Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion

Plasmodium falciparum malaria parasite invasion of erythrocytes is an essential step in host infection and the proteins involved in such invasion are the main target in developing an antimalarial vaccine. Secretory organelle-derived proteins (micronemal AMA1 protein and the RON2, 4, and 5 rhoptry ne...

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Autores:
Tipo de recurso:
Fecha de publicación:
2014
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/22793
Acceso en línea:
https://doi.org/10.1016/j.peptides.2013.07.028
https://repository.urosario.edu.co/handle/10336/22793
Palabra clave:
Chymotrypsin
Peptide derivative
Plasmodium falciparum rhoptry neck protein 5 peptide derivative
Protein
Ron5 protein
Trypsin
Unclassified drug
Malaria vaccine
Protozoal protein
Article
Assay
Cell interaction
Cell invasion
Controlled study
Erythrocyte
Human
Human cell
Merozoite
Plasmodium falciparum
Priority journal
Protein binding
Receptor ligand interaction assay
Cell culture
Circular dichroism
Erythrocyte
Immunoelectron microscopy
Immunology
Metabolism
Parasitology
Pathogenicity
Plasmodium falciparum
Circular dichroism
Erythrocytes
Humans
Malaria vaccines
Merozoites
Plasmodium falciparum
Protozoan proteins
Binding
Malaria
Merozoite
Rhoptry neck
Synthetic peptide
immunoelectron
cultured
Cells
Microscopy
Rights
License
Abierto (Texto Completo)
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spelling 9122558960077273e86-df40-4d8e-90a6-4e1c78ea40d6-1eca483d3-a229-42c8-8a6d-3b5e6f002e5b-151721018-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-179653065-12020-05-25T23:58:03Z2020-05-25T23:58:03Z2014Plasmodium falciparum malaria parasite invasion of erythrocytes is an essential step in host infection and the proteins involved in such invasion are the main target in developing an antimalarial vaccine. Secretory organelle-derived proteins (micronemal AMA1 protein and the RON2, 4, and 5 rhoptry neck proteins) have been recently described as components of moving junction complex formation allowing merozoites to move into a newly created parasitophorous vacuole. This study led to identifying RON5 regions involved in binding to human erythrocytes by using a highly robust, sensitive and specific receptor-ligand interaction assay; it is further shown that the RON5 protein remains highly conserved throughout different parasite strains. It is shown that the binding peptide-erythrocyte interaction is saturable and sensitive to chymotrypsin and trypsin. Invasion inhibition assays using erythrocyte binding peptides showed that the RON5-erythrocyte interaction could be critical for merozoite invasion of erythrocytes. This work provides evidence (for the first time) suggesting a fundamental role for RON5 in erythrocyte invasion. © 2013 Elsevier Inc.application/pdfhttps://doi.org/10.1016/j.peptides.2013.07.0281969781https://repository.urosario.edu.co/handle/10336/22793engElsevier Inc.217210PeptidesVol. 53Peptides, ISSN:1969781, Vol.53,(2014); pp. 210-217https://www.scopus.com/inward/record.uri?eid=2-s2.0-84899437196&doi=10.1016%2fj.peptides.2013.07.028&partnerID=40&md5=9cea022e232e0b56ee56f32803f670cdAbierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURChymotrypsinPeptide derivativePlasmodium falciparum rhoptry neck protein 5 peptide derivativeProteinRon5 proteinTrypsinUnclassified drugMalaria vaccineProtozoal proteinArticleAssayCell interactionCell invasionControlled studyErythrocyteHumanHuman cellMerozoitePlasmodium falciparumPriority journalProtein bindingReceptor ligand interaction assayCell cultureCircular dichroismErythrocyteImmunoelectron microscopyImmunologyMetabolismParasitologyPathogenicityPlasmodium falciparumCircular dichroismErythrocytesHumansMalaria vaccinesMerozoitesPlasmodium falciparumProtozoan proteinsBindingMalariaMerozoiteRhoptry neckSynthetic peptideimmunoelectronculturedCellsMicroscopyPlasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasionarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Curtidor, HernandoPatiño, Liliana C.Arévalo-Pinzón, GabrielaVanegas, MagnoliaPatarroyo, Manuel E.Patarroyo, Manuel A.ORIGINAL1-s2-0-S0196978113002684-main.pdfapplication/pdf1339314https://repository.urosario.edu.co/bitstreams/d946c214-cb2c-4e15-a95a-5032df6aa510/downloadd8197c548ea9a658f9c82994e1760332MD51TEXT1-s2-0-S0196978113002684-main.pdf.txt1-s2-0-S0196978113002684-main.pdf.txtExtracted texttext/plain45066https://repository.urosario.edu.co/bitstreams/5088c403-4193-4526-91b1-8fa89242491a/download13811f18b7fffbb1ee469255bc336d23MD52THUMBNAIL1-s2-0-S0196978113002684-main.pdf.jpg1-s2-0-S0196978113002684-main.pdf.jpgGenerated Thumbnailimage/jpeg4631https://repository.urosario.edu.co/bitstreams/77d6e9a9-3dab-49f2-94af-6cec220844ca/downloadffe24c11966b3b7ace697d263fa4bccbMD5310336/22793oai:repository.urosario.edu.co:10336/227932022-05-02 07:37:20.649565https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion
title Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion
spellingShingle Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion
Chymotrypsin
Peptide derivative
Plasmodium falciparum rhoptry neck protein 5 peptide derivative
