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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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)
Description
Summary: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.