Supplementary_materials: In silico analysis of HTLV-1 complete genomes from patients with different clinical outcomes.

Figure S1: Analysis of the physicochemical profile of the gp46 protein. The analysis suggests that the L55P mutation may generate an important change in hydrophilicity, hydropathy, antigenicity, accessibility, and membrane buried-helix.

Figure S2: Analysis of the physicochemical profile of the gp46 protein. The analysis suggests that the Q64H and S72G mutations may generate an important change in antigenicity, accessibility, and membrane buried-helix. It also suggests that the V247I mutation may generate an important change in antigenicity.

Figure S3: Analysis of the physicochemical profile of the HBZ protein. The analysis suggests that the G90R mutation may generate an important change in hydrophilicity, hydropathy, antigenicity, accessibility, and membrane buried-helix. It also suggests that the K169R mutation may alter accessibility.

Figure S4: Analysis of the physicochemical profile of the p14 protein. The analysis suggests that the G244D mutation may generate an important change in hydrophilicity, hydropathy, antigenicity, accessibility, and membrane buried-helix.