Fig. 7: LICA1 showed conserved interaction with αVβ6 from multiple species.

A Structure of human αVβ6 binding to human TGF-β3-derived motif (pdb code: 4um9). The binding interface, defined as all amino acid in αVβ6 with distance to the binding motif of < 8 Å, is highlighted. B Aligment of ITGAV (upper panel) and ITGB6 (lower panel) protein sequence around the binding interface from multiple species. The binding interface defined in A is highlighted, and is identical across species being examined. Amino acids with distance to the binding motif of < 6 Å, are in bold and boxed. The sequence mismatches, only found outside the binding interface, are colored in red. C Transduction efficiency, measured by luciferase activity, of AAV_ITGs but not AAV9 was inhibited by pre-incubating AAVs before infection with recombinant αVβ6 protein from both human, rat, and mouse. 2E8vg AAVs were incubated with different αVβ6 concentrations (0–120 nM) for 1 h at 37 °C before added directly into cell medium (dose: 1E4 vg/cell, 96-well plate, duration: 24 h, cell line: 293_WT, n = 3 biological replicates). Same incubation conditions using 120 nM of recombinant SGCA protein were used as the control, which showed no significant difference with 0 nM αVβ6 condition. Data are presented as mean ± SEM. The statistics were performed to compare with the condition of no αVβ6 protein during incubation (0 nM αVβ6) by using two-way ANOVA (~AAV serotypes * αVβ6 treatments) followed by FDR correction. *p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001; ns not significant. Source data are provided as a Source Data file.