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

César Reyes, Rocío Rojas-Luna, Jorge Aza-Conde, Luisa Tabares, Manuel A. Patarroyo, Manuel Elkin Patarroyo

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

6 Citas (Scopus)

Resumen

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.

Idioma originalInglés estadounidense
Páginas (desde-hasta)339-345
Número de páginas7
PublicaciónBiochemical and Biophysical Research Communications
Volumen489
N.º3
DOI
EstadoPublicada - jul. 29 2017

Áreas temáticas de ASJC Scopus

  • Biofísica
  • Bioquímica
  • Biología molecular
  • Biología celular

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