<i>Pv</i>12 structure model. Yoelis Yepes-Pérez Carolina López Carlos Fernando Suárez Manuel Alfonso Patarroyo 10.1371/journal.pone.0203715.g008 https://plos.figshare.com/articles/figure/_i_Pv_i_12_structure_model_/7069580 <p>A (top view) and B (bottom view). <i>Pv</i>12 3D homology model. B-cell epitope 39038 (red) and T-cell epitopes 39117 (blue) and 39113 (grey) are shown as transparent surfaces. Potential interacting positions with <i>Pv</i>41 are shown in green and conserved Cys residues in yellow. C. <i>Pv</i>12 regions and primary/secondary structure representation, including relative solvent accessibility and potential interacting residues with <i>Pv</i>41 (green triangles). Best epitopes are shown (39038- red box, 39117-blue box, 39113-gray box). Other B- and T-cell epitopes are underlined. Conserved cysteine residues are shaded in brown.</p> 2018-09-10 17:34:01 Pv 12 affinity binding vaccine candidates naturally-acquired antibodies characterised HLA-DR Pv 12 protein regions vivax malaria merozoite surface T-epitopes 39113 Plasmodium vivax Pv 12 B-cell epitopes vivax Pv 12 protein B-cell epitope 39038 BepiPred -1.0 software antibody in-vitro binding assays B-cell epitopes antigenicity Malaria vivax infection individual T-cell epitopes genus Plasmodium peptide-based vaccine humoral response memory T-cell response subtropical regions cytokine production NetMHCIIpan -3.1 prediction software