Rh1 high activity binding peptides inhibit high percentages of Plasmodium falciparum FVO strain invasion

Identifying the minimal functional regions of the proteins which the malaria parasite uses when invading its host cells constitutes the first and most important approach in an effective design for a chemically synthesised, multi-antigen, multi-stage, subunit-based vaccine. This work has been aimed a...

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Autores:
Tipo de recurso:
Fecha de publicación:
2013
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/23460
Acceso en línea:
https://doi.org/10.1016/j.vaccine.2013.01.052
https://repository.urosario.edu.co/handle/10336/23460
Palabra clave:
Amino acid
Membrane receptor
Protein
Rh1 protein
Unclassified drug
Alpha helix
Article
Cell invasion
Controlled study
Erythrocyte
Gene expression
In vitro study
Nonhuman
Plasmodium falciparum
Priority journal
Protein binding
Protein polymorphism
Reticulocyte
Schizont
Amino acid sequence
Erythrocytes
Host-pathogen interactions
Humans
Malaria
Malaria vaccines
Molecular sequence data
Peptides
Plasmodium falciparum
Protein structure, secondary
Protein structure, tertiary
Protozoan proteins
Schizonts
Malaria
Plasmodium falciparum
Reticulocyte binding-like
Synthetic peptide
subunit
Vaccines
Rights
License
Abierto (Texto Completo)
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network_name_str Repositorio EdocUR - U. Rosario
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dc.title.spa.fl_str_mv Rh1 high activity binding peptides inhibit high percentages of Plasmodium falciparum FVO strain invasion
title Rh1 high activity binding peptides inhibit high percentages of Plasmodium falciparum FVO strain invasion
spellingShingle Rh1 high activity binding peptides inhibit high percentages of Plasmodium falciparum FVO strain invasion
Amino acid
Membrane receptor
Protein
Rh1 protein
Unclassified drug
Alpha helix
Article
Cell invasion
Controlled study
Erythrocyte
Gene expression
In vitro study
Nonhuman
Plasmodium falciparum
Priority journal
Protein binding
Protein polymorphism
Reticulocyte
Schizont
Amino acid sequence
Erythrocytes
Host-pathogen interactions
Humans
Malaria
Malaria vaccines
Molecular sequence data
Peptides
Plasmodium falciparum
Protein structure, secondary
Protein structure, tertiary
Protozoan proteins
Schizonts
Malaria
Plasmodium falciparum
Reticulocyte binding-like
Synthetic peptide
subunit
Vaccines
title_short Rh1 high activity binding peptides inhibit high percentages of Plasmodium falciparum FVO strain invasion
title_full Rh1 high activity binding peptides inhibit high percentages of Plasmodium falciparum FVO strain invasion
title_fullStr Rh1 high activity binding peptides inhibit high percentages of Plasmodium falciparum FVO strain invasion
title_full_unstemmed Rh1 high activity binding peptides inhibit high percentages of Plasmodium falciparum FVO strain invasion
title_sort Rh1 high activity binding peptides inhibit high percentages of Plasmodium falciparum FVO strain invasion
dc.subject.keyword.spa.fl_str_mv Amino acid
Membrane receptor
Protein
Rh1 protein
Unclassified drug
Alpha helix
Article
Cell invasion
Controlled study
Erythrocyte
Gene expression
In vitro study
Nonhuman
Plasmodium falciparum
Priority journal
Protein binding
Protein polymorphism
Reticulocyte
Schizont
Amino acid sequence
Erythrocytes
Host-pathogen interactions
Humans
Malaria
Malaria vaccines
Molecular sequence data
Peptides
Plasmodium falciparum
Protein structure, secondary
Protein structure, tertiary
Protozoan proteins
Schizonts
Malaria
Plasmodium falciparum
Reticulocyte binding-like
Synthetic peptide
topic Amino acid
Membrane receptor
Protein
Rh1 protein
Unclassified drug
Alpha helix
Article
Cell invasion
Controlled study
Erythrocyte
Gene expression
In vitro study
Nonhuman
Plasmodium falciparum
Priority journal
Protein binding
Protein polymorphism
Reticulocyte
Schizont
Amino acid sequence
Erythrocytes
Host-pathogen interactions
Humans
Malaria
Malaria vaccines
Molecular sequence data
Peptides
Plasmodium falciparum
Protein structure, secondary
Protein structure, tertiary
Protozoan proteins
Schizonts
Malaria
Plasmodium falciparum
Reticulocyte binding-like
Synthetic peptide
subunit
Vaccines
dc.subject.keyword.eng.fl_str_mv subunit
Vaccines
description Identifying the minimal functional regions of the proteins which the malaria parasite uses when invading its host cells constitutes the first and most important approach in an effective design for a chemically synthesised, multi-antigen, multi-stage, subunit-based vaccine. This work has been aimed at identifying the PfRh1 protein binding regions (residues 1-2580) belonging to the reticulocyte binding-like (RBL or P. falciparum Rh [PfRh]) family implicated in the parasite's alternative target cell invasion routes. Eighteen peptide regions (called high activity binding peptides - HABPs) binding to red blood cells (RBC) were identified in peptides mapped in a highly robust, specific and sensitive receptor-ligand assay. These HABPs were saturable in the experimental conditions assayed here and most had an alpha helix structure. Polymorphism studies revealed that only six of the eighteen HABPs identified had changes at amino acid level amongst the seven P. falciparum strains evaluated. Most HABPs' specific binding became altered when RBC were treated with neuraminidase, chymotrypsin and trypsin, suggesting differing sensitivity for RBC membrane receptors. After ascertaining that the Rh1 gene was transcribed and expressed in late-stage schizonts of the FCB-2 strain, invasion inhibition assays were carried out. When most of these HABPs were assayed in P. falciparum in vitro culture they were able to inhibit high percentages of FVO strain invasion compared to low inhibition percentages observed with the FCB-2 strain. This data shows small Rh1 regions' participation during invasion and suggests that these units should be included in further immunological and structural studies. © 2013 Elsevier Ltd.
