Atomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malaria

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 i...

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Autores:
Tipo de recurso:
Fecha de publicación:
2010
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/23507
Acceso en línea:
https://doi.org/10.1016/j.bbrc.2010.03.004
https://repository.urosario.edu.co/handle/10336/23507
Palabra clave:
Malaria vaccine
Parasite antigen
Amino acid composition
Animal experiment
Animal model
Aotus
Article
Controlled study
Host resistance
Hydrogen bond
Immunogenicity
Malaria falciparum
Nonhuman
Physical chemistry
Plasmodium falciparum
Priority journal
Vaccine production
Amino acid sequence
Animals
Aotus trivirgatus
Host-parasite interactions
Hydrogen bonding
Malaria
Malaria vaccines
Molecular sequence data
Peptides
Protein conformation
Plasmodium falciparum
H-bonds
Malaria
Plasmodium falciparum
Sterile immunity
x-ray
protozoan
protozoan
biomolecular
Antibodies
Antigens
Crystallography
Nuclear magnetic resonance
Rights
License
Abierto (Texto Completo)