Specific β-Turns Precede PPIIL Structures Binding to Allele-Specific HLA-DRβ1* PBRs in Fully-Protective Malaria Vaccine Components

Adriana Bermudez; Martha P. Alba; Magnolia Vanegas; Manuel A. Patarroyo; Manuel E. Patarroyo

doi:10.3389/fchem.2018.00106

Specific β-Turns Precede PPIIL Structures Binding to Allele-Specific HLA-DRβ1* PBRs in Fully-Protective Malaria Vaccine Components

Adriana Bermudez, Martha P. Alba, Magnolia Vanegas, Manuel A. Patarroyo, Manuel E. Patarroyo

Producción científica: Contribución a una revista › Artículo de Investigación › revisión exhaustiva

3 Citas (Scopus)

Resumen

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.

Idioma original	Inglés estadounidense
Número de artículo	106
Publicación	Frontiers in Chemistry
Volumen	6
N.º	APR
DOI	https://doi.org/10.3389/fchem.2018.00106
Estado	Publicada - abr. 1 2018

Áreas temáticas de ASJC Scopus

Química General

ODS de las Naciones Unidas

Este resultado contribuye a los siguientes Objetivos de Desarrollo Sostenible

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abstract = "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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AU - Vanegas, Magnolia

AU - Patarroyo, Manuel A.

AU - Patarroyo, Manuel E.

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AB - 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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