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...
- Autores:
- 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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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 |
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http://purl.org/coar/access_right/c_abf2 |
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Abierto (Texto Completo) |
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Abierto (Texto Completo) http://purl.org/coar/access_right/c_abf2 |
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