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

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Reyes C.
Rojas-Luna R.
Aza-Conde J.
Tabares L.
Patarroyo M.A.
Patarroyo M.E.



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Elsevier B.V.

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A vaccine candidate component must fit perfectly into the antigen presenting HLA-DR?* 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-DR?* - 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. © 2017 Elsevier Inc.
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HLA DR antigen , Malaria vaccine , HLA DRB1 antigen , Malaria vaccine , Peptide , Animal experiment , Aotus , Article , Binding affinity , Hydrogen bond , Immunogenicity , Immunological memory , Nonhuman , Physical chemistry , Priority journal , Protein structure , Sequence analysis , Structure analysis , Animal , Aotidae , Binding site , Chemistry , Immunology , Synthesis , Animals , Aotidae , Binding Sites , HLA-DRB1 Chains , Malaria Vaccines , Peptides , Amino acid side-chain polarity , Immune protection-inducing peptide structure (IMPIPS) , MHCII-peptide-TCR complex , Peripheral flanking residues
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