Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing

Adriana Janneth Bermudez Quintero, Luz Mary Salazar, Martha Patricia Alba, Hernando Curtidor, Luis E Vargas, Zuly J. Rivera, Manuel Elkin Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

14 Citas (Scopus)

Resumen

The Plasmodium falciparum acidic-basic repeat antigen represents a potential malarial vaccine candidate. One of this protein's high activity binding peptides, named 2150 ((161)KMNMLKENVDYIQKNQNLFK(180)), is conserved, non-immunogenic, and non-protection-inducing. Analogue peptides whose critical binding residues (in bold) were replaced by amino-acids having similar mass but different charge were synthesized and tested to try to modify such immunological properties. These analogues' HLA-DRbeta1* molecule binding ability were also studied in an attempt to explain their biological mechanisms and correlate binding capacity and immunological function with their three-dimensional structure determined by (1)H NMR. A 3(10) distorted helical structure was identified in protective and immunogenic peptide 24922 whilst alpha-helical structure was found for non-immunogenic, non-protective peptides having differences in alpha-helical position. The changes performed on immunogenic, protection-inducing peptide 24922 allowed it to bind specifically to the HLA-DRbeta1*0301 molecule, suggesting that these changes may lead to better interaction with the MHC Class II-peptide-TCR complex rendering it immunogenic and protective, thus suggesting a new way of developing multi-component, sub-unit-based anti-malarial vaccines
Idioma originalEnglish (US)
Páginas (desde-hasta)119-125
Número de páginas7
PublicaciónBiochemical and Biophysical Research Communications
Volumen322
N.º1
DOI
EstadoPublished - sep 10 2004

Huella dactilar

Peptides
Molecules
Malaria Vaccines
Proteins
Antimalarials
Plasmodium falciparum
Nuclear magnetic resonance
Antigens
Amino Acids

Citar esto

Bermudez Quintero, A. J., Salazar, L. M., Alba, M. P., Curtidor, H., Luis E Vargas, Rivera, Z. J., & Patarroyo, M. E. (2004). Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing. Biochemical and Biophysical Research Communications, 322(1), 119-125. https://doi.org/10.1016/j.bbrc.2004.07.086
Bermudez Quintero, Adriana Janneth ; Salazar, Luz Mary ; Alba, Martha Patricia ; Curtidor, Hernando ; Luis E Vargas ; Rivera, Zuly J. ; Patarroyo, Manuel Elkin. / Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing. En: Biochemical and Biophysical Research Communications. 2004 ; Vol. 322, N.º 1. pp. 119-125.
@article{d662567a11f64b71835c2c84974d4765,
title = "Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing",
abstract = "The Plasmodium falciparum acidic-basic repeat antigen represents a potential malarial vaccine candidate. One of this protein's high activity binding peptides, named 2150 ((161)KMNMLKENVDYIQKNQNLFK(180)), is conserved, non-immunogenic, and non-protection-inducing. Analogue peptides whose critical binding residues (in bold) were replaced by amino-acids having similar mass but different charge were synthesized and tested to try to modify such immunological properties. These analogues' HLA-DRbeta1* molecule binding ability were also studied in an attempt to explain their biological mechanisms and correlate binding capacity and immunological function with their three-dimensional structure determined by (1)H NMR. A 3(10) distorted helical structure was identified in protective and immunogenic peptide 24922 whilst alpha-helical structure was found for non-immunogenic, non-protective peptides having differences in alpha-helical position. The changes performed on immunogenic, protection-inducing peptide 24922 allowed it to bind specifically to the HLA-DRbeta1*0301 molecule, suggesting that these changes may lead to better interaction with the MHC Class II-peptide-TCR complex rendering it immunogenic and protective, thus suggesting a new way of developing multi-component, sub-unit-based anti-malarial vaccines",
author = "{Bermudez Quintero}, {Adriana Janneth} and Salazar, {Luz Mary} and Alba, {Martha Patricia} and Hernando Curtidor and {Luis E Vargas} and Rivera, {Zuly J.} and Patarroyo, {Manuel Elkin}",
year = "2004",
month = "9",
day = "10",
doi = "10.1016/j.bbrc.2004.07.086",
language = "English (US)",
volume = "322",
pages = "119--125",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

