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Identification and evaluation of universal epitopes in Plasmodium vivax Duffy binding protein

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Saravia, Carolina
Martinez, Paola
Granados, Diana S.
Lopez, Carolina
Reyes, Claudia
Patarroyo, Manuel A.

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2008

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Abstract
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.
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Duffy binding protein , cell surface , 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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