Specific β-Turns Precede PPII(L) Structures Binding to Allele-Specific HLA-DRβ1(*) PBRs in Fully-Protective Malaria Vaccine Components

The 3D structural analysis of 62 peptides derived from highly pathogenic Plasmodium falciparum malaria parasite proteins involved in host cell invasion led to finding a striking association between particular β-turn types located in the N-terminal peripheral flanking residue region (preceding the po...

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Detalles Bibliográficos
Autores principales: Bermudez, Adriana, Alba, Martha P., Vanegas, Magnolia, Patarroyo, Manuel A., Patarroyo, Manuel E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2018
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5898157/
https://www.ncbi.nlm.nih.gov/pubmed/29682500
http://dx.doi.org/10.3389/fchem.2018.00106
Descripción
Sumario:The 3D structural analysis of 62 peptides derived from highly pathogenic Plasmodium falciparum malaria parasite proteins involved in host cell invasion led to finding a striking association between particular β-turn types located in the N-terminal peripheral flanking residue region (preceding the polyproline II left-handed structures fitting into the HLA-DRβ(*) allele family) and modified immune protection-inducing protein structure induced long-lasting protective immunity. This is the first time association between two different secondary structures associated with a specific immunological function has been described: full, long-lasting protective immunity.

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