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. 2019 Nov 5;29(6):1621–1632.e3. doi: 10.1016/j.celrep.2019.09.074

Figure 1.

Figure 1

HLA-A Molecules, Particularly Members of the A2 and A24 Supertypes, Exhibit Stronger Binding to TAPBPR Than HLA-B and -C Molecules

(A) Schematic representation of the LABScreen SAB assay used to measure soluble TAPBPR binding to individual HLA I allotypes. The SABs were incubated with 1 μM TAPBPR or with 100 nM TAPBPR (Figure S1C) for 1 h, at 22°C, and then stained for TAPBPR.

(B) Bar graph showing the level of TAPBPR binding to the top 34 binders of the HLA I library, comprising HLA-A (blue), HLA-B (orange), and HLA-C (red) molecules.

(C) Bar graph summarizing TAPBPR binding to all HLA-A allotypes tested, with members of the HLA-A2 (blue) and -A24 (green) supertypes highlighted. TAPBPR binding to all HLA-B and -C allotypes tested is shown in Figures S1A and S1B, respectively.

Error bars show mean fluorescence intensity (MFI) ± SD from triplicates within one experiment. This experiment is representative of three independent experiments.