supplementary_materials.docx (3.58 MB)
Download file

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

Download (3.58 MB)
media
posted on 31.01.2022, 16:19 authored by Melina Mosquera Navarro Borba, Luciane Amorim Santos, Reinaldo Conceição Neto, Felipe de Oliveira Andrade, Álvaro Salgado, Filipe Ferreira de Almeida Rego, Luiz Carlos Júnior Alcantara, Lourdes Farre, Fernanda Khouri Barreto

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.

Funding

This research was funded by Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), N. 421342/2018-8 and Fundação de Amparo à Pesquisa do Estado da Bahia (FAPESB), N. BOL0157/2019.

History