Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells

The Plasmodium falciparum P0 ribosomal phosphoprotein (PfP0) was identified for the first time by screening a cDNA expression library of P. falciparum parasites with sera from malaria-immune individuals. Due to its localization on the surface of different parasite life-cycle stages (merozoites and g...

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Tipo de recurso:
Fecha de publicación:
2010
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/22404
Acceso en línea:
https://doi.org/10.1007/s00109-009-0533-5
https://repository.urosario.edu.co/handle/10336/22404
Palabra clave:
Phosphoprotein
Amino acid sequence
Article
Erythrocyte
Merozoite
Nonhuman
Plasmodium falciparum
Protein binding
Protein determination
Protein synthesis
Ribosome
Amino acid sequence
Erythrocytes
Humans
Molecular sequence data
Plasmodium falciparum
Protein binding
Protozoan proteins
Ribosomal proteins
High activity binding peptide (habp)
Malaria
Peptides
Plasmodium falciparum
Red blood cells (rbcs)
Ribosomal phosphoprotein p0
Vaccine
Rights
License
Abierto (Texto Completo)
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dc.title.spa.fl_str_mv Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells
title Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells
spellingShingle Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells
Phosphoprotein
Amino acid sequence
Article
Erythrocyte
Merozoite
Nonhuman
Plasmodium falciparum
Protein binding
Protein determination
Protein synthesis
Ribosome
Amino acid sequence
Erythrocytes
Humans
Molecular sequence data
Plasmodium falciparum
Protein binding
Protozoan proteins
Ribosomal proteins
High activity binding peptide (habp)
Malaria
Peptides
Plasmodium falciparum
Red blood cells (rbcs)
Ribosomal phosphoprotein p0
Vaccine
title_short Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells
title_full Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells
title_fullStr Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells
title_full_unstemmed Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells
title_sort Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells
dc.subject.keyword.spa.fl_str_mv Phosphoprotein
Amino acid sequence
Article
Erythrocyte
Merozoite
Nonhuman
Plasmodium falciparum
Protein binding
Protein determination
Protein synthesis
Ribosome
Amino acid sequence
Erythrocytes
Humans
Molecular sequence data
Plasmodium falciparum
Protein binding
Protozoan proteins
Ribosomal proteins
High activity binding peptide (habp)
Malaria
Peptides
Plasmodium falciparum
Red blood cells (rbcs)
Ribosomal phosphoprotein p0
Vaccine
topic Phosphoprotein
Amino acid sequence
Article
Erythrocyte
Merozoite
Nonhuman
Plasmodium falciparum
Protein binding
Protein determination
Protein synthesis
Ribosome
Amino acid sequence
Erythrocytes
Humans
Molecular sequence data
Plasmodium falciparum
Protein binding
Protozoan proteins
Ribosomal proteins
High activity binding peptide (habp)
Malaria
Peptides
Plasmodium falciparum
Red blood cells (rbcs)
Ribosomal phosphoprotein p0
Vaccine
description The Plasmodium falciparum P0 ribosomal phosphoprotein (PfP0) was identified for the first time by screening a cDNA expression library of P. falciparum parasites with sera from malaria-immune individuals. Due to its localization on the surface of different parasite life-cycle stages (merozoites and gametocytes) and its recognition by invasion-blocking antibodies, PfP0 has been considered a potential malaria-vaccine component. In this study, 16 20-mer-long synthetic peptides spanning the entire PfP0 sequence were evaluated by means of receptor-ligand assays with human red blood cells (RBCs) in order to determine the role played by these peptides in the invasion process. Four RBC high-activity binding peptides (HABPs), located mostly toward the N-terminal region, were identified: HABP 33898 (1MAKLSKQQKKQMYIEKLSSL 20), HABP 33900 (41ASVRKSLRGKATILMGKNTRY60), HABP 33901 (61IRTALKKNLQAVPQIEKLLPY 80), and HABP 33906 (161LIKQGEKVTASSATLLRKFNY180). The binding pattern of HABPs 33898 and 33906 to enzyme-treated RBCs suggests receptors of protein nature for these two HABPs, one of which could correspond to a common 58-kDa RBC membrane protein, as indicated by results of cross-linking assays. Both HABPs exhibited high content of ?-helical features and prevented P. falciparum merozoite invasion to RBCs in vitro by up to 91%. The invasion-blocking ability reported here for these PfP0 HABPs supports their inclusion in immunological studies with the aim of assessing their potential as candidates for a vaccine against P. falciparum malaria. © 2009 Springer-Verlag.
