Fig. 2: Evolution of MARV proteome-wide IgM, IgG, and IgA antibody epitope repertoires in MVD survivors.

a IgM, IgG, and IgA antibody epitope repertoire recognized in the human plasma at different months post-MARV infection (pi) during convalescence (12-, 30-, 43- and 60-months pi are color coded) and their alignment to the whole proteome of MARV (showing different proteins: NP, VP35, VP40, GP, VP30, VP24 and L). Graphical distribution of representative clones with a frequency of ≥2, obtained after affinity selection, are shown. The horizontal position and the length of the bars indicate the peptide sequence displayed on the selected phage clone to its homologous sequence in the MARV proteome on alignment. The thickness of each bar represents the frequency of repetitively isolated phage, with the scale shown below the alignment. The GFPDL affinity selection data was performed in duplicate (two independent experiments by researcher in the lab, who was blinded to sample identity), and similar number of phage clones and epitope repertoire was observed in both phage display analysis. b Structural representations of immunodominant antigenic sites recognized by IgG using MARV-GFPDL on the surface structure of mature trimeric MARV GP solved structure [PDB #5UQY⁴⁴]. The different domains of mature GP: GP1 (residues 1334-1769 in cyan), receptor binding site (RBS; residues 1372-1522 in orange), GP2 (residues 1842-2015 in blue), fusion loop (FL; residues 1842-1885 in pink) and N-terminal heptad repeat (NHR; residues 1886-1929 in yellow) are shown on the structure of MARV-GP, with the residue numbers corresponding to the complete MARV proteome used for GFPDL. The MARV GP structure used for crystallography encodes for MARV GPΔmuc ectodomain (encompassing amino acid residues 1–636 with a mucin deletion of residues 257–425). The immunodominant antigenic sites recognized by IgG in MVD survivors identified using MARV-GFPDL that can be mapped on the crystal structure are depicted in red.