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...
- 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)
id |
EDOCUR2_bbdd571f484477761444cbcfa73f7906 |
---|---|
oai_identifier_str |
oai:repository.urosario.edu.co:10336/22793 |
network_acronym_str |
EDOCUR2 |
network_name_str |
Repositorio EdocUR - U. Rosario |
repository_id_str |
|
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 |
dc.rights.coar.fl_str_mv |
http://purl.org/coar/access_right/c_abf2 |
dc.rights.acceso.spa.fl_str_mv |
Abierto (Texto Completo) |
rights_invalid_str_mv |
Abierto (Texto Completo) http://purl.org/coar/access_right/c_abf2 |
dc.format.mimetype.none.fl_str_mv |
application/pdf |
dc.publisher.spa.fl_str_mv |
Elsevier Inc. |
institution |
Universidad del Rosario |
dc.source.instname.spa.fl_str_mv |
instname:Universidad del Rosario |
dc.source.reponame.spa.fl_str_mv |
reponame:Repositorio Institucional EdocUR |
bitstream.url.fl_str_mv |
https://repository.urosario.edu.co/bitstreams/d946c214-cb2c-4e15-a95a-5032df6aa510/download https://repository.urosario.edu.co/bitstreams/5088c403-4193-4526-91b1-8fa89242491a/download https://repository.urosario.edu.co/bitstreams/77d6e9a9-3dab-49f2-94af-6cec220844ca/download |
bitstream.checksum.fl_str_mv |
d8197c548ea9a658f9c82994e1760332 13811f18b7fffbb1ee469255bc336d23 ffe24c11966b3b7ace697d263fa4bccb |
bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 MD5 |
repository.name.fl_str_mv |
Repositorio institucional EdocUR |
repository.mail.fl_str_mv |
edocur@urosario.edu.co |
_version_ |
1814167443166199808 |