Vista Equipo: Conserved high activity binding peptides are involved in adhesion of two detergent-resistant membrane-associated merozoite proteins to red blood cells during invasion

Conserved high activity binding peptides are involved in adhesion of two detergent-resistant membrane-associated merozoite proteins to red blood cells during invasion

Detergent resistant membranes (DRMs) of Plasmodium falciparum merozoites contain a large number of glycosylphosphatidylinositol (GPI)-anchored proteins that have been implicated in interactions between merozoites and red blood cells (RBCs). In this study, two cysteine-rich proteins anchored by GPI t...

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Autores Principales:	Obando-Martinez A.Z., Curtidor H., Arévalo-Pinzón G., Vanegas M., Vizcaino C., Patarroyo M.A., Patarroyo M.E.
Formato:	Artículo (Article)
Lenguaje:	Inglés (English)
Publicado:	2010
Materias:	Binding protein Cell surface receptor Cysteine Detergent Glycosylphosphatidylinositol High activity binding peptide Malaria vaccine Pf113 protein Pf92 protein Protozoal protein Unclassified drug Amino acid sequence Animal experiment Animal model Article Binding affinity Binding assay Binding site Cell adhesion Cell invasion Circular dichroism Controlled study Cross linking Erythrocyte Human Human cell Immunofluorescence Lipid raft Merozoite Nonhuman Plasmodium falciparum Protein binding Protein localization Protein polymorphism Animals Binding sites Chymotrypsin Cross-linking reagents Detergents Erythrocytes Glycosylphosphatidylinositols Host-parasite interactions Immune sera Membrane proteins Merozoites Neuraminidase Peptides Protozoan proteins Rabbits Succinimides Trypsin molecular secondary genetic Models Polymorphism Protein structure
Acceso en línea:	https://repository.urosario.edu.co/handle/10336/22401 https://doi.org/10.1021/jm901474p

