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J.M. Lozano, M.P. Alba, M. Vanegas, Y. Silva, J.L. Torres-Castellanos, M.E. Patarroyo

MSP-1 Malaria Pseudopeptide Analogs: Biological and Immunological Significance and Three-Dimensional Structure

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 ?[CH2-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.

Biological Chemistry, Walter de Gruyter

Print ISSN: 1431-6730
Volume: 384, 01/2003
Pages: 71 - 82

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