Fig. 3: AlproTox morphology, binding kinetics and cellular recycling. | British Journal of Cancer

Fig. 3: AlproTox morphology, binding kinetics and cellular recycling.

From: Identification of a high-risk immunogenic prostate cancer patient subset as candidates for T-cell engager immunotherapy and the introduction of a novel albumin-fused anti-CD3 × anti-PSMA bispecific design

Fig. 3

a–c Schematic representation of the AlproTox panel containing an anti-PSMA human domain antibody (Green) linked to an anti-CD3 scFv (Blue) and HSA (Red) with amino acid point mutations (yellow dots) providing different FcRn affinity (NB: K500A, H510Q, HB: E505Q, T527M, K573P). d–f Representative AFM images of particle height and histograms showing distribution and average height of AlproTox WT, NB and HB, respectively. Scale bar is 200 nm and intensity scale −6–6 nm. g–j Sensorgrams showing binding of serial dilutions of protein to immobilised human FcRn at pH 5.5. Red curves display fit. g Binding curves of albumin WT. h Binding curves of AlproTox WT. i Binding curves of albumin HB. j Binding curves of AlproTox HB. k rHSA detection in the supernatant following a cellular recycling assay. l AlproTox detection in the supernatant following a cellular recycling assay. Statistical analysis was made in Graphpad prism v.8 using ANOVA one-way with Tukey Post hoc correction. Mean ± SEM shown, N = 3 independent experiments.

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