The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles
Título de la revista
Patarroyo, Manuel E.
Alba, Martha P.
The importance of CSP- and STARP-derived ? and ? dihedral angles in mHABP structure was analysed by 1H NMR in the search for molecules which can be included as components of a first-line-of-defence Plasmodium falciparum sporozoite multi-epitope vaccine against the most lethal form of human malaria. Most of the aforementioned dihedral angles were left-hand-like polyproline type II (PPIIL) structures whilst others had right-hand-like ?-helix (?R), thus allowing mHABPS to fit better into MHCII molecules and thereby form an appropriate pMHCII complex and also establish the H-bonds which stabilise such complex and by this means induce an appropriate immune response. This information has great implications for vaccine development, malaria being one of them. © 2012 Elsevier Inc.
Binding protein , secondary , High activity binding peptide , Major histocompatibility antigen class 2 , Proline , Protozoal protein , Sporozoite threonine and asparagine rich protein , Sporozoite vaccine , Unclassified drug , Alpha helix , Amino acid sequence , Article , Complex formation , Hydrogen bond , Immunogenicity , Plasmodium falciparum , Priority journal , Protein structure , Proton nuclear magnetic resonance , Amino acid sequence , Animals , Antigens , Aotus trivirgatus , Hla-dr beta-chains , Humans , Malaria vaccines , Molecular sequence data , Nuclear magnetic resonance , Peptide fragments , Peptides , Plasmodium falciparum , Protein structure , Protozoan proteins , Sporozoites , Plasmodium falciparum , ? and ? angles , Antimalarial-vaccine , Hladr?* molecules , Plasmodium falciparum , Pre-erythrocyte stage