publishDate 2013
dc.date.created.spa.fl_str_mv 2013
dc.date.accessioned.none.fl_str_mv 2020-05-26T00:02:13Z
dc.date.available.none.fl_str_mv 2020-05-26T00:02:13Z
dc.type.eng.fl_str_mv article
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dc.identifier.doi.none.fl_str_mv https://doi.org/10.1016/j.vaccine.2013.01.052
dc.identifier.issn.none.fl_str_mv 0264410X
13588745
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url https://doi.org/10.1016/j.vaccine.2013.01.052
https://repository.urosario.edu.co/handle/10336/23460
identifier_str_mv 0264410X
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dc.relation.citationIssue.none.fl_str_mv No. 14
dc.relation.citationStartPage.none.fl_str_mv 1830
dc.relation.citationTitle.none.fl_str_mv Vaccine
dc.relation.citationVolume.none.fl_str_mv Vol. 31
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spelling eca483d3-a229-42c8-8a6d-3b5e6f002e5b-191225589-1453006a5-2ec3-4faf-8e32-a9d7075d519d-19a090035-7467-44ed-a0ec-490f7325f9e8-179653065-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-12020-05-26T00:02:13Z2020-05-26T00:02:13Z2013Identifying the minimal functional regions of the proteins which the malaria parasite uses when invading its host cells constitutes the first and most important approach in an effective design for a chemically synthesised, multi-antigen, multi-stage, subunit-based vaccine. This work has been aimed at identifying the PfRh1 protein binding regions (residues 1-2580) belonging to the reticulocyte binding-like (RBL or P. falciparum Rh [PfRh]) family implicated in the parasite's alternative target cell invasion routes. Eighteen peptide regions (called high activity binding peptides - HABPs) binding to red blood cells (RBC) were identified in peptides mapped in a highly robust, specific and sensitive receptor-ligand assay. These HABPs were saturable in the experimental conditions assayed here and most had an alpha helix structure. Polymorphism studies revealed that only six of the eighteen HABPs identified had changes at amino acid level amongst the seven P. falciparum strains evaluated. Most HABPs' specific binding became altered when RBC were treated with neuraminidase, chymotrypsin and trypsin, suggesting differing sensitivity for RBC membrane receptors. After ascertaining that the Rh1 gene was transcribed and expressed in late-stage schizonts of the FCB-2 strain, invasion inhibition assays were carried out. When most of these HABPs were assayed in P. falciparum in vitro culture they were able to inhibit high percentages of FVO strain invasion compared to low inhibition percentages observed with the FCB-2 strain. This data shows small Rh1 regions' participation during invasion and suggests that these units should be included in further immunological and structural studies. © 2013 Elsevier Ltd.application/pdfhttps://doi.org/10.1016/j.vaccine.2013.01.0520264410X13588745https://repository.urosario.edu.co/handle/10336/23460eng1837No. 141830VaccineVol. 31Vaccine, ISSN:0264410X, 13588745, Vol.31, No.14 (2013); pp. 1830-1837https://www.scopus.com/inward/record.uri?eid=2-s2.0-84875262025&doi=10.1016%2fj.vaccine.2013.01.052&partnerID=40&md5=311561ae13a870b5a99facbc23290097Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURAmino acidMembrane receptorProteinRh1 proteinUnclassified drugAlpha helixArticleCell invasionControlled studyErythrocyteGene expressionIn vitro studyNonhumanPlasmodium falciparumPriority journalProtein bindingProtein polymorphismReticulocyteSchizontAmino acid sequenceErythrocytesHost-pathogen interactionsHumansMalariaMalaria vaccinesMolecular sequence dataPeptidesPlasmodium falciparumProtein structure, secondaryProtein structure, tertiaryProtozoan proteinsSchizontsMalariaPlasmodium falciparumReticulocyte binding-likeSynthetic peptidesubunitVaccinesRh1 high activity binding peptides inhibit high percentages of Plasmodium falciparum FVO strain invasionarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Arévalo-Pinzón, GabrielaCurtidor, HernandoMuñoz, MarinaSuarez, DianaPatarroyo, Manuel A.Patarroyo, Manuel E.ORIGINALRh1_high_activity_binding_peptides_inhib.pdfapplication/pdf792301https://repository.urosario.edu.co/bitstreams/351f8605-b6f1-42d5-9083-52a4e5610cd4/download7854252c56fb9614bd0a60da7e348228MD51TEXTRh1_high_activity_binding_peptides_inhib.pdf.txtRh1_high_activity_binding_peptides_inhib.pdf.txtExtracted texttext/plain48377https://repository.urosario.edu.co/bitstreams/a43c5767-7501-4da8-8f8f-e3a268cc7867/download5aeba60b94632fc7faaa93f8b2c68cf2MD52THUMBNAILRh1_high_activity_binding_peptides_inhib.pdf.jpgRh1_high_activity_binding_peptides_inhib.pdf.jpgGenerated Thumbnailimage/jpeg4673https://repository.urosario.edu.co/bitstreams/358f4ecf-9b3a-49f7-bd30-a5fa23961a6c/downloadc3f397f23244c69ca19051dc21bcd0f9MD5310336/23460oai:repository.urosario.edu.co:10336/234602022-05-02 07:37:14.606099https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co