Fig. 1: BTN2A1 is essential for pAg sensing but does not directly bind to pAgs. | Nature

Fig. 1: BTN2A1 is essential for pAg sensing but does not directly bind to pAgs.

From: Phosphoantigens glue butyrophilin 3A1 and 2A1 to activate Vγ9Vδ2 T cells

Fig. 1

a, MIA PaCa-2 cells transfected with a whole-genome sgRNA library were pretreated with HMBPP (10 nM) for 4 h, and were then co-incubated with Vγ9Vδ2 T cells (sequentially, seven times) to enrich for genes related to target-cell killing. BTN3A1 and BTN2A1 (sgRNA ≥ 4) were identified in the screening. b, The cytotoxicity of Vγ9Vδ2 T cells towards BTN2A1WT (red) or BTN2A1−/− (blue) MIA PaCa-2 cells treated with HMBPP (100 pM to 1 mM). n = 4. Data are mean ± s.e.m. c, Cartoon model of the apo BTN2A1 B30.2 crystal structure (PDB: 8IGT). The two β-sheets, the extended C-terminal loop and the His tag are indicated. The zinc ion associated with the His tag is displayed as a blue sphere. d, Electrostatic surface of BTN3A1 B30.2 (left) and HMBPP-interacting residues (right). The highly cationic region (blue) and anionic regions (red) are shown. e, Electrostatic surface (left) and residues (right) in the BTN2A1 B30.2 structure corresponding to BTN3A1 B30.2 are illustrated.

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