Protein
Ron5 protein
Trypsin
Unclassified drug
Malaria vaccine
Protozoal protein
Article
Assay
Cell interaction
Cell invasion
Controlled study
Erythrocyte
Human
Human cell
Merozoite
Plasmodium falciparum
Priority journal
Protein binding
Receptor ligand interaction assay
Cell culture
Circular dichroism
Erythrocyte
Immunoelectron microscopy
Immunology
Metabolism
Parasitology
Pathogenicity
Plasmodium falciparum
Circular dichroism
Erythrocytes
Humans
Malaria vaccines
Merozoites
Plasmodium falciparum
Protozoan proteins
Binding
Malaria
Merozoite
Rhoptry neck
Synthetic peptide
immunoelectron
cultured
Cells
Microscopy
title_short Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion
title_full Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion
title_fullStr Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion
title_full_unstemmed Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion
title_sort Plasmodium falciparum rhoptry neck protein 5 peptides bind to human red blood cells and inhibit parasite invasion
dc.subject.keyword.spa.fl_str_mv Chymotrypsin
Peptide derivative
Plasmodium falciparum rhoptry neck protein 5 peptide derivative
Protein
Ron5 protein
Trypsin
Unclassified drug
Malaria vaccine
Protozoal protein
Article
Assay
Cell interaction
Cell invasion
Controlled study
Erythrocyte
Human
Human cell
Merozoite
Plasmodium falciparum
Priority journal
Protein binding
Receptor ligand interaction assay
Cell culture
Circular dichroism
Erythrocyte
Immunoelectron microscopy
Immunology
Metabolism
Parasitology
Pathogenicity
Plasmodium falciparum
Circular dichroism
Erythrocytes
Humans
Malaria vaccines
Merozoites
Plasmodium falciparum
Protozoan proteins
Binding
Malaria
Merozoite
Rhoptry neck
Synthetic peptide
topic Chymotrypsin
Peptide derivative
Plasmodium falciparum rhoptry neck protein 5 peptide derivative
Protein
Ron5 protein
Trypsin
Unclassified drug
Malaria vaccine
Protozoal protein
Article
Assay
Cell interaction
Cell invasion
Controlled study
Erythrocyte
Human
Human cell
Merozoite
Plasmodium falciparum
Priority journal
Protein binding
Receptor ligand interaction assay
Cell culture
Circular dichroism
Erythrocyte
Immunoelectron microscopy
Immunology
Metabolism
Parasitology
Pathogenicity
Plasmodium falciparum
Circular dichroism
Erythrocytes
Humans
Malaria vaccines
Merozoites
Plasmodium falciparum
Protozoan proteins
Binding
Malaria
Merozoite
Rhoptry neck
Synthetic peptide
immunoelectron
cultured
Cells
Microscopy
dc.subject.keyword.eng.fl_str_mv immunoelectron
cultured
Cells
Microscopy
description Plasmodium falciparum malaria parasite invasion of erythrocytes is an essential step in host infection and the proteins involved in such invasion are the main target in developing an antimalarial vaccine. Secretory organelle-derived proteins (micronemal AMA1 protein and the RON2, 4, and 5 rhoptry neck proteins) have been recently described as components of moving junction complex formation allowing merozoites to move into a newly created parasitophorous vacuole. This study led to identifying RON5 regions involved in binding to human erythrocytes by using a highly robust, sensitive and specific receptor-ligand interaction assay; it is further shown that the RON5 protein remains highly conserved throughout different parasite strains. It is shown that the binding peptide-erythrocyte interaction is saturable and sensitive to chymotrypsin and trypsin. Invasion inhibition assays using erythrocyte binding peptides showed that the RON5-erythrocyte interaction could be critical for merozoite invasion of erythrocytes. This work provides evidence (for the first time) suggesting a fundamental role for RON5 in erythrocyte invasion. © 2013 Elsevier Inc.
publishDate 2014
dc.date.created.spa.fl_str_mv 2014
dc.date.accessioned.none.fl_str_mv 2020-05-25T23:58:03Z
dc.date.available.none.fl_str_mv 2020-05-25T23:58:03Z
dc.type.eng.fl_str_mv article
dc.type.coarversion.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.coar.fl_str_mv http://purl.org/coar/resource_type/c_6501
dc.type.spa.spa.fl_str_mv Artículo
dc.identifier.doi.none.fl_str_mv https://doi.org/10.1016/j.peptides.2013.07.028
dc.identifier.issn.none.fl_str_mv 1969781
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/22793
url https://doi.org/10.1016/j.peptides.2013.07.028
https://repository.urosario.edu.co/handle/10336/22793
identifier_str_mv 1969781
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 217
dc.relation.citationStartPage.none.fl_str_mv 210
dc.relation.citationTitle.none.fl_str_mv Peptides
dc.relation.citationVolume.none.fl_str_mv Vol. 53
dc.relation.ispartof.spa.fl_str_mv Peptides, ISSN:1969781, Vol.53,(2014); pp. 210-217
dc.relation.uri.spa.fl_str_mv https://www.scopus.com/inward/record.uri?eid=2-s2.0-84899437196&doi=10.1016%2fj.peptides.2013.07.028&partnerID=40&md5=9cea022e232e0b56ee56f32803f670cd
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rights_invalid_str_mv Abierto (Texto Completo)
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dc.format.mimetype.none.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Elsevier Inc.
institution Universidad del Rosario
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