Analysis of a Plasmodium falciparum EBA-175 peptide with high binding capacity to erythrocytes and their analogues using 1H NMR.
A 175-erythrocyte-binding protein (EBA-175) conserved high-activity binding peptide (HABP), called 1783 (nonimmunogenic, nonprotective against Plasmodium falciparum malaria), was analyzed for antigenic and protective activity in Aotus monkeys, together with several of its analogues. 1H NMR studies of peptides 17912, 14016, and 22814 allowed their structure to be related to their biological function. These peptides showed helical regions having differences in their position and length. Nonimmunogenic, nonprotective peptides 1783 and 17912 showed an extensive helical region, while the 22814 immunogenic protective peptide's alpha-helix was found in the N-terminal region. This suggests that the more flexible C-terminal region will allow better interaction between these peptides and immune system molecules as well as relating these peptides' three-dimensional structure to their immunogenicity and protective activity, thus leading to a more rational development of the new malaria multicomponent vaccine.
Cifuentes
Gladys
G
Fundación Instituto de Inmunología de Colombia (FIDIC), Universidad Nacional de Colombia, Carrera 50 No. 26-00, Santa fe de Bogota, Colombia.
Guzmán
Fanny
F
Alba
Martha Patricia
MP
Salazar
Luz Mary
LM
Patarroyo
Manuel Elkin
ME
D000595:Amino Acid Sequence; D000818:Animals; D001029:Aotus trivirgatus; D015153:Blotting, Western; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010452:Peptide Biosynthesis; D010455:Peptides / Q000737:chemistry; D010963:Plasmodium falciparum / Q000378:metabolism*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D010455:Peptides