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

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.

• Fecha de publicación: 2010
• Institución: Universidad del Rosario
• Repositorio: Repositorio EdocUR - U. Rosario
• Idioma: eng
• OAI Identifier: oai:repository.urosario.edu.co:10336/23454
• Acceso en línea: https://doi.org/10.1016/j.vaccine.2010.01.004; https://repository.urosario.edu.co/handle/10336/23454
• Palabra clave: Cell receptor; Cytoadherence linked asexual protein 9; 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; 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; falciparum; Malaria
• License: Abierto (Texto Completo)