Characterization of Plasmodium falciparum integral membrane protein Pf25-IMP and identification of its red blood cell binding sequences inhibiting merozoite invasion in vitro
The identification of proteins present on the surface of Plasmodium falciparum-infected red blood cells as well as of free merozoites has been widely considered as one of the main areas of research in the development of an antimalarial vaccine due to their involvement in the parasite's pathogen...
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2008
- Institución:
- Universidad del Rosario
- Repositorio:
- Repositorio EdocUR - U. Rosario
- Idioma:
- eng
- OAI Identifier:
- oai:repository.urosario.edu.co:10336/22894
- Acceso en línea:
- https://doi.org/10.1110/ps.036251.108
https://repository.urosario.edu.co/handle/10336/22894
- Palabra clave:
- Amino acid
Leucylasparaginyllysyllysylthreonylvalylvalylarginyllysyl isoleucylalanylglutamylglycylleucylglycyltyrosylthreonylisoleucylvalyl phenylalanine
Membrane protein
Pf25 membrane protein
Tyrosyllysylthreonylalanylasparaginylglutamylasparaginylvalyllysyl leucylalanylserylserylleucylserylaspartylarginylleucylserylarginine
Unclassified drug
Article
Binding affinity
Controlled study
Erythrocyte
Gene
Genetic transcription
Human
Human cell
Immunofluorescence
Mal8p1.3 gene
Merozoite
Plasmodium falciparum
Priority journal
Protein analysis
Protein binding
Western blotting
Amino acid sequence
Animals
Base sequence
Binding sites
Chymotrypsin
Erythrocytes
Humans
Membrane proteins
Merozoites
Molecular sequence data
Molecular weight
Neuraminidase
Peptide fragments
Plasmodium falciparum
Protein binding
Protozoan proteins
Trypsin
Capra hircus
Plasmodium falciparum
Binding assay
Pf25-imp
Plasmodium falciparum
Red blood cell
Synthetic peptide
secondary
protozoan
genetic
drug
amino acid
cultured
tertiary
Cells
Dose-response relationship
Genes
Protein structure
Protein structure
Sequence homology
Transcription
- Rights
- License
- Abierto (Texto Completo)
Summary: | The identification of proteins present on the surface of Plasmodium falciparum-infected red blood cells as well as of free merozoites has been widely considered as one of the main areas of research in the development of an antimalarial vaccine due to their involvement in the parasite's pathogenesis and invasion mechanisms. Major advances had been accomplished in this area thanks to the analysis of the reported genomic sequence of P. falciparum, allowing for the identification of genes encoding for putative integral membrane proteins. This study reports for the first time the transcription of the MAL8P1.3 gene, which codifies for a 25-kDa integral membrane protein of P. falciparum (FCB-2 strain), namely, Pf25-IMP. Western blot and immunofluorescence assays using goat polyclonal sera indicate that this protein is expressed in erythrocytic asexual blood stages. A highly robust, sensible, and specific receptor-ligand interaction assay allowed identification of two high activity binding peptides (HABPs) derived from Pf25-IMP: 30577 (41YKTANENVKLASSLSDRLSR 60) and 30583 (161LNKKTVVRKIAEGLGYTIVF180). Both HABPs bound with high affinity to human red blood cells (RBCs), and such binding was susceptible to enzyme treatment with trypsin. A common RBC surface receptor of apparently 48 kDa was found for both HABPs, plus an additional 31-kDa receptor for HABP 30577. HABP 30577 inhibited merozoite invasion in vitro by 73%, while HABP 30583 showed a 59% inhibition at 200 ?M concentration. The data suggest a possible role of Pf25-IMP in merozoite invasion to RBCs and support its inclusion in further immunological studies for evaluating its potential as vaccine candidates. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society. |
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