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

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.

publication date

  • 2008/12/26

keywords

  • Assays
  • Carrier Proteins
  • Enzyme-Linked Immunosorbent Assay
  • Epitopes
  • HLA-DR Antigens
  • HLA-DR1 Antigen
  • HLA-DR11 antigen
  • HLA-DR4 Antigen
  • HLA-DR7 Antigen
  • In Vitro Techniques
  • Molecules
  • Peptides
  • Plasmodium Duffy antigen binding protein
  • Plasmodium vivax
  • Synthetic Vaccines
  • Vivax Malaria

International Standard Serial Number (ISSN)

  • 0006-291X

number of pages

  • 5

start page

  • 1279

end page

  • 1283