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

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.

• Autores: Reyes, Cesar; Rojas Luna, Rocío; Aza Conde, Jorge; Tabares, Luisa; Patarroyo, Manuel A.; Patarroyo, Manuel Elkin
• Tipo de recurso: Article of journal
• Fecha de publicación: 2017
• Institución: Universidad de Ciencias Aplicadas y Ambientales U.D.C.A
• Repositorio: Repositorio Institucional UDCA
• Idioma: eng
• OAI Identifier: oai:repository.udca.edu.co:11158/3503
• Acceso en línea: https://www.scopus.com/search/form.uri?display=basic
• Palabra clave: Merozoítos; Plasmodium vivax; Vacunas contra la Malaria; Aminoácidos; Amino acid side-chain polarity; Immune protection-inducing peptide structure; MHCII-peptide-TCR complex; complexPeripheral flanking residues
• Rights: openAccess
• License: Derechos Reservados - Universidad de Ciencias Aplicadas y Ambientales