Phi (Φ) and psi (Ψ) angles involved in malarial peptide bonds determine sterile protective immunity

Manuel E Patarroyo; Armando Moreno-Vranich; Adriana Bermúdez

doi:10.1016/j.bbrc.2012.10.089

Phi (Φ) and psi (Ψ) angles involved in malarial peptide bonds determine sterile protective immunity

Título traducido de la contribución: Los ángulos phi ( Φ ) y psi ( Ψ ) implicados en los enlaces peptídicos de la malaria determinan la inmunidad protectora estéril

Manuel E Patarroyo
, Armando Moreno-Vranich
, Adriana Bermúdez

Escuela de Medicina y Ciencias de la Salud

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

16 Citas (Scopus)

Resumen

Las regiones de HABP modificadas (mHABP) que interactúan con moléculas HLA-DRβ1 ∗ tienen una conformación y/o secuencia más restringida que otras mHABP que no encajan perfectamente en sus regiones de unión a péptidos (PBR) y no inducen una respuesta inmune aceptable debido a las condiciones críticas . papel de sus ángulos de torsión Φ y Ψ . El papel crítico de estos ángulos se determinó en una respuesta altamente inmunogénica e inductora de protección contra la malaria experimental utilizando los confórmeros (mHABP) obtenidos por 1H -NMR y superpuestos en moléculas de mono Aotus similares a HLA-DRβ1 ∗ ; Se midieron sus ángulos phi ( Φ ) y psi ( Ψ ) y se evaluó la formación de enlaces H entre estas moléculas. La propensión antes mencionada de mHABP a asumir una conformación regular similar a una hélice de poliprolina tipo II zurda (PPII L ) llevó a sugerir que favorecer estas conformaciones según su secuencia de aminoácidos conduciría a una producción elevada de títulos de anticuerpos y a una inducción de inmunidad protectora estéril contra la malaria. , añadiendo así nuevos principios o reglas para el desarrollo de vacunas, siendo la malaria una de ellas.

Título traducido de la contribución	Los ángulos phi ( Φ ) y psi ( Ψ ) implicados en los enlaces peptídicos de la malaria determinan la inmunidad protectora estéril
Idioma original	Inglés estadounidense
Páginas (desde-hasta)	75-80
Número de páginas	6
Publicación	Biochemical and Biophysical Research Communications
Volumen	429
N.º	1-2
DOI	https://doi.org/10.1016/j.bbrc.2012.10.089
Estado	Publicada - dic. 7 2012

ODS de las Naciones Unidas

Este resultado contribuye a los siguientes Objetivos de Desarrollo Sostenible

ODS 3: Salud y bienestar

Áreas temáticas de ASJC Scopus

Microbiología (médica)

Acceder al documento

10.1016/j.bbrc.2012.10.089

Citar esto

@article{85071b1943474735a822e6410b8e7d1f,

title = "Phi (Φ) and psi (Ψ) angles involved in malarial peptide bonds determine sterile protective immunity",

abstract = "Modified HABP (mHABP) regions interacting with HLA-DRβ1(∗) molecules have a more restricted conformation and/or sequence than other mHABPs which do not fit perfectly into their peptide binding regions (PBR) and do not induce an acceptable immune response due to the critical role of their Φ and Ψ torsion angles. These angle's critical role was determined in such highly immunogenic, protection-inducing response against experimental malaria using the conformers (mHABPs) obtained by (1)H-NMR and superimposed into HLA-DRβ1(∗)-like Aotus monkey molecules; their phi (Φ) and psi (Ψ) angles were measured and the H-bond formation between these molecules was evaluated. The aforementioned mHABP propensity to assume a regular conformation similar to a left-handed polyproline type II helix (PPII(L)) led to suggesting that favouring these conformations according to their amino acid sequence would lead to high antibody titre production and sterile protective immunity induction against malaria, thereby adding new principles or rules for vaccine development, malaria being one of them.",

author = "Patarroyo, \{Manuel E\} and Armando Moreno-Vranich and Adriana Berm{\'u}dez",

year = "2012",

month = dec,

day = "7",

doi = "10.1016/j.bbrc.2012.10.089",

language = "English (US)",

volume = "429",

pages = "75--80",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier BV",

number = "1-2",

}

Phi (Φ) and psi (Ψ) angles involved in malarial peptide bonds determine sterile protective immunity. / Patarroyo, Manuel E; Moreno-Vranich, Armando; Bermúdez, Adriana.
En: Biochemical and Biophysical Research Communications, Vol. 429, N.º 1-2, 07.12.2012, p. 75-80.

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

TY - JOUR

T1 - Phi (Φ) and psi (Ψ) angles involved in malarial peptide bonds determine sterile protective immunity

AU - Patarroyo, Manuel E

AU - Moreno-Vranich, Armando

AU - Bermúdez, Adriana

PY - 2012/12/7

Y1 - 2012/12/7

N2 - Modified HABP (mHABP) regions interacting with HLA-DRβ1(∗) molecules have a more restricted conformation and/or sequence than other mHABPs which do not fit perfectly into their peptide binding regions (PBR) and do not induce an acceptable immune response due to the critical role of their Φ and Ψ torsion angles. These angle's critical role was determined in such highly immunogenic, protection-inducing response against experimental malaria using the conformers (mHABPs) obtained by (1)H-NMR and superimposed into HLA-DRβ1(∗)-like Aotus monkey molecules; their phi (Φ) and psi (Ψ) angles were measured and the H-bond formation between these molecules was evaluated. The aforementioned mHABP propensity to assume a regular conformation similar to a left-handed polyproline type II helix (PPII(L)) led to suggesting that favouring these conformations according to their amino acid sequence would lead to high antibody titre production and sterile protective immunity induction against malaria, thereby adding new principles or rules for vaccine development, malaria being one of them.

AB - Modified HABP (mHABP) regions interacting with HLA-DRβ1(∗) molecules have a more restricted conformation and/or sequence than other mHABPs which do not fit perfectly into their peptide binding regions (PBR) and do not induce an acceptable immune response due to the critical role of their Φ and Ψ torsion angles. These angle's critical role was determined in such highly immunogenic, protection-inducing response against experimental malaria using the conformers (mHABPs) obtained by (1)H-NMR and superimposed into HLA-DRβ1(∗)-like Aotus monkey molecules; their phi (Φ) and psi (Ψ) angles were measured and the H-bond formation between these molecules was evaluated. The aforementioned mHABP propensity to assume a regular conformation similar to a left-handed polyproline type II helix (PPII(L)) led to suggesting that favouring these conformations according to their amino acid sequence would lead to high antibody titre production and sterile protective immunity induction against malaria, thereby adding new principles or rules for vaccine development, malaria being one of them.

U2 - 10.1016/j.bbrc.2012.10.089

DO - 10.1016/j.bbrc.2012.10.089

M3 - Research Article

C2 - 23142598

SN - 0006-291X

VL - 429

SP - 75

EP - 80

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1-2

ER -

Phi (Φ) and psi (Ψ) angles involved in malarial peptide bonds determine sterile protective immunity

Resumen

ODS de las Naciones Unidas

Áreas temáticas de ASJC Scopus

Acceder al documento

Huella

Citar esto