<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