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

Adriana Janneth Bermudez Quintero, Manuel Alfonso Patarroyo, Magnolia Vanegas Murcia, Martha Patricia Alba, Manuel Elkin Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

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.
Idioma originalEnglish (US)
Páginas (desde-hasta)1-10
Número de páginas10
PublicaciónFrontiers in Chemistry
Volumen6
N.º106
DOI
EstadoPublished - abr 6 2018

Citar esto

Bermudez Quintero, Adriana Janneth ; Patarroyo, Manuel Alfonso ; Vanegas Murcia, Magnolia ; Alba, Martha Patricia ; Patarroyo, Manuel Elkin. / Specific β-Turns Precede PPIIL Structures Binding to Allele-Specific HLA-DRβ1* PBRs in Fully-Protective Malaria Vaccine Components. En: Frontiers in Chemistry. 2018 ; Vol. 6, N.º 106. pp. 1-10.
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title = "Specific β-Turns Precede PPIIL Structures Binding to Allele-Specific HLA-DRβ1* PBRs in Fully-Protective Malaria Vaccine Components.",
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.",
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Specific β-Turns Precede PPIIL Structures Binding to Allele-Specific HLA-DRβ1* PBRs in Fully-Protective Malaria Vaccine Components. / Bermudez Quintero, Adriana Janneth; Patarroyo, Manuel Alfonso; Vanegas Murcia, Magnolia; Alba, Martha Patricia; Patarroyo, Manuel Elkin.

En: Frontiers in Chemistry, Vol. 6, N.º 106, 06.04.2018, p. 1-10.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Specific β-Turns Precede PPIIL Structures Binding to Allele-Specific HLA-DRβ1* PBRs in Fully-Protective Malaria Vaccine Components.

AU - Bermudez Quintero, Adriana Janneth

AU - Patarroyo, Manuel Alfonso

AU - Vanegas Murcia, Magnolia

AU - Alba, Martha Patricia

AU - Patarroyo, Manuel Elkin

PY - 2018/4/6

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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.

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DO - 10.3389/fchem.2018.00106

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JO - Frontiers in Chemistry

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