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. 2019 Oct 28;15(10):e1008080. doi: 10.1371/journal.ppat.1008080

Fig 7. Location of amino acid substitutions in 3D structure of E1 glycoprotein.

Fig 7

a. E1 monomer with all the identified substitutions mapped. The models of mutations were based on the coordinates from PDB entry 4adg. Mutational hotspots are shown encircled by a red line, the hotspot I including the residues I32, D34, K158, Q351, P415 and the hotspot II including the residues I50, V57, F84, V87, E118. The mutation A24->V is common in all iVDRV strains studied. The mutation F84->L was found in 5 of 6 strains and is located in the vicinity of the fusion loops. The color codes used: the variant residues found both in RVs and RVi (white spacefill), only in RVs (cyan spacefill), only in RVi (red spacefill); neutralizing epitopes NT1 (residues 225–235, brown), NT2 (245–251, orange), NT3 (260–266, violet) and NT4 (274–285, yellow); fusion loops (FL-I, residues 89–98, blue; FL-II, residues 130–138, magenta). b, c. Mutated amino acid residues on the surface of E1 monomer (b) and trimer (c) in iVDRVs (solvent accessibility >0.5, probe size 1.4A). d. The NT epitopes in E1 monomer. e. Possible escape mutations in the E1 neutralizing epitopes NT2, NT3 and NT4.