The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles

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....

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Autores:
Tipo de recurso:
Fecha de publicación:
2012
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/23512
Acceso en línea:
https://doi.org/10.1016/j.bbrc.2012.10.088
https://repository.urosario.edu.co/handle/10336/23512
Palabra clave:
Binding protein
Circumsporozoite protein
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
Aotus trivirgatus
Hla-dr beta-chains
Humans
Malaria vaccines
Molecular sequence data
Peptide fragments
Peptides
Plasmodium falciparum
Protozoan proteins
Sporozoites
Plasmodium falciparum
? and ? angles
Antimalarial-vaccine
Hladr?* molecules
Plasmodium falciparum
Pre-erythrocyte stage
secondary
protozoan
biomolecular
Antigens
Nuclear magnetic resonance
Protein structure
Rights
License
Abierto (Texto Completo)
Description
Summary: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.