Evaluación del efecto in vitro de anticuerpos inducidos por péptido-miméticos derivados del antígeno de superficie de merozoito-2 de Plasmodium en malaria causada por Plasmodium yoelii y Plasmodium berghei en ratones BALB/c

based on previous studies in which those residues being critical for plasmodium falciparum binding to red blood cells (rbcs) through the antigenic sequence ( 21 kneskysntfinnaynmsir 40 ) from the merozoite surface antigen-2 (msp-2) were identified, we have designed and synthesized two reduced amide pseudopeptide sequences based on the 31 in 32 binding motif. synthesized peptido- mimetics, possess each one a modified peptide bond that presented as a ψ [ch2-nh] reduced amide isoster bond, to allowing the phe-ile modified aminoacid pair allowing pseudopeptides coded ψ-128 (monomer form) and ψ-129 (polymer form) and the ile-asn modified aminoacid pair for pseudopeptides coded ψ-130 (monomer form) and ψ-131 (polymer form). by using the polymer forms of both peptido-mimetics as immunogens, monoclonal antibodies were produced in balb/c mice. these ig showed an igm isotype. the isotype antibody switching was lead by in vitro immunization of the original hybridomas. isolated immunoglobulins were tested for their functional in vitro activity, on a infection controlled experiment of rodent plasmodium strains infecting red blood cells. obtained results reveal the role played by anti- bodies to peptido-mimetic in infection assays performed further on animal experimental models.