Ítem
Solo Metadatos

Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes

Título de la revista
Autores
Pinzón, Carlos Giovanni
Curtidor, Hernando
García, Jeison
Vanegas, Magnolia
Vizcaíno, Carolina
Patarroyo, Manuel A.
Patarroyo, Manuel E.

Fecha
2010

Directores

ISSN de la revista
Título del volumen
Editor

Buscar en:

Métricas alternativas

Resumen
Abstract
In this study, we synthesized the complete sequence of the CLAG-9 protein as 67 20-mer-long non-overlapped peptides and assessed their ability to bind to erythrocytes in receptor-ligand assays. Twenty CLAG-9 peptides were found to have specific high-affinity binding ability to erythrocytes (thereby named as HABPs), with nanomolar dissociation constants. CLAG-9 HABPs interacted with different erythrocyte surface receptors having apparent molecular weights of 85, 63 and 34 kDa. CLAG-9 HABPs binding was also affected by pre-treatment of RBCs with enzymes and inhibited erythrocyte invasion in vitro by up to 72% at 200 ?M. These results suggest that some protein fragments of CLAG-9 may be part of the molecular machinery used by malaria parasites to invade erythrocytes, hence supporting their study as possible vaccine candidates. © 2010 Elsevier Ltd. All rights reserved.
Palabras clave
Keywords
Cell receptor , falciparum , Protozoal protein , Unclassified drug , Amino acid sequence , Article , Binding affinity , Cell invasion , Dissociation constant , Erythrocyte , Human , Human cell , Molecular weight , Nonhuman , Plasmodium falciparum , Priority journal , Protein binding , Protein interaction , Protein synthesis , Amino acid sequence , Animals , Cell adhesion molecules , Erythrocytes , Humans , Kinetics , Malaria , Membrane proteins , Molecular sequence data , Molecular weight , Peptide hydrolases , Plasmodium falciparum , Protein binding , Protozoan proteins , Virulence factors , Antimalarial vaccine , Cytoadherence-linked asexual protein 9 , Plasmodium falciparum
Buscar en:
Colecciones