MSP-1 malaria pseudopeptide analogs: biological and immunological significance and three-dimensional structure |
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Authors: | Lozano José Manuel Alba Martha Patricia Vanegas Magnolia Silva Yolanda Torres-Castellanos José Libardo Patarroyo Manuel Elkin |
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Institution: | Fundación Instituto de Inmunología de Colombia, Carrera 50 No. 26-00, Bogotá, Colombia. |
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Abstract: | Merozoite Surface Protein-1 (MSP-1) has been considered as a malaria vaccine candidate. It is processed during the Plasmodium falciparum invasion process of red blood cells (RBCs). A conserved MSP-1 C-terminal peptide was identified as a high-activity erythrocyte-binding peptide (HAEBP) termed 1585. Since conserved HAEBPs are neither antigenic nor immunogenic we decided to assess the significance of a single peptide bond replacement in 1585. Thus, two pseudopeptides were obtained by introducing a YCH2-NH] reduced amide isoster into the 1585 critical binding motif. The pseudopeptides bound to different HLA-DR alleles, suggesting that backbone modifications affect MHC-II binding patterns. Pseudopeptide-antibodies inhibit in vitro parasite RBC invasion by recognizing MSP-1. Each pseudopeptide-induced antibody shows distinct recognition patterns. 1H-NMR studies demonstrated that isoster bonds modulate the pseudopeptides' structure and thus their immunological properties, therefore representing a possible subunit malaria vaccine component. |
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