Ítem
Acceso Abierto
A Maurer's cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membrane
Título de la revista
Autores
García, Jeison
Curtidor, Hernando
Gil, Olga L.
Vanegas, Magnolia
Patarroyo, Manuel E.
Resumen
Abstract
The membrane-associated histidine-rich protein-1 (MAHRP-1) is a Maurer's cleft-resident molecule that has been recently described as an important protein for the trafficking of PfEMP-1 to infected erythrocyte membrane, a major virulence factor. We have studied the specific interactions between 20-mer-long synthetic peptides spanning the complete MAHRP-1 sequence and erythrocytes. A high-activity binding peptide (HABP) with saturable binding to a 46-kDa erythrocyte membrane protein was identified and its binding was affected by chymotrypsin treatment. Random coil and ?-helical features were found in the HABP's structure. Our results suggest that MAHRP-1 specifically interacts with erythrocyte membrane through a 20-mer-long amino acid region, raising questions about this region's potential as a therapeutic target against malaria. © 2009 Elsevier Inc. All rights reserved.
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Keywords
Carrier proteins and binding proteins , Chymotrypsin , Erythrocyte membrane protein 1 , Protein habp , Protein mahrp 1 , Protozoal protein , Unclassified drug , Amino acid sequence , Article , Controlled study , Erythrocyte membrane , Nonhuman , Plasmodium falciparum , Priority journal , Protein analysis , Protein binding , Protein interaction , Protein localization , Protein structure , Amino acid sequence , Animals , Carrier proteins , Erythrocyte membrane , Molecular sequence data , Peptides , Plasmodium falciparum , Protozoan proteins , Plasmodium falciparum , Antimalarial candidate , High-activity binding peptide , Mahrp-1 , Malaria , Maurer's clefts , Plasmodium falciparum
