Identification and evaluation of universal epitopes in Plasmodium vivax Duffy binding protein

Selected PvDBP-derived synthetic peptides were tested in competition assays with HLA molecules in order to identify and evaluate their binding to a wide range of MHC class II molecules. Binding was evaluated as the peptide's ability to displace the biotinylated control peptide (HA306-318) and w...

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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:10336/23504
Acceso en línea:
https://doi.org/10.1016/j.bbrc.2008.10.153
https://repository.urosario.edu.co/handle/10336/23504
Palabra clave:
Duffy binding protein
Epitope
Hla dr1 antigen
Hla dr11 antigen
Hla dr4 antigen
Hla dr7 antigen
Unclassified drug
Antigen binding
Article
Biotinylation
Controlled study
Enzyme linked immunosorbent assay
Nucleotide sequence
Plasmodium vivax
Priority journal
Protein analysis
Amino acid sequence
Animals
Epitope mapping
Hla-dr antigens
Immunodominant epitopes
Malaria vaccines
Molecular sequence data
Peptides
Plasmodium vivax
Protein conformation
Protozoan proteins
Receptors, cell surface
Sequence alignment
Vaccines, synthetic
Plasmodium vivax
Duffy binding protein (dbp)
Malaria
Plasmodium vivax
Universal epitopes
cell surface
protozoan
synthetic
Rights
License
Abierto (Texto Completo)
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spelling b6e36d05-19f8-4f97-b0fe-8807d163c303-11609eecf-af24-4e1e-9f07-4f944f55908f-176467280-a15b-4c27-99b0-5b63a4a9266a-1e08b398f-d152-45f2-94ea-b8ffa291ac69-16fc431a4-2889-4e78-ba01-10c2807c6557-179653065-12020-05-26T00:02:35Z2020-05-26T00:02:35Z2008Selected PvDBP-derived synthetic peptides were tested in competition assays with HLA molecules in order to identify and evaluate their binding to a wide range of MHC class II molecules. Binding was evaluated as the peptide's ability to displace the biotinylated control peptide (HA306-318) and was detected by a conventional ELISA. Thus, one epitope for the HLA-DR1 molecule, two epitopes for the HLA-DR4 molecule, six epitopes for the HLA-DR7 molecule and three epitopes for the HLA-DR11 molecule displaying a high binding percentage (above 50%) were experimentally obtained. The in vitro results were compared with the epitope prediction results. Two peptides behaved as universal epitopes since they bound to a larger number of HLA-DR molecules. Given that these peptides are located in the conserved PvDBP region II, they could be considered good candidates to be included in the design of a synthetic vaccine against Plasmodium vivax malaria. © 2008 Elsevier Inc. All rights reserved.application/pdfhttps://doi.org/10.1016/j.bbrc.2008.10.1530006-291X1090-2104https://repository.urosario.edu.co/handle/10336/23504eng1283No. 41279Biochemical and Biophysical Research CommunicationsVol. 377Biochemical and Biophysical Research Communications, ISSN:0006-291X, 1090-2104, Vol.377, No.4 (2008); pp. 1279-1283https://www.scopus.com/inward/record.uri?eid=2-s2.0-56349138132&doi=10.1016%2fj.bbrc.2008.10.153&partnerID=40&md5=43e85aaec428ebeae8cf0d29273a5aceAbierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURDuffy binding proteinEpitopeHla dr1 antigenHla dr11 antigenHla dr4 antigenHla dr7 antigenUnclassified drugAntigen bindingArticleBiotinylationControlled studyEnzyme linked immunosorbent assayNucleotide sequencePlasmodium vivaxPriority journalProtein analysisAmino acid sequenceAnimalsEpitope mappingHla-dr antigensImmunodominant epitopesMalaria vaccinesMolecular sequence dataPeptidesPlasmodium vivaxProtein conformationProtozoan proteinsReceptors, cell surfaceSequence alignmentVaccines, syntheticPlasmodium vivaxDuffy binding protein (dbp)MalariaPlasmodium vivaxUniversal epitopescell surfaceprotozoansyntheticIdentification and evaluation of universal epitopes in Plasmodium vivax Duffy binding proteinarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Saravia, CarolinaMartinez, PaolaGranados, Diana S.Lopez, CarolinaReyes, ClaudiaPatarroyo, Manuel A.ORIGINALIdentification_and_evaluation_of_univers.pdfapplication/pdf452483https://repository.urosario.edu.co/bitstreams/7473b143-d3f3-4c9e-909a-c268f2f41302/download002217e6147b85a7fa1858fcbd8b8c61MD51TEXTIdentification_and_evaluation_of_univers.pdf.txtIdentification_and_evaluation_of_univers.pdf.txtExtracted texttext/plain29387https://repository.urosario.edu.co/bitstreams/a0e8cfab-42c5-4266-be78-252cba90c71d/download8084c1cb126a4983a1f52edbdb19184aMD52THUMBNAILIdentification_and_evaluation_of_univers.pdf.jpgIdentification_and_evaluation_of_univers.pdf.jpgGenerated Thumbnailimage/jpeg4942https://repository.urosario.edu.co/bitstreams/61754539-f327-4a73-b37e-e9a4b65ce347/downloadb13fa9a62af0653d5a0f5605d3e0236fMD5310336/23504oai:repository.urosario.edu.co:10336/235042022-05-02 07:37:13.084572https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Identification and evaluation of universal epitopes in Plasmodium vivax Duffy binding protein
title Identification and evaluation of universal epitopes in Plasmodium vivax Duffy binding protein
