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A single amino acid change in the Plasmodium falciparum RH5 (PfRH5) human RBC binding sequence modifies its structure and determines species-specific binding activity

Identifying the ligands or regions derived from them which parasites use to invade their target cells has proved to be an excellent strategy for identifying targets for vaccine development. Members of the reticulocyte-binding homologue family (P. fRH), including RH5, have been implicated in invasion...

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Detalles Bibliográficos
Autores Principales: Arévalo-Pinzón, Gabriela, Curtidor, Hernando, Muñoz, Marina, Patarroyo, Manuel A., Bermudez, Adriana, Patarroyo, Manuel E.
Formato: Artículo (Article)
Lenguaje:Inglés (English)
Publicado: 2012
Materias:
Binding protein
Chloroquine
Malaria vaccine
Membrane protein
Plasmodium falciparum rh5 protein
Trypsin
Unclassified drug
Amino acid analysis
Amino acid sequence
Article
Binding affinity
Binding competition
Blood sampling
Competitive inhibition
Controlled study
Erythrocyte
Female
Hela cell
Human
Human cell
Immunogenicity
Parasitemia
Peptide mapping
Plasmodium falciparum
Polyacrylamide gel electrophoresis
Priority journal
Protein modification
Protein structure
Protein synthesis
Reversed phase high performance liquid chromatography
Sequence analysis
Structure activity relation
Structure analysis
Western blotting
Amino acid substitution
Animals
Aotus trivirgatus
Carrier proteins
Cell adhesion
Erythrocytes
Humans
Molecular sequence data
Mutant proteins
Protein binding
Protein conformation
Sequence alignment
Malaria
Peptide
Receptor
Red blood cell
Structure-activity relationship
Vaccine
missense
Mutation
Acceso en línea:https://repository.urosario.edu.co/handle/10336/23459
https://doi.org/10.1016/j.vaccine.2011.11.012

Internet

https://repository.urosario.edu.co/handle/10336/23459
https://doi.org/10.1016/j.vaccine.2011.11.012

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