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Fig. 4 | Journal of Translational Medicine

Fig. 4

From: 32A9, a novel human antibody for designing an immunotoxin and CAR-T cells against glypican-3 in hepatocellular carcinoma

Fig. 4

Epitope mapping of 32A9. a Structural model of the 32A9/GPC3 complex. YP7 is used as a control antibody against GPC3. GPC3: gray. 32A9: blue. YP7: red. HS chains: green. b The predicted epitope of 32A9. Essential residues of the 32A9 epitope are labeled in blue. The region recognized by YP7 is labeled in red. HS chain binding residues (S495 and S505) are shown as atoms. c ELISA to detect the binding activity of 32A9 and YP7 on the indicated mutant GPC3. Point mutations Y295A, D464A, K467A, H468A, Q471A and R474A were constructed to destroy the 32A9 epitope, whereas point mutations F41E, L92E and A96L are used as control residues. Values represent the mean ± SD, with p*** < 0.001. d ELISA to detect 32A9 binding activity on wild-type GPC3 and GPC3ΔHS. Values represent the mean ± SD, with ***p < 0.001. e Sequence comparison of human GPC3 epitope and its corresponding sequences in mouse GPC3 and human GPC5. The key residues of 32A9 epitope are showed in red. Two different residues in human GPC5 are labeled in pink. f Structural comparison of 32A9 epitope among modeled human GPC3, mouse GPC3 and human GPC5. Arrows indicate the residues with different orientation of side chain

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