Bermudez Quintero, AJ, Salazar, LM, Alba, MP, Curtidor, H, Luis E Vargas, Rivera, ZJ & Patarroyo, ME 2004, 'Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing', Biochemical and Biophysical Research Communications, vol. 322, n.º 1, pp. 119-125. https://doi.org/10.1016/j.bbrc.2004.07.086

Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing. / Bermudez Quintero, Adriana Janneth; Salazar, Luz Mary; Alba, Martha Patricia; Curtidor, Hernando; Luis E Vargas; Rivera, Zuly J.; Patarroyo, Manuel Elkin.

En: Biochemical and Biophysical Research Communications, Vol. 322, N.º 1, 10.09.2004, p. 119-125.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing

AU - Bermudez Quintero, Adriana Janneth

AU - Salazar, Luz Mary

AU - Alba, Martha Patricia

AU - Curtidor, Hernando

AU - Luis E Vargas, null

AU - Rivera, Zuly J.

AU - Patarroyo, Manuel Elkin

PY - 2004/9/10

Y1 - 2004/9/10

N2 - The Plasmodium falciparum acidic-basic repeat antigen represents a potential malarial vaccine candidate. One of this protein's high activity binding peptides, named 2150 ((161)KMNMLKENVDYIQKNQNLFK(180)), is conserved, non-immunogenic, and non-protection-inducing. Analogue peptides whose critical binding residues (in bold) were replaced by amino-acids having similar mass but different charge were synthesized and tested to try to modify such immunological properties. These analogues' HLA-DRbeta1* molecule binding ability were also studied in an attempt to explain their biological mechanisms and correlate binding capacity and immunological function with their three-dimensional structure determined by (1)H NMR. A 3(10) distorted helical structure was identified in protective and immunogenic peptide 24922 whilst alpha-helical structure was found for non-immunogenic, non-protective peptides having differences in alpha-helical position. The changes performed on immunogenic, protection-inducing peptide 24922 allowed it to bind specifically to the HLA-DRbeta1*0301 molecule, suggesting that these changes may lead to better interaction with the MHC Class II-peptide-TCR complex rendering it immunogenic and protective, thus suggesting a new way of developing multi-component, sub-unit-based anti-malarial vaccines

AB - The Plasmodium falciparum acidic-basic repeat antigen represents a potential malarial vaccine candidate. One of this protein's high activity binding peptides, named 2150 ((161)KMNMLKENVDYIQKNQNLFK(180)), is conserved, non-immunogenic, and non-protection-inducing. Analogue peptides whose critical binding residues (in bold) were replaced by amino-acids having similar mass but different charge were synthesized and tested to try to modify such immunological properties. These analogues' HLA-DRbeta1* molecule binding ability were also studied in an attempt to explain their biological mechanisms and correlate binding capacity and immunological function with their three-dimensional structure determined by (1)H NMR. A 3(10) distorted helical structure was identified in protective and immunogenic peptide 24922 whilst alpha-helical structure was found for non-immunogenic, non-protective peptides having differences in alpha-helical position. The changes performed on immunogenic, protection-inducing peptide 24922 allowed it to bind specifically to the HLA-DRbeta1*0301 molecule, suggesting that these changes may lead to better interaction with the MHC Class II-peptide-TCR complex rendering it immunogenic and protective, thus suggesting a new way of developing multi-component, sub-unit-based anti-malarial vaccines

UR - http://www.sciencedirect.com/science/article/pii/S0006291X04015803?via%3Dihub

U2 - 10.1016/j.bbrc.2004.07.086

DO - 10.1016/j.bbrc.2004.07.086

M3 - Article

VL - 322

SP - 119

EP - 125

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -