Distorting malaria peptide backbone structure to enable fitting into MHC class II molecules renders modified peptides immunogenic and protective.

Gladys Cifuentes; Manuel Elkin Patarroyo; Mauricio Urquiza; Luis E Ramirez; Claudia Reyes; Raul Rodriguez

doi:10.1021/jm020440w

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Distorting malaria peptide backbone structure to enable fitting into MHC class II molecules renders modified peptides immunogenic and protective.

Gladys Cifuentes·Manuel Elkin Patarroyo·Mauricio Urquiza·Luis E Ramirez·Claudia Reyes·Raul Rodriguez

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Abstract

The conserved, nonantigenic, nonimmunogenic malaria Merozoite Surface Protein-2 peptide 1, having high affinity for red blood cells, was rendered immunogenic and protective in Aotus monkeys by specifically changing some critical residues. The NMR structure revealed a switch from classical type III' into distorted III' and III beta turns in the protective peptides. These changes may lead to a better fit into the Aotus MHC class II human HLA-DRbeta1 12 molecule equivalent, thus activating the immune system.

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Animals Antigens, Protozoan Aotidae Histocompatibility Antigens Class II Magnetic Resonance Spectroscopy Malaria, Falciparum Models, Molecular Peptides Plasmodium falciparum Protein Conformation Protozoan Proteins Vaccination Journal Article Research Support, Non-U.S. Gov't

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Gladys Cifuentes, Manuel Elkin Patarroyo, Mauricio Urquiza, Luis E Ramirez, Claudia Reyes, Raul Rodriguez. 2003-05-22. Distorting malaria peptide backbone structure to enable fitting into MHC class II molecules renders modified peptides immunogenic and protective.. https://doi.org/10.1021/jm020440w

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