Biochemistry Z 0250 Intimate Molecular Interactions of P. falciparum Merozoite Proteins Involved in Invasion of Red Blood Cells and Their Implications for Vaccine Design -[443 refs.]. -(RODRIGUEZ, L. E.; CURTIDOR, H.; URQUIZA, M.; CIFUENTES, G.; REYES, C.; PATARROYO*, M. E.; Chem. Rev. (Washington, D. C.) 108 (2008) 9, 3656-3705; Inst. Immunol., Univ. Nac. Colombia, Bogota, Colombia; Eng.) -Lindner 50-274

in 1991. The principal focus of his research at the Fundación Instituto de Inmunología de Colombia is the molecular characterization of receptor-ligand interactions between pathogenic proteins involved in invasion and their corresponding host cell receptors, mainly for P. falciparum and M. tuberculosis. He is currently candidate for a Dr. Sc. degree in chemistry at the Universidad Nacional de Colombia.Mauricio Urquiza graduated in chemistry at the Universidad Nacional de Colombia in 1991. He is currently working as a researcher in the Virology department at the Fundación Instituto de Inmunología de Colombia and is candidate for a Dr. Sc. degree in chemistry at the Universidad Nacional de Colombia. The main focus of his research is the study of the host-parasite interactions, using as model P. falciparum, P. vivax, Human Papilloma virus, and Epstein-Barr virus. He is also working in the development of a Human Papilloma virus detection test.Gladys Cifuentes graduated in chemistry at the Universidad Nacional de Colombia in 1994 and is a member of the Nuclear Magnetic Resonance and Molecular Design section of the Three-Dimensional Structure Department at the Fundación Instituto de Inmunología de Colombia. Her research interests include 3D-structure and molecular design of peptides and proteins with shown biological and chemical relevance in host-parasite interactions.

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.

Developing a rational methodology for obtaining vaccines against P. falciparum malaria (the disease's most lethal form, afflicting more than 250 million people around the world per year and killing about 2 million of them) [1] has become one of the main objectives of public health authorities around the world. [2] A multiantigenic vaccine, containing molecules from the parasite's different developmental stages, is required due to the parasite's remarkable complexity and adaptability. [3] The first such approach (the SPf66 synthetic vaccine), [4,5] which used peptides from molecules from different parasite stages, conferred limited protective efficacy in Aotus monkey studies and in field trials carried out on human volunteers around the world. [6] [a] Prof.