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 Eduardo Vargas, Zuly J. Rivera, Manuel Elkin Patarroyo

Research output: Contribution to journalArticle

15 Citations (Scopus)

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
Original languageEnglish (US)
Pages (from-to)119-125
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume322
Issue number1
DOIs
StatePublished - Sep 10 2004

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

Cite this

Bermudez Quintero, A. J., Salazar, L. M., Alba, M. P., Curtidor, H., Vargas, L. E., 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 ; Vargas, Luis Eduardo ; Rivera, Zuly J. ; Patarroyo, Manuel Elkin. / Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing. In: Biochemical and Biophysical Research Communications. 2004 ; Vol. 322, No. 1. pp. 119-125.
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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",
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Bermudez Quintero, AJ, Salazar, LM, Alba, MP, Curtidor, H, Vargas, LE, 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, no. 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; Vargas, Luis Eduardo; Rivera, Zuly J.; Patarroyo, Manuel Elkin.

In: Biochemical and Biophysical Research Communications, Vol. 322, No. 1, 10.09.2004, p. 119-125.

Research output: Contribution to journalArticle

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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 - Vargas, Luis Eduardo

AU - Rivera, Zuly J.

AU - Patarroyo, Manuel Elkin

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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

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