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

Carlos Giovanni Pinzón, Hernando Curtidor, Jeison García, Magnolia Vanegas, Carolina Vizcaíno, Manuel A. Patarroyo, Manuel E. Patarroyo

Resultado de la investigación: Contribución a una revistaArtículo

7 Citas (Scopus)


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 μM. 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.
Idioma originalInglés estadounidense
Páginas (desde-hasta)2653-2663
Número de páginas11
EstadoPublicada - mar 19 2010

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