Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion

Plasmodium falciparum malaria parasite invasion of erythrocytes is an essential step in host infection and the proteins involved in such invasion are the main target in developing an antimalarial vaccine. Secretory organelle-derived proteins (micronemal AMA1 protein and the RON2, 4, and 5 rhoptry ne...

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Autores:
Tipo de recurso:
Fecha de publicación:
2014
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/22793
Acceso en línea:
https://doi.org/10.1016/j.peptides.2013.07.028
https://repository.urosario.edu.co/handle/10336/22793
Palabra clave:
Chymotrypsin
Peptide derivative
Plasmodium falciparum rhoptry neck protein 5 peptide derivative
Protein
Ron5 protein
Trypsin
Unclassified drug
Malaria vaccine
Protozoal protein
Article
Assay
Cell interaction
Cell invasion
Controlled study
Erythrocyte
Human
Human cell
Merozoite
Plasmodium falciparum
Priority journal
Protein binding
Receptor ligand interaction assay
Cell culture
Circular dichroism
Erythrocyte
Immunoelectron microscopy
Immunology
Metabolism
Parasitology
Pathogenicity
Plasmodium falciparum
Circular dichroism
Erythrocytes
Humans
Malaria vaccines
Merozoites
Plasmodium falciparum
Protozoan proteins
Binding
Malaria
Merozoite
Rhoptry neck
Synthetic peptide
immunoelectron
cultured
Cells
Microscopy
Rights
License
Abierto (Texto Completo)
Description
Summary:Plasmodium falciparum malaria parasite invasion of erythrocytes is an essential step in host infection and the proteins involved in such invasion are the main target in developing an antimalarial vaccine. Secretory organelle-derived proteins (micronemal AMA1 protein and the RON2, 4, and 5 rhoptry neck proteins) have been recently described as components of moving junction complex formation allowing merozoites to move into a newly created parasitophorous vacuole. This study led to identifying RON5 regions involved in binding to human erythrocytes by using a highly robust, sensitive and specific receptor-ligand interaction assay; it is further shown that the RON5 protein remains highly conserved throughout different parasite strains. It is shown that the binding peptide-erythrocyte interaction is saturable and sensitive to chymotrypsin and trypsin. Invasion inhibition assays using erythrocyte binding peptides showed that the RON5-erythrocyte interaction could be critical for merozoite invasion of erythrocytes. This work provides evidence (for the first time) suggesting a fundamental role for RON5 in erythrocyte invasion. © 2013 Elsevier Inc.