spellingShingle Identification and evaluation of universal epitopes in Plasmodium vivax Duffy binding protein
Duffy binding protein
Epitope
Hla dr1 antigen
Hla dr11 antigen
Hla dr4 antigen
Hla dr7 antigen
Unclassified drug
Antigen binding
Article
Biotinylation
Controlled study
Enzyme linked immunosorbent assay
Nucleotide sequence
Plasmodium vivax
Priority journal
Protein analysis
Amino acid sequence
Animals
Epitope mapping
Hla-dr antigens
Immunodominant epitopes
Malaria vaccines
Molecular sequence data
Peptides
Plasmodium vivax
Protein conformation
Protozoan proteins
Receptors, cell surface
Sequence alignment
Vaccines, synthetic
Plasmodium vivax
Duffy binding protein (dbp)
Malaria
Plasmodium vivax
Universal epitopes
cell surface
protozoan
synthetic
title_short Identification and evaluation of universal epitopes in Plasmodium vivax Duffy binding protein
title_full Identification and evaluation of universal epitopes in Plasmodium vivax Duffy binding protein
title_fullStr Identification and evaluation of universal epitopes in Plasmodium vivax Duffy binding protein
title_full_unstemmed Identification and evaluation of universal epitopes in Plasmodium vivax Duffy binding protein
title_sort Identification and evaluation of universal epitopes in Plasmodium vivax Duffy binding protein
dc.subject.keyword.spa.fl_str_mv Duffy binding protein
Epitope
Hla dr1 antigen
Hla dr11 antigen
Hla dr4 antigen
Hla dr7 antigen
Unclassified drug
Antigen binding
Article
Biotinylation
Controlled study
Enzyme linked immunosorbent assay
Nucleotide sequence
Plasmodium vivax
Priority journal
Protein analysis
Amino acid sequence
Animals
Epitope mapping
Hla-dr antigens
Immunodominant epitopes
Malaria vaccines
Molecular sequence data
Peptides
Plasmodium vivax
Protein conformation
Protozoan proteins
Receptors, cell surface
Sequence alignment
Vaccines, synthetic
Plasmodium vivax
Duffy binding protein (dbp)
Malaria
Plasmodium vivax
Universal epitopes
topic Duffy binding protein
Epitope
Hla dr1 antigen
Hla dr11 antigen
Hla dr4 antigen
Hla dr7 antigen
Unclassified drug
Antigen binding
Article
Biotinylation
Controlled study
Enzyme linked immunosorbent assay
Nucleotide sequence
Plasmodium vivax
Priority journal
Protein analysis
Amino acid sequence
Animals
Epitope mapping
Hla-dr antigens
Immunodominant epitopes
Malaria vaccines
Molecular sequence data
Peptides
Plasmodium vivax
Protein conformation
Protozoan proteins
Receptors, cell surface
Sequence alignment
Vaccines, synthetic
Plasmodium vivax
Duffy binding protein (dbp)
Malaria
Plasmodium vivax
Universal epitopes
cell surface
protozoan
synthetic
dc.subject.keyword.eng.fl_str_mv cell surface
protozoan
synthetic
description Selected PvDBP-derived synthetic peptides were tested in competition assays with HLA molecules in order to identify and evaluate their binding to a wide range of MHC class II molecules. Binding was evaluated as the peptide's ability to displace the biotinylated control peptide (HA306-318) and was detected by a conventional ELISA. Thus, one epitope for the HLA-DR1 molecule, two epitopes for the HLA-DR4 molecule, six epitopes for the HLA-DR7 molecule and three epitopes for the HLA-DR11 molecule displaying a high binding percentage (above 50%) were experimentally obtained. The in vitro results were compared with the epitope prediction results. Two peptides behaved as universal epitopes since they bound to a larger number of HLA-DR molecules. Given that these peptides are located in the conserved PvDBP region II, they could be considered good candidates to be included in the design of a synthetic vaccine against Plasmodium vivax malaria. © 2008 Elsevier Inc. All rights reserved.
publishDate 2008
dc.date.created.spa.fl_str_mv 2008
dc.date.accessioned.none.fl_str_mv 2020-05-26T00:02:35Z
dc.date.available.none.fl_str_mv 2020-05-26T00:02:35Z
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.2008.10.153
dc.identifier.issn.none.fl_str_mv 0006-291X
1090-2104
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/23504
url https://doi.org/10.1016/j.bbrc.2008.10.153
https://repository.urosario.edu.co/handle/10336/23504
identifier_str_mv 0006-291X
1090-2104
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 1283
dc.relation.citationIssue.none.fl_str_mv No. 4
dc.relation.citationStartPage.none.fl_str_mv 1279
dc.relation.citationTitle.none.fl_str_mv Biochemical and Biophysical Research Communications
dc.relation.citationVolume.none.fl_str_mv Vol. 377
dc.relation.ispartof.spa.fl_str_mv Biochemical and Biophysical Research Communications, ISSN:0006-291X, 1090-2104, Vol.377, No.4 (2008); pp. 1279-1283
dc.relation.uri.spa.fl_str_mv https://www.scopus.com/inward/record.uri?eid=2-s2.0-56349138132&doi=10.1016%2fj.bbrc.2008.10.153&partnerID=40&md5=43e85aaec428ebeae8cf0d29273a5ace
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dc.rights.acceso.spa.fl_str_mv Abierto (Texto Completo)
rights_invalid_str_mv Abierto (Texto Completo)
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