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Title: Critical role of HLA-DRb* binding peptides' peripheralflankingresidues in fully-protective malaria vaccine development
Authors: Reyes, César
Rojas-Luna, Rocío
Aza-Conde, Jorge
Tabares, Luisa
Patarroyo, Manuel A.
Patarroyo, Manuel Elkin
Issue Date: 2017
Citation: Reyes, C., Rojas-Luna, R., Aza-Conde, J., Tabares, L., Patarroyo, M. A., & Patarroyo, M. E. (2017). Critical role of HLA-DRβ* binding peptides' peripheral flanking residues in fully-protective malaria vaccine development. Biochemical and Biophysical Research Communications, 489(3), 339-345. doi:10.1016/j.bbrc.2017.05.123
Series/Report no.: Biochemical and Biophysical Research Communications;Vol. 489, No. 3, Jul., 29 2017, páginas 339-345
Abstract: 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.
ISSN: 0006-291X
Appears in Collections:CCB. Artículos indexados en Scopus

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