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 Castellanos, Luis Eduardo Vargas, Zuly J. Rivera, Manuel Elkin Patarroyo

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

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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