A Maurer's cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membrane

The membrane-associated histidine-rich protein-1 (MAHRP-1) is a Maurer's cleft-resident molecule that has been recently described as an important protein for the trafficking of PfEMP-1 to infected erythrocyte membrane, a major virulence factor. We have studied the specific interactions between...

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Tipo de recurso:
Fecha de publicación:
2009
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/23505
Acceso en línea:
https://doi.org/10.1016/j.bbrc.2009.01.050
https://repository.urosario.edu.co/handle/10336/23505
Palabra clave:
Carrier proteins and binding proteins
Chymotrypsin
Erythrocyte membrane protein 1
Protein habp
Protein mahrp 1
Protozoal protein
Unclassified drug
Amino acid sequence
Article
Controlled study
Erythrocyte membrane
Nonhuman
Plasmodium falciparum
Priority journal
Protein analysis
Protein binding
Protein interaction
Protein localization
Protein structure
Amino acid sequence
Animals
Carrier proteins
Erythrocyte membrane
Molecular sequence data
Peptides
Plasmodium falciparum
Protozoan proteins
Plasmodium falciparum
Antimalarial candidate
High-activity binding peptide
Mahrp-1
Malaria
Maurer's clefts
Plasmodium falciparum
Rights
License
Abierto (Texto Completo)
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spelling 8524e52b-4a7c-4435-9244-66a621a020c8-191225589-1758196fd-aae9-4104-a9c4-754f1fae7dee-151721018-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-12020-05-26T00:02:36Z2020-05-26T00:02:36Z2009The membrane-associated histidine-rich protein-1 (MAHRP-1) is a Maurer's cleft-resident molecule that has been recently described as an important protein for the trafficking of PfEMP-1 to infected erythrocyte membrane, a major virulence factor. We have studied the specific interactions between 20-mer-long synthetic peptides spanning the complete MAHRP-1 sequence and erythrocytes. A high-activity binding peptide (HABP) with saturable binding to a 46-kDa erythrocyte membrane protein was identified and its binding was affected by chymotrypsin treatment. Random coil and ?-helical features were found in the HABP's structure. Our results suggest that MAHRP-1 specifically interacts with erythrocyte membrane through a 20-mer-long amino acid region, raising questions about this region's potential as a therapeutic target against malaria. © 2009 Elsevier Inc. All rights reserved.application/pdfhttps://doi.org/10.1016/j.bbrc.2009.01.0500006291X10902104https://repository.urosario.edu.co/handle/10336/23505eng126No. 1122Biochemical and Biophysical Research CommunicationsVol. 380Biochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.380, No.1 (2009); pp. 122-126https://www.scopus.com/inward/record.uri?eid=2-s2.0-59849116166&doi=10.1016%2fj.bbrc.2009.01.050&partnerID=40&md5=e70102eeb4d87406c39ac31ca50e3e0dAbierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURCarrier proteins and binding proteinsChymotrypsinErythrocyte membrane protein 1Protein habpProtein mahrp 1Protozoal proteinUnclassified drugAmino acid sequenceArticleControlled studyErythrocyte membraneNonhumanPlasmodium falciparumPriority journalProtein analysisProtein bindingProtein interactionProtein localizationProtein structureAmino acid sequenceAnimalsCarrier proteinsErythrocyte membraneMolecular sequence dataPeptidesPlasmodium falciparumProtozoan proteinsPlasmodium falciparumAntimalarial candidateHigh-activity binding peptideMahrp-1MalariaMaurer's cleftsPlasmodium falciparumA Maurer's cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membranearticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501García, JeisonCurtidor, HernandoGil, Olga L.Vanegas, MagnoliaPatarroyo, Manuel E.ORIGINALA_Maurer_s_cleft_associated_Plasmodium_f.pdfapplication/pdf386659https://repository.urosario.edu.co/bitstreams/502f9e6e-f9f7-4d0a-81d2-d3d95e4f72c0/download8483f7c404cda11511b78c5ccd067396MD51TEXTA_Maurer_s_cleft_associated_Plasmodium_f.pdf.txtA_Maurer_s_cleft_associated_Plasmodium_f.pdf.txtExtracted texttext/plain30929https://repository.urosario.edu.co/bitstreams/da5831d8-4f5a-4aea-bd3e-2b73f3d64680/download1d285bc1c912860deaf43711543faa99MD52THUMBNAILA_Maurer_s_cleft_associated_Plasmodium_f.pdf.jpgA_Maurer_s_cleft_associated_Plasmodium_f.pdf.jpgGenerated Thumbnailimage/jpeg5211https://repository.urosario.edu.co/bitstreams/99db8d8c-724a-4a5b-b6e0-c6998043b6e7/download6e781a6fe48795af68eec343f1c63091MD5310336/23505oai:repository.urosario.edu.co:10336/235052022-05-02 07:37:21.026784https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv A Maurer's cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membrane
