Critical role of HLA-DRβ* binding peptides' peripheral flanking residues in fully-protective malaria vaccine development Academic Article


  • Biochemical and Biophysical Research Communications


  • A vaccine candidate component must fit perfectly into the antigen presenting HLA-DRβ* molecule's groove (or canonical nonapeptide) peptide binding region (PBR) during antigen presentation to the T-cell receptor (TCR), conforming a specific and stable macromolecular complex and induce an appropriate immune response. Antigen's peripheral flanking residues (PFR, positions (p) -p2 and p10) must thus establish strong interactions with the HLA-DRβ* - TCR complex. These amino acids (aa) have specific physico-chemical characteristics enabling differentiation between non-protective but antibody-inducer (NPAI), short-lived protection inducer (SLPI) and long-lasting protection inducer (LLPI) peptides when used as an antimalarial vaccine component. Their identification (through 1H-NMR and Aotus monkey immunization) and proper modification contributes to a logical and rational methodology for long-lasting and protective immunological memory.

publication date

  • 2017-7-29


  • 489


  • Amino Acids
  • Antibodies
  • Antigen Presentation
  • Antigens
  • Antimalarials
  • Data storage equipment
  • HLA-DR Antigens
  • Haplorhini
  • Immunization
  • Immunologic Memory
  • Macromolecular Substances
  • Malaria Vaccines
  • Molecules
  • Nuclear magnetic resonance
  • Peptides
  • Proton Magnetic Resonance Spectroscopy
  • T-Cell Antigen Receptor
  • Vaccines

International Standard Serial Number (ISSN)

  • 0006-291X

number of pages

  • 7

start page

  • 339

end page

  • 345