Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing

The Plasmodium falciparum acidic–basic repeat antigen represents a potential malarial vaccine candidate. One of this protein’s high activity binding peptides, named 2150 (161KMNMLKENVDYIQKNQNLFK180), is conserved, non-immunogenic, and non-protection-inducing. Analogue peptides whose critical binding...

Full description

Autores:
Tipo de recurso:
Fecha de publicación:
2004
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/26036
Acceso en línea:
https://doi.org/10.1016/j.bbrc.2004.07.086
https://repository.urosario.edu.co/handle/10336/26036
Palabra clave:
ABRA protein
Peptide analogues
Vaccine candidate
Malaria
Conformation
NMR
Rights
License
Restringido (Acceso a grupos específicos)
id EDOCUR2_33494b4267bb496e0ba29635fe4e6f7d
oai_identifier_str oai:repository.urosario.edu.co:10336/26036
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 4fda4c81-5558-46e6-a038-005cc454bf3a-108b7b42f-4645-4ff5-a2ef-eaccc7f7eab0-191225589-17087a113-5fb2-42c2-9e86-ec137635b868-17b000441-0f07-4b3f-8025-f0c59b37d338-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-1518908816002020-08-06T16:20:30Z2020-08-06T16:20:30Z2004-09-10The Plasmodium falciparum acidic–basic repeat antigen represents a potential malarial vaccine candidate. One of this protein’s high activity binding peptides, named 2150 (161KMNMLKENVDYIQKNQNLFK180), is conserved, non-immunogenic, and non-protection-inducing. Analogue peptides whose critical binding residues (in bold) were replaced by amino-acids having similar mass but different charge were synthesized and tested to try to modify such immunological properties. These analogues’ HLA-DR?1* molecule binding ability were also studied in an attempt to explain their biological mechanisms and correlate binding capacity and immunological function with their three-dimensional structure determined by 1H NMR. A 310 distorted helical structure was identified in protective and immunogenic peptide 24922 whilst ?-helical structure was found for non-immunogenic, non-protective peptides having differences in ?-helical position. The changes performed on immunogenic, protection-inducing peptide 24922 allowed it to bind specifically to the HLA-DR?1*0301 molecule, suggesting that these changes may lead to better interaction with the MHC Class II-peptide-TCR complex rendering it immunogenic and protective, thus suggesting a new way of developing multi-component, sub-unit-based anti-malarial vaccines.application/pdfhttps://doi.org/10.1016/j.bbrc.2004.07.086ISSN: 0006-291XEISSN: 1090-2104https://repository.urosario.edu.co/handle/10336/26036engElsevier125No. 1119Biochemical and Biophysical Research CommunicationsVol. 332Biochemical and Biophysical Research Communications, ISSN: 0006-291X;EISSN: 1090-2104, Vol.332, No.1 (2004); pp.119-125https://www.sciencedirect.com/science/article/abs/pii/S0006291X04015803?via%3DihubRestringido (Acceso a grupos específicos)http://purl.org/coar/access_right/c_16ecBiochemical and Biophysical Research Communicationsinstname:Universidad del Rosarioreponame:Repositorio Institucional EdocURABRA proteinPeptide analoguesVaccine candidateMalariaConformationNMRChanging ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducingCambiar el péptido de la proteína ABRA para que se ajuste a la molécula HLA-DRbeta1 * 0301 hace que induzca la protecciónarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Salazar, Luz M.Alba, Martha P.Curtidor, HernandoVargas, Luis E.Rivera, Zuly J.Patarroyo, Manuel E.Bermudez, Adriana10336/26036oai:repository.urosario.edu.co:10336/260362021-06-03 00:50:24.513https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing
dc.title.TranslatedTitle.spa.fl_str_mv Cambiar el péptido de la proteína ABRA para que se ajuste a la molécula HLA-DRbeta1 * 0301 hace que induzca la protección
title Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing
spellingShingle Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing
ABRA protein
Peptide analogues
Vaccine candidate
Malaria
Conformation
NMR
title_short Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing
title_full Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing
title_fullStr Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing
title_full_unstemmed Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing
title_sort Changing ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing
dc.subject.keyword.spa.fl_str_mv ABRA protein
Peptide analogues
Vaccine candidate
Malaria
Conformation
NMR
topic ABRA protein
Peptide analogues
Vaccine candidate
Malaria
Conformation
NMR
description The Plasmodium falciparum acidic–basic repeat antigen represents a potential malarial vaccine candidate. One of this protein’s high activity binding peptides, named 2150 (161KMNMLKENVDYIQKNQNLFK180), is conserved, non-immunogenic, and non-protection-inducing. Analogue peptides whose critical binding residues (in bold) were replaced by amino-acids having similar mass but different charge were synthesized and tested to try to modify such immunological properties. These analogues’ HLA-DR?1* molecule binding ability were also studied in an attempt to explain their biological mechanisms and correlate binding capacity and immunological function with their three-dimensional structure determined by 1H NMR. A 310 distorted helical structure was identified in protective and immunogenic peptide 24922 whilst ?-helical structure was found for non-immunogenic, non-protective peptides having differences in ?-helical position. The changes performed on immunogenic, protection-inducing peptide 24922 allowed it to bind specifically to the HLA-DR?1*0301 molecule, suggesting that these changes may lead to better interaction with the MHC Class II-peptide-TCR complex rendering it immunogenic and protective, thus suggesting a new way of developing multi-component, sub-unit-based anti-malarial vaccines.
publishDate 2004
dc.date.created.spa.fl_str_mv 2004-09-10
dc.date.accessioned.none.fl_str_mv 2020-08-06T16:20:30Z
dc.date.available.none.fl_str_mv 2020-08-06T16:20:30Z
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.2004.07.086
dc.identifier.issn.none.fl_str_mv ISSN: 0006-291X
EISSN: 1090-2104
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/26036
url https://doi.org/10.1016/j.bbrc.2004.07.086
https://repository.urosario.edu.co/handle/10336/26036
identifier_str_mv ISSN: 0006-291X
EISSN: 1090-2104
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 125
dc.relation.citationIssue.none.fl_str_mv No. 1
dc.relation.citationStartPage.none.fl_str_mv 119
dc.relation.citationTitle.none.fl_str_mv Biochemical and Biophysical Research Communications
dc.relation.citationVolume.none.fl_str_mv Vol. 332
dc.relation.ispartof.spa.fl_str_mv Biochemical and Biophysical Research Communications, ISSN: 0006-291X;EISSN: 1090-2104, Vol.332, No.1 (2004); pp.119-125
dc.relation.uri.spa.fl_str_mv https://www.sciencedirect.com/science/article/abs/pii/S0006291X04015803?via%3Dihub
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_16ec
dc.rights.acceso.spa.fl_str_mv Restringido (Acceso a grupos específicos)
rights_invalid_str_mv Restringido (Acceso a grupos específicos)
http://purl.org/coar/access_right/c_16ec
dc.format.mimetype.none.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Elsevier
dc.source.spa.fl_str_mv Biochemical and Biophysical Research Communications
institution Universidad del Rosario
dc.source.instname.none.fl_str_mv instname:Universidad del Rosario
dc.source.reponame.none.fl_str_mv reponame:Repositorio Institucional EdocUR
repository.name.fl_str_mv Repositorio institucional EdocUR
repository.mail.fl_str_mv edocur@urosario.edu.co
_version_ 1814167431630815232