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MSP-1 Malaria Pseudopeptide Analogs: Biological and Immunological Significance and Three-Dimensional Structure
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J.M. Lozano
Published/Copyright:
June 1, 2005
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 ψ[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.
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Published Online: 2005-06-01
Published in Print: 2003-01-27
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
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