity measured at a different scFv concentration. All the experiments were repeated at least twice

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Molecular Cancer

ISSN: 1476-4598