Actividad funcional de anticuerpos inducidos por péptido-miméticos derivados del antígeno MSP-2 del Plasmodium, como potenciales agentes inmunoterapéuticos en malaria causada por Plasmodium yoelii y Plasmodium berghei en ratones BALB/c

bearing in mind the high degree of genetical conservation of critical binding residues from the primary structure of the peptide 4044 ( 21 kneskysnt- finnaynmsir 40 ), which was previously identified as being crucial for the msp-2 antigen to lead plasmodium falciparum to bind red blood cells with high specific capacity, and so causing malaria, two peptido-mimetics so-named reduced amide pseudopeptides, in which a nature-made amide bond was replaced with a ψ[ch 2 -nh] methylene amide isoster bond, one between the phe-ile aminoacid pair and the second between ile-asn, were designed and synthesized in a site-directed manner as monomer and polymer forms, and were coded as ψ-128 for the monomer (ψ-129 polymer) and ψ-130 for the monomer (ψ-131 for polymer) respectively. these peptido-mimetics were used to produce monoclonal antibodies which displayed in both cases igm isotype. by controlled in vitro immunization experiments their parent reactive hybridomas were induced to a ig isotype-switching to igg1, igg2a, igg2b and igg3 sub-classes. these immunoglobulins were tested for their in vivo functional activity against malaria, showing a high efficacy property for controlling the malaria infection when passively transferred into balb/c mice. the neutralizing effect of these site-directed designed antibodies on the plasmodium biological development, make them a potential tool for the control of malaria