Identification and evaluation of universal epitopes in Plasmodium vivax Duffy binding protein
Granados, Diana S.
Patarroyo, Manuel A.
"Selected PvDBP-derived synthetic peptides were tested in competition assays with HLA molecules in order to identify and evaluate their binding to a wide range of MHC class II molecules. Binding was evaluated as the peptide's ability to displace the biotinylated control peptide (HA306-318) and was detected by a conventional ELISA. Thus, one epitope for the HLA-DR1 molecule, two epitopes for the HLA-DR4 molecule, six epitopes for the HLA-DR7 molecule and three epitopes for the HLA-DR11 molecule displaying a high binding percentage (above 50%) were experimentally obtained. The in vitro results were compared with the epitope prediction results. Two peptides behaved as universal epitopes since they bound to a larger number of HLA-DR molecules. Given that these peptides are located in the conserved PvDBP region II, they could be considered good candidates to be included in the design of a synthetic vaccine against Plasmodium vivax malaria. © 2008 Elsevier Inc. All rights reserved."
Duffy binding protein ; cell surface ; Epitope ; synthetic ; protozoan ; Hla dr1 antigen ; Hla dr11 antigen ; Hla dr4 antigen ; Hla dr7 antigen ; Unclassified drug ; Antigen binding ; Article ; Biotinylation ; Controlled study ; Enzyme linked immunosorbent assay ; Nucleotide sequence ; Plasmodium vivax ; Priority journal ; Protein analysis ; Amino acid sequence ; Animals ; Epitope mapping ; Hla-dr antigens ; Immunodominant epitopes ; Malaria vaccines ; Molecular sequence data ; Peptides ; Plasmodium vivax ; Protein conformation ; Protozoan proteins ; Receptors, cell surface ; Sequence alignment ; Vaccines, synthetic ; Plasmodium vivax ; Duffy binding protein (dbp) ; Malaria ; Plasmodium vivax ; Universal epitopes ;
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