TAILIEUCHUNG - Báo cáo khoa học: Modified merozoite surface protein-1 peptides with short alpha helical regions are associated with inducing protection against malaria

The merozoite surface protein-1 represents a prime candi-date for development of a malaria vaccine. Merozoite sur-face protein-1 has been shown to demonstrate high-activity peptide binding to human red blood cells. One of the high-activity binding peptides, named 5501, located in the N-terminus (amino acid sequence MLNISQHQCVKKQ CPQNS) of the 19-kDa molecular mass fragment of mero-zoite surface protein-1, is conserved, nonimmunogenic and nonprotective. | Eur. J. Biochem. 270 3946-3952 2003 FEBS 2003 doi Modified merozoite surface protein-1 peptides with short alpha helical regions are associated with inducing protection against malaria Marv H. Torres1 Luz M. Salazar1 Maanolia Vaneaas1 Fannv Guzman1. Raul Rodriauez1 Yolanda Silva1 . . Jaiver Rosas1 and Manuel E. Patarroyo1 2 1Fundacion Instituto de Inmunologla de Colombia FIDIC Bogota Colombia 2Universidad National de Colombia Bogota Colombia The merozoite surface protein-1 represents a prime candidate for development of a malaria vaccine. Merozoite surface protein-1 has been shown to demonstrate high-activity peptide binding to human red blood cells. One of the high-activity binding peptides named 5501 located in the N-terminus amino acid sequence MLNISQHQCVKKQ CPQNS of the 19-kDa molecular mass fragment of mero-zoite surface protein-1 is conserved nonimmunogenic and nonprotective. Its critical binding residues were identified and replaced with amino acids of similar mass but different charge in order to modify their immunogenic and protective characteristics. Three analogues with positive or negative immunological results were studied by nuclear magnetic resonance to correlate their three-dimensional structure with their biological functions. The studied peptides presented a-helical fragments but in different peptide regions and extensions except for randomly structured 5501. We show that altering a few amino acids induced immunogenicity and protectivity against experimental malaria and changed the peptide three-dimensional structure suggesting a better fit with immune-system molecules. Keywords MSP-1 protein peptide analogues nuclear magnetic resonance vaccine candidate. Multiple receptor-ligand type interactions are involved in the host-cell invasion process of the Plasmodium falciparum malaria parasite 1-3 allowing the entry and survival of this deadly parasite. More than 250 miliion pcopIc are infected with P. falciparum .

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