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...
- 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)
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Repositorio EdocUR - U. Rosario |
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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 |