Abstract
A conserved high activity erythrocyte binding peptide (HAEBP) derived from the 175-erythrocyte binding antigen (EBA-175), coded 1758, was synthesized and analyzed for antigenic and protective activities in Aotus monkeys, together with several of its analogues. Conformational analysis by 1H Nuclear Magnetic Resonance in TFE-solution was done for some of them, as well as the 1758 parent peptide. We show that the conserved 1758 HAEBP (being neither immunogenic nor protective) has an α helical structure, whilst its analogues contain β-turn structures. The 13790 peptide (highly immunogenic and protective for some monkeys) shows a type I β-turn structure distorted in ψ i + 1 ψ i + 2 angles, whilst immunogenic and non-protective (as well as the non-immunogenic and non-protective peptides) have type III' β-turns. An understanding of native peptide's correlation with altered peptide three-dimensional structure and resulting immunogenicity and protective activity may lead to a more rational design of multi-antigenic, multi-stage P. falciparum subunit based malaria vaccines.
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