2mu9
Changing ABRA protein peptide to fit the HLA-DR B1*0301 molecule renders it protection-inducing
Structural highlights
FunctionMSP9_PLAF7 During the asexual blood stage, involved in the sialic acid-independent (SAID) merozoite invasion of host erythrocytes by binding to host SLC4A1/Band 3 protein on the surface of the host erythrocyte.[1] Publication Abstract from PubMedThe 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. Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing.,Salazar LM, Alba MP, Curtidor H, Bermudez A, Luis E Vargas, Rivera ZJ, Patarroyo ME Biochem Biophys Res Commun. 2004 Sep 10;322(1):119-25. PMID:15313182[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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