id	ir-10336-22401
recordtype	dspace
spelling	ir-10336-224012022-05-02T12:37:18Z Conserved high activity binding peptides are involved in adhesion of two detergent-resistant membrane-associated merozoite proteins to red blood cells during invasion Obando-Martinez A.Z. Curtidor H. Arévalo-Pinzón G. Vanegas M. Vizcaino C. Patarroyo M.A. Patarroyo M.E. Binding protein Cell surface receptor Cysteine Detergent Glycosylphosphatidylinositol High activity binding peptide Malaria vaccine Pf113 protein Pf92 protein Protozoal protein Unclassified drug Amino acid sequence Animal experiment Animal model Article Binding affinity Binding assay Binding site Cell adhesion Cell invasion Circular dichroism Controlled study Cross linking Erythrocyte Human Human cell Immunofluorescence Lipid raft Merozoite Nonhuman Plasmodium falciparum Protein binding Protein localization Protein polymorphism Animals Binding sites Chymotrypsin Circular dichroism Cross-linking reagents Cysteine Detergents Erythrocytes Glycosylphosphatidylinositols Host-parasite interactions Immune sera Membrane proteins Merozoites Neuraminidase Peptides Plasmodium falciparum Protein binding Protozoan proteins Rabbits Succinimides Trypsin molecular secondary genetic Models Polymorphism Protein structure Detergent resistant membranes (DRMs) of Plasmodium falciparum merozoites contain a large number of glycosylphosphatidylinositol (GPI)-anchored proteins that have been implicated in interactions between merozoites and red blood cells (RBCs). In this study, two cysteine-rich proteins anchored by GPI to merozoite DRMs (Pf92 and Pf113) were studied with the aim of identifying regions actively involved in RBC invasion. By means of binding assays, high-activity binding peptides (HABPs) with a large number of binding sites per RBC were identified in Pf92 and Pf113. The nature of the RBC surface receptors for these HABPs was explored using enzyme-treated RBCs and cross-linking assays. Invasion inhibition and immunofluorescence localization studies suggest that Pf92 and Pf113 are involved in RBC invasion and that their adhesion to RBCs is mediated by such HABPs. Additionally, polymorphism and circular dichroism studies support their inclusion in further studies to design components of an antimalarial vaccine. © 2010 American Chemical Society. 2010 2020-05-25T23:56:20Z info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 00222623 15204804 https://repository.urosario.edu.co/handle/10336/22401 https://doi.org/10.1021/jm901474p eng info:eu-repo/semantics/openAccess application/pdf instname:Universidad del Rosario
institution	EdocUR - Universidad del Rosario
collection	DSpace
language	Inglés (English)
topic	Binding protein Cell surface receptor Cysteine Detergent Glycosylphosphatidylinositol High activity binding peptide Malaria vaccine Pf113 protein Pf92 protein Protozoal protein Unclassified drug Amino acid sequence Animal experiment Animal model Article Binding affinity Binding assay Binding site Cell adhesion Cell invasion Circular dichroism Controlled study Cross linking Erythrocyte Human Human cell Immunofluorescence Lipid raft Merozoite Nonhuman Plasmodium falciparum Protein binding Protein localization Protein polymorphism Animals Binding sites Chymotrypsin Circular dichroism Cross-linking reagents Cysteine Detergents Erythrocytes Glycosylphosphatidylinositols Host-parasite interactions Immune sera Membrane proteins Merozoites Neuraminidase Peptides Plasmodium falciparum Protein binding Protozoan proteins Rabbits Succinimides Trypsin molecular secondary genetic Models Polymorphism Protein structure
spellingShingle	Binding protein Cell surface receptor Cysteine Detergent Glycosylphosphatidylinositol High activity binding peptide Malaria vaccine Pf113 protein Pf92 protein Protozoal protein Unclassified drug Amino acid sequence Animal experiment Animal model Article Binding affinity Binding assay Binding site Cell adhesion Cell invasion Circular dichroism Controlled study Cross linking Erythrocyte Human Human cell Immunofluorescence Lipid raft Merozoite Nonhuman Plasmodium falciparum Protein binding Protein localization Protein polymorphism Animals Binding sites Chymotrypsin Circular dichroism Cross-linking reagents Cysteine Detergents Erythrocytes Glycosylphosphatidylinositols Host-parasite interactions Immune sera Membrane proteins Merozoites Neuraminidase Peptides Plasmodium falciparum Protein binding Protozoan proteins Rabbits Succinimides Trypsin molecular secondary genetic Models Polymorphism Protein structure Obando-Martinez A.Z. Curtidor H. Arévalo-Pinzón G. Vanegas M. Vizcaino C. Patarroyo M.A. Patarroyo M.E. Conserved high activity binding peptides are involved in adhesion of two detergent-resistant membrane-associated merozoite proteins to red blood cells during invasion
description	Detergent resistant membranes (DRMs) of Plasmodium falciparum merozoites contain a large number of glycosylphosphatidylinositol (GPI)-anchored proteins that have been implicated in interactions between merozoites and red blood cells (RBCs). In this study, two cysteine-rich proteins anchored by GPI to merozoite DRMs (Pf92 and Pf113) were studied with the aim of identifying regions actively involved in RBC invasion. By means of binding assays, high-activity binding peptides (HABPs) with a large number of binding sites per RBC were identified in Pf92 and Pf113. The nature of the RBC surface receptors for these HABPs was explored using enzyme-treated RBCs and cross-linking assays. Invasion inhibition and immunofluorescence localization studies suggest that Pf92 and Pf113 are involved in RBC invasion and that their adhesion to RBCs is mediated by such HABPs. Additionally, polymorphism and circular dichroism studies support their inclusion in further studies to design components of an antimalarial vaccine. © 2010 American Chemical Society.
format	Artículo (Article)
author	Obando-Martinez A.Z. Curtidor H. Arévalo-Pinzón G. Vanegas M. Vizcaino C. Patarroyo M.A. Patarroyo M.E.
author_facet	Obando-Martinez A.Z. Curtidor H. Arévalo-Pinzón G. Vanegas M. Vizcaino C. Patarroyo M.A. Patarroyo M.E.
author_sort	Obando-Martinez A.Z.
title	Conserved high activity binding peptides are involved in adhesion of two detergent-resistant membrane-associated merozoite proteins to red blood cells during invasion
title_short	Conserved high activity binding peptides are involved in adhesion of two detergent-resistant membrane-associated merozoite proteins to red blood cells during invasion
title_full	Conserved high activity binding peptides are involved in adhesion of two detergent-resistant membrane-associated merozoite proteins to red blood cells during invasion
title_fullStr	Conserved high activity binding peptides are involved in adhesion of two detergent-resistant membrane-associated merozoite proteins to red blood cells during invasion
title_full_unstemmed	Conserved high activity binding peptides are involved in adhesion of two detergent-resistant membrane-associated merozoite proteins to red blood cells during invasion
title_sort	conserved high activity binding peptides are involved in adhesion of two detergent-resistant membrane-associated merozoite proteins to red blood cells during invasion
publishDate	2010
url	https://repository.urosario.edu.co/handle/10336/22401 https://doi.org/10.1021/jm901474p
_version_	1740172278626254848
score	12,131701

Conserved high activity binding peptides are involved in adhesion of two detergent-resistant membrane-associated merozoite proteins to red blood cells during invasion

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