title A Maurer's cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membrane
spellingShingle A Maurer's cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membrane
Carrier proteins and binding proteins
Chymotrypsin
Erythrocyte membrane protein 1
Protein habp
Protein mahrp 1
Protozoal protein
Unclassified drug
Amino acid sequence
Article
Controlled study
Erythrocyte membrane
Nonhuman
Plasmodium falciparum
Priority journal
Protein analysis
Protein binding
Protein interaction
Protein localization
Protein structure
Amino acid sequence
Animals
Carrier proteins
Erythrocyte membrane
Molecular sequence data
Peptides
Plasmodium falciparum
Protozoan proteins
Plasmodium falciparum
Antimalarial candidate
High-activity binding peptide
Mahrp-1
Malaria
Maurer's clefts
Plasmodium falciparum
title_short A Maurer's cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membrane
title_full A Maurer's cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membrane
title_fullStr A Maurer's cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membrane
title_full_unstemmed A Maurer's cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membrane
title_sort A Maurer's cleft-associated Plasmodium falciparum membrane-associated histidine-rich protein peptide specifically interacts with the erythrocyte membrane
dc.subject.keyword.spa.fl_str_mv Carrier proteins and binding proteins
Chymotrypsin
Erythrocyte membrane protein 1
Protein habp
Protein mahrp 1
Protozoal protein
Unclassified drug
Amino acid sequence
Article
Controlled study
Erythrocyte membrane
Nonhuman
Plasmodium falciparum
Priority journal
Protein analysis
Protein binding
Protein interaction
Protein localization
Protein structure
Amino acid sequence
Animals
Carrier proteins
Erythrocyte membrane
Molecular sequence data
Peptides
Plasmodium falciparum
Protozoan proteins
Plasmodium falciparum
Antimalarial candidate
High-activity binding peptide
Mahrp-1
Malaria
Maurer's clefts
Plasmodium falciparum
topic Carrier proteins and binding proteins
Chymotrypsin
Erythrocyte membrane protein 1
Protein habp
Protein mahrp 1
Protozoal protein
Unclassified drug
Amino acid sequence
Article
Controlled study
Erythrocyte membrane
Nonhuman
Plasmodium falciparum
Priority journal
Protein analysis
Protein binding
Protein interaction
Protein localization
Protein structure
Amino acid sequence
Animals
Carrier proteins
Erythrocyte membrane
Molecular sequence data
Peptides
Plasmodium falciparum
Protozoan proteins
Plasmodium falciparum
Antimalarial candidate
High-activity binding peptide
Mahrp-1
Malaria
Maurer's clefts
Plasmodium falciparum
description The membrane-associated histidine-rich protein-1 (MAHRP-1) is a Maurer's cleft-resident molecule that has been recently described as an important protein for the trafficking of PfEMP-1 to infected erythrocyte membrane, a major virulence factor. We have studied the specific interactions between 20-mer-long synthetic peptides spanning the complete MAHRP-1 sequence and erythrocytes. A high-activity binding peptide (HABP) with saturable binding to a 46-kDa erythrocyte membrane protein was identified and its binding was affected by chymotrypsin treatment. Random coil and ?-helical features were found in the HABP's structure. Our results suggest that MAHRP-1 specifically interacts with erythrocyte membrane through a 20-mer-long amino acid region, raising questions about this region's potential as a therapeutic target against malaria. © 2009 Elsevier Inc. All rights reserved.
publishDate 2009
dc.date.created.spa.fl_str_mv 2009
dc.date.accessioned.none.fl_str_mv 2020-05-26T00:02:36Z
dc.date.available.none.fl_str_mv 2020-05-26T00:02:36Z
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.bbrc.2009.01.050
dc.identifier.issn.none.fl_str_mv 0006291X
10902104
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/23505
url https://doi.org/10.1016/j.bbrc.2009.01.050
https://repository.urosario.edu.co/handle/10336/23505
identifier_str_mv 0006291X
10902104
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 126
dc.relation.citationIssue.none.fl_str_mv No. 1
dc.relation.citationStartPage.none.fl_str_mv 122
dc.relation.citationTitle.none.fl_str_mv Biochemical and Biophysical Research Communications
dc.relation.citationVolume.none.fl_str_mv Vol. 380
dc.relation.ispartof.spa.fl_str_mv Biochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.380, No.1 (2009); pp. 122-126
dc.relation.uri.spa.fl_str_mv https://www.scopus.com/inward/record.uri?eid=2-s2.0-59849116166&doi=10.1016%2fj.bbrc.2009.01.050&partnerID=40&md5=e70102eeb4d87406c39ac31ca50e3e0d
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)
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