publishDate 2010
dc.date.created.spa.fl_str_mv 2010
dc.date.accessioned.none.fl_str_mv 2020-05-25T23:56:21Z
dc.date.available.none.fl_str_mv 2020-05-25T23:56:21Z
dc.type.eng.fl_str_mv article
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dc.type.spa.spa.fl_str_mv Artículo
dc.identifier.doi.none.fl_str_mv https://doi.org/10.1007/s00109-009-0533-5
dc.identifier.issn.none.fl_str_mv 09462716
14321440
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https://repository.urosario.edu.co/handle/10336/22404
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dc.relation.citationIssue.none.fl_str_mv No. 1
dc.relation.citationStartPage.none.fl_str_mv 61
dc.relation.citationTitle.none.fl_str_mv Journal of Molecular Medicine
dc.relation.citationVolume.none.fl_str_mv Vol. 88
dc.relation.ispartof.spa.fl_str_mv Journal of Molecular Medicine, ISSN:09462716, 14321440, Vol.88, No.1 (2010); pp. 61-74
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spelling 1a837cee-dfa1-42d9-9f6c-31cbb52d5383-191225589-16fc431a4-2889-4e78-ba01-10c2807c6557-143d18b71-7077-40fa-a03c-e1b25ea690c3-19de1cfc2-5d95-4925-a819-b9b2b20ff2d2-179653065-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-12020-05-25T23:56:21Z2020-05-25T23:56:21Z2010The Plasmodium falciparum P0 ribosomal phosphoprotein (PfP0) was identified for the first time by screening a cDNA expression library of P. falciparum parasites with sera from malaria-immune individuals. Due to its localization on the surface of different parasite life-cycle stages (merozoites and gametocytes) and its recognition by invasion-blocking antibodies, PfP0 has been considered a potential malaria-vaccine component. In this study, 16 20-mer-long synthetic peptides spanning the entire PfP0 sequence were evaluated by means of receptor-ligand assays with human red blood cells (RBCs) in order to determine the role played by these peptides in the invasion process. Four RBC high-activity binding peptides (HABPs), located mostly toward the N-terminal region, were identified: HABP 33898 (1MAKLSKQQKKQMYIEKLSSL 20), HABP 33900 (41ASVRKSLRGKATILMGKNTRY60), HABP 33901 (61IRTALKKNLQAVPQIEKLLPY 80), and HABP 33906 (161LIKQGEKVTASSATLLRKFNY180). The binding pattern of HABPs 33898 and 33906 to enzyme-treated RBCs suggests receptors of protein nature for these two HABPs, one of which could correspond to a common 58-kDa RBC membrane protein, as indicated by results of cross-linking assays. Both HABPs exhibited high content of ?-helical features and prevented P. falciparum merozoite invasion to RBCs in vitro by up to 91%. The invasion-blocking ability reported here for these PfP0 HABPs supports their inclusion in immunological studies with the aim of assessing their potential as candidates for a vaccine against P. falciparum malaria. © 2009 Springer-Verlag.application/pdfhttps://doi.org/10.1007/s00109-009-0533-50946271614321440https://repository.urosario.edu.co/handle/10336/22404eng74No. 161Journal of Molecular MedicineVol. 88Journal of Molecular Medicine, ISSN:09462716, 14321440, Vol.88, No.1 (2010); pp. 61-74https://www.scopus.com/inward/record.uri?eid=2-s2.0-75749089592&doi=10.1007%2fs00109-009-0533-5&partnerID=40&md5=e9a1096adf0d5564ac641165d006348eAbierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURPhosphoproteinAmino acid sequenceArticleErythrocyteMerozoiteNonhumanPlasmodium falciparumProtein bindingProtein determinationProtein synthesisRibosomeAmino acid sequenceErythrocytesHumansMolecular sequence dataPlasmodium falciparumProtein bindingProtozoan proteinsRibosomal proteinsHigh activity binding peptide (habp)MalariaPeptidesPlasmodium falciparumRed blood cells (rbcs)Ribosomal phosphoprotein p0VaccineFine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cellsarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Arevalo-Pinzon, GabrielaCurtidor, HernandoReyes, ClaudiaPinto, MarthaVizcaíno, CarolinaPatarroyo, Manuel A.Patarroyo, Manuel E.ORIGINALArevalo-Pinzon2010_Article_FineMappingOfPlasmodiumFalcipa.pdfapplication/pdf403019https://repository.urosario.edu.co/bitstreams/d9a0e99f-e205-4f6f-8181-e4efef15d477/downloadf9afdebd54198156f29af173db796d3cMD51TEXTArevalo-Pinzon2010_Article_FineMappingOfPlasmodiumFalcipa.pdf.txtArevalo-Pinzon2010_Article_FineMappingOfPlasmodiumFalcipa.pdf.txtExtracted texttext/plain64109https://repository.urosario.edu.co/bitstreams/c8218020-c880-4075-b828-cea8bfca2d1f/download8ee12260be5308c586e01f50eeda85bdMD52THUMBNAILArevalo-Pinzon2010_Article_FineMappingOfPlasmodiumFalcipa.pdf.jpgArevalo-Pinzon2010_Article_FineMappingOfPlasmodiumFalcipa.pdf.jpgGenerated Thumbnailimage/jpeg4481https://repository.urosario.edu.co/bitstreams/9736d371-6a00-47f0-9544-45f513f637a6/download8de79f487a80eff6c6391a2613bf73d0MD5310336/22404oai:repository.urosario.edu.co:10336/224042022-05-02 07:37:14.144227https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co