Atomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malaria.
Biochem Biophys Res Commun
; 394(3): 529-35, 2010 Apr 09.
Article
em En
| MEDLINE
| ID: mdl-20206601
ABSTRACT
Based on the 3D X-ray crystallographic structures of relevant proteins of the malaria parasite involved in invasion to host cells and 3D NMR structures of High Activity Binding Peptides (HABPs) and their respective analogues, it was found that HABPs are rendered into highly immunogenic and sterile immunity inducers in the Aotus experimental model by modifying those amino acids that establish H-bonds with other HABPs or binding to host's cells. This finding adds striking and novel physicochemical principles, at the atomic level, for a logical and rational vaccine development methodology against infectious disease, among them malaria.
Texto completo:
1
Coleções:
01-internacional
Contexto em Saúde:
2_ODS3
/
3_ND
Base de dados:
MEDLINE
Assunto principal:
Vacinas Antimaláricas
/
Interações Hospedeiro-Parasita
/
Malária
/
Antígenos de Protozoários
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
2010
Tipo de documento:
Article