Ítem
Acceso Abierto
Synthetic peptides from conserved regions of the Plasmodium falciparum early transcribed membrane and ring exported proteins bind specifically to red blood cell proteins
Título de la revista
Autores
Garcia, Jeison
Curtidor, Hernando
Obando-Martinez, Ana Z.
Vizcaíno, Carolina
Pinto, Martha
Martinez, Nora L.
Patarroyo, Manuel A.
Patarroyo, Manuel E.
Resumen
Abstract
Severe malaria pathology is directly associated with cytoadherence of infected red blood cells (iRBCs) to healthy RBCs and/or endothelial cells occurring during the intraerythrocytic development of Plasmodium falciparum. We synthesized, as 20-mer long peptides, the members of the ring exported (REX) protein family encoded in chromosome 9, as well as the early transcribed membrane proteins (E-TRAMP) 10.2 and 4, to identify specific RBC binding regions in these proteins. Twelve binding peptides were identified (designated as HABPs): three were identified in REX1, two in REX2, one in REX3, two in REX4 and four in E-TRAMP 10.2. The majority of these HABPs was conserved among different P. falciparum strains, according to sequence analysis. No HABPs were found in E-TRAMP 4. Bindings of HABPs were saturable and sensitive to the enzymatic treatment of RBCs and HABPs had different structural features, according to circular dichroism studies. Our results suggest that the REX and E-TRAMP families participate in relevant interactions with RBC membrane proteins, which highlight these proteins as potential targets for the development of fully effective immunoprophylactic methods. © 2009 Elsevier Ltd. All rights reserved.
Palabras clave
Keywords
Early transcribed membrane protein 10.2 , Membrane protein , Rex protein , Rex1 protein , Rex2 protein , Rex3 protein , Rex4 protein , Unclassified drug , Article , Chromosome 9 , Circular dichroism , Controlled study , Erythrocyte , Human , Immunoprophylaxis , Nonhuman , Peptide synthesis , Plasmodium falciparum , Priority journal , Protein analysis , Protein binding , Sequence analysis , Amino acid sequence , Dna , Erythrocyte membrane , Erythrocytes , Humans , Malaria vaccines , Molecular sequence data , Peptides , Plasmodium falciparum , Polymorphism , Protein binding , Protozoan proteins , Sensitivity and specificity , Antimalarial vaccine , E-tramp , Early transcribed membrane protein , Habps , High activity binding peptides , Plasmodium falciparum , Rex , Ring exported protein
