Distorting malaria peptide backbone structure to enable fitting into MHC class II molecules renders modified peptides immunogenic and protective.
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.
Fundación Instituto de Inmunología de Colombia, Carrera 50 No. 26-00 Bogotá, Colombia.
Gladys
G
Cifuentes
Manuel Elkin
ME
Patarroyo
Mauricio
M
Urquiza
Luis E
LE
Ramirez
Claudia
C
Reyes
Raul
R
Rodriguez
D000818:Animals; D000953:Antigens, Protozoan / Q000737:chemistry* / Q000276:immunology; D016645:Aotidae; D000949:Histocompatibility Antigens Class II / Q000276:immunology*; D009682:Magnetic Resonance Spectroscopy; D016778:Malaria, Falciparum / Q000276:immunology / Q000517:prevention & control; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry* / Q000276:immunology; D010963:Plasmodium falciparum / Q000276:immunology; D011487:Protein Conformation; D015800:Protozoan Proteins / Q000737:chemistry* / Q000276:immunology; D014611:Vaccination
D000953:Antigens, Protozoan; D000949:Histocompatibility Antigens Class II; D010455:Peptides; D015800:Protozoan Proteins; C065974:merozoite surface protein 2, Plasmodium