HLA-DR allele reading register shifting is associated with immunity induced by SERA peptide analogues

Adriana Janneth Bermudez Quintero, Manuel Elkin Patarroyo, Luz M. Salazar

Resultado de la investigación: Contribución a RevistaArtículo

2 Citas (Scopus)

Resumen

SERA protein is a leading candidate molecule to be included in an antimalarial vaccine. Conserved high activity binding peptides (HABP) binding to red blood cells (RBC) have been identified in this protein. One of them (6762) localising in the 18-kDa C-terminal fragment was used to induce protective immunity with negative result. Critical RBC binding residues (assessed by glycine-analogue scanning) were replaced by others having the same mass, volume and surface but different polarity, rendering some of them immunogenic as assessed by antibody production against the parasite or its proteins and protection-inducing against challenge with a highly infectious Aotus monkey-adapted Plasmodium falciparum strain. A shift in binding to purified HLA-DR allelic molecules from the same haplotype and in their reading register was found, suggesting that modified molecules had adopted a different (1)H NMR 3D structure allowing a better fit into the MHCII-pept-TCR complex, thereby representing a new mechanism for inducing immune protection
Idioma originalEnglish (US)
Páginas (desde-hasta)114-120
Número de páginas6
PublicaciónBiochemical and Biophysical Research Communications
Volumen372
N.º1
DOI
EstadoPublished - jul 18 2008

Huella dactilar

HLA-DR Antigens
Reading
Immunity
Alleles
Peptides
Molecules
Blood
Erythrocytes
Proteins
Antimalarials
Plasmodium falciparum
Glycine
Haplotypes
Antibody Formation
Haplorhini
Parasites
Vaccines
Cells
Nuclear magnetic resonance
Scanning

Citar esto

Bermudez Quintero, Adriana Janneth ; Patarroyo, Manuel Elkin ; Salazar, Luz M. / HLA-DR allele reading register shifting is associated with immunity induced by SERA peptide analogues. En: Biochemical and Biophysical Research Communications. 2008 ; Vol. 372, N.º 1. pp. 114-120.
@article{05966bf18d2d45cf83289bd85b0a817c,
title = "HLA-DR allele reading register shifting is associated with immunity induced by SERA peptide analogues",
abstract = "SERA protein is a leading candidate molecule to be included in an antimalarial vaccine. Conserved high activity binding peptides (HABP) binding to red blood cells (RBC) have been identified in this protein. One of them (6762) localising in the 18-kDa C-terminal fragment was used to induce protective immunity with negative result. Critical RBC binding residues (assessed by glycine-analogue scanning) were replaced by others having the same mass, volume and surface but different polarity, rendering some of them immunogenic as assessed by antibody production against the parasite or its proteins and protection-inducing against challenge with a highly infectious Aotus monkey-adapted Plasmodium falciparum strain. A shift in binding to purified HLA-DR allelic molecules from the same haplotype and in their reading register was found, suggesting that modified molecules had adopted a different (1)H NMR 3D structure allowing a better fit into the MHCII-pept-TCR complex, thereby representing a new mechanism for inducing immune protection",
author = "{Bermudez Quintero}, {Adriana Janneth} and Patarroyo, {Manuel Elkin} and Salazar, {Luz M.}",
year = "2008",
month = "7",
day = "18",
doi = "10.1016/j.bbrc.2008.04.186",
language = "English (US)",
volume = "372",
pages = "114--120",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

HLA-DR allele reading register shifting is associated with immunity induced by SERA peptide analogues. / Bermudez Quintero, Adriana Janneth; Patarroyo, Manuel Elkin; Salazar, Luz M.

En: Biochemical and Biophysical Research Communications, Vol. 372, N.º 1, 18.07.2008, p. 114-120.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - HLA-DR allele reading register shifting is associated with immunity induced by SERA peptide analogues

AU - Bermudez Quintero, Adriana Janneth

AU - Patarroyo, Manuel Elkin

AU - Salazar, Luz M.

PY - 2008/7/18

Y1 - 2008/7/18

N2 - SERA protein is a leading candidate molecule to be included in an antimalarial vaccine. Conserved high activity binding peptides (HABP) binding to red blood cells (RBC) have been identified in this protein. One of them (6762) localising in the 18-kDa C-terminal fragment was used to induce protective immunity with negative result. Critical RBC binding residues (assessed by glycine-analogue scanning) were replaced by others having the same mass, volume and surface but different polarity, rendering some of them immunogenic as assessed by antibody production against the parasite or its proteins and protection-inducing against challenge with a highly infectious Aotus monkey-adapted Plasmodium falciparum strain. A shift in binding to purified HLA-DR allelic molecules from the same haplotype and in their reading register was found, suggesting that modified molecules had adopted a different (1)H NMR 3D structure allowing a better fit into the MHCII-pept-TCR complex, thereby representing a new mechanism for inducing immune protection

AB - SERA protein is a leading candidate molecule to be included in an antimalarial vaccine. Conserved high activity binding peptides (HABP) binding to red blood cells (RBC) have been identified in this protein. One of them (6762) localising in the 18-kDa C-terminal fragment was used to induce protective immunity with negative result. Critical RBC binding residues (assessed by glycine-analogue scanning) were replaced by others having the same mass, volume and surface but different polarity, rendering some of them immunogenic as assessed by antibody production against the parasite or its proteins and protection-inducing against challenge with a highly infectious Aotus monkey-adapted Plasmodium falciparum strain. A shift in binding to purified HLA-DR allelic molecules from the same haplotype and in their reading register was found, suggesting that modified molecules had adopted a different (1)H NMR 3D structure allowing a better fit into the MHCII-pept-TCR complex, thereby representing a new mechanism for inducing immune protection

UR - http://www.sciencedirect.com/science/article/pii/S0006291X08008772?via%3Dihub

U2 - 10.1016/j.bbrc.2008.04.186

DO - 10.1016/j.bbrc.2008.04.186

M3 - Article

VL - 372

SP - 114

EP - 120

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -