Functional, biochemical and 3D studies of Mycobacterium tuberculosis protein peptides for an effective anti-tuberculosis vaccine
Tuberculosis (TB) is an air-born, transmissible disease, having an estimated 9.4 million new TB cases worldwide in 2009. Eventual control of this disease by developing a safe and efficient new vaccine able to detain its spread will have an enormous impact on public health policy. Selecting potential...
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2014
- Institución:
- Universidad del Rosario
- Repositorio:
- Repositorio EdocUR - U. Rosario
- Idioma:
- eng
- OAI Identifier:
- oai:repository.urosario.edu.co:10336/23782
- Acceso en línea:
- https://doi.org/10.3109/1040841X.2013.763221
https://repository.urosario.edu.co/handle/10336/23782
- Palabra clave:
- Bacterial antigen
Bacterial protein
Bcg vaccine
Rv 0180 c protein
Rv 0227 c protein
Rv 0679 c protein
Rv 1490 protein
Rv 1510 c protein
Rv 1980 c protein
Rv 2004 c protein
Rv 2301 protein
Rv 2536 protein
Rv 2560 protein
Rv 2707 protein
Rv 2969c protein
Rv 3166 c protein
Rv 3481 c protein
Rv 3629 c protein
Rv 3630 protein
Rv 3804 c protein
Rv 3910 protein
Synthetic peptide
Unclassified drug
Bioinformatics
Immune response
Molecular biology
Mycobacterium tuberculosis
Nonhuman
Priority journal
Protein analysis
Protein binding
Protein function
Proteomics
Review
Three dimensional imaging
Bacterial adhesion
Bacterial proteins
Cell line
Epithelial cells
Humans
Macrophages
Mycobacterium tuberculosis
Tuberculosis vaccines
Mycobacterium tuberculosis surface protein
Receptor-ligand interaction
Subunit-vaccine
Synthetic-peptides
bacterial
Antigens
- Rights
- License
- Abierto (Texto Completo)
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5184882660079653065-151721018-108b7b42f-4645-4ff5-a2ef-eaccc7f7eab0-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-12020-05-26T00:05:21Z2020-05-26T00:05:21Z2014Tuberculosis (TB) is an air-born, transmissible disease, having an estimated 9.4 million new TB cases worldwide in 2009. Eventual control of this disease by developing a safe and efficient new vaccine able to detain its spread will have an enormous impact on public health policy. Selecting potential antigens to be included in a multi-epitope, minimal subunit-based, chemically-synthesized vaccine containing the minimum sequences needed for blocking mycobacterial interaction with host cells is a complex task due to the multiple mechanisms involved in M. tuberculosis infection and the mycobacterium's immune evasion mechanisms. Our methodology, described here takes into account a highly robust, specific, sensitive and functional approach to the search for potential epitopes to be included in an anti-TB vaccine; it has been based on identifying short mycobacterial protein fragments using synthetic peptides having high affinity interaction with alveolar epithelial cells (A549) and monocyte-derived macrophages (U937) which are able to block the microorganism's entry to target cells in in vitro assays. This manuscript presents a review of the results obtained with some of the MTB H37Rv proteins studied to date, aimed at using these high activity binding peptides (HABPs) as platforms to be included in a minimal subunit-based, multiepitope, chemically-synthesized, antituberculosis vaccine. © 2014 Informa Healthcare USA, Inc. All rights reserved: reproduction in whole or part not permitted.application/pdfhttps://doi.org/10.3109/1040841X.2013.763221154978281040841Xhttps://repository.urosario.edu.co/handle/10336/23782eng145No. 2117Critical Reviews in MicrobiologyVol. 40Critical Reviews in Microbiology, ISSN:15497828, 1040841X, Vol.40, No.2 (2014); pp. 117-145https://www.scopus.com/inward/record.uri?eid=2-s2.0-84891085960&doi=10.3109%2f1040841X.2013.763221&partnerID=40&md5=ed6960a662a4b4df4c6560ddc2487e93Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURBacterial antigenBacterial proteinBcg vaccineRv 0180 c proteinRv 0227 c proteinRv 0679 c proteinRv 1490 proteinRv 1510 c proteinRv 1980 c proteinRv 2004 c proteinRv 2301 proteinRv 2536 proteinRv 2560 proteinRv 2707 proteinRv 2969c proteinRv 3166 c proteinRv 3481 c proteinRv 3629 c proteinRv 3630 proteinRv 3804 c proteinRv 3910 proteinSynthetic peptideUnclassified drugBioinformaticsImmune responseMolecular biologyMycobacterium tuberculosisNonhumanPriority journalProtein analysisProtein bindingProtein functionProteomicsReviewThree dimensional imagingBacterial adhesionBacterial proteinsCell lineEpithelial cellsHumansMacrophagesMycobacterium tuberculosisTuberculosis vaccinesMycobacterium tuberculosis surface proteinReceptor-ligand interactionSubunit-vaccineSynthetic-peptidesbacterialAntigensFunctional, biochemical and 3D studies of Mycobacterium tuberculosis protein peptides for an effective anti-tuberculosis vaccinearticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Ocampo, MarisolPatarroyo, Manuel A.Vanegas, MagnoliaAlba, Martha P.Patarroyo, Manuel E.10336/23782oai:repository.urosario.edu.co:10336/237822022-05-02 07:37:19.442384https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co |
dc.title.spa.fl_str_mv |
Functional, biochemical and 3D studies of Mycobacterium tuberculosis protein peptides for an effective anti-tuberculosis vaccine |
title |
Functional, biochemical and 3D studies of Mycobacterium tuberculosis protein peptides for an effective anti-tuberculosis vaccine |
spellingShingle |
Functional, biochemical and 3D studies of Mycobacterium tuberculosis protein peptides for an effective anti-tuberculosis vaccine Bacterial antigen Bacterial protein Bcg vaccine Rv 0180 c protein Rv 0227 c protein Rv 0679 c protein Rv 1490 protein Rv 1510 c protein Rv 1980 c protein Rv 2004 c protein Rv 2301 protein Rv 2536 protein Rv 2560 protein Rv 2707 protein Rv 2969c protein Rv 3166 c protein Rv 3481 c protein Rv 3629 c protein Rv 3630 protein Rv 3804 c protein Rv 3910 protein Synthetic peptide Unclassified drug Bioinformatics Immune response Molecular biology Mycobacterium tuberculosis Nonhuman Priority journal Protein analysis Protein binding Protein function Proteomics Review Three dimensional imaging Bacterial adhesion Bacterial proteins Cell line Epithelial cells Humans Macrophages Mycobacterium tuberculosis Tuberculosis vaccines Mycobacterium tuberculosis surface protein Receptor-ligand interaction Subunit-vaccine Synthetic-peptides bacterial Antigens |
title_short |
Functional, biochemical and 3D studies of Mycobacterium tuberculosis protein peptides for an effective anti-tuberculosis vaccine |
title_full |
Functional, biochemical and 3D studies of Mycobacterium tuberculosis protein peptides for an effective anti-tuberculosis vaccine |
title_fullStr |
Functional, biochemical and 3D studies of Mycobacterium tuberculosis protein peptides for an effective anti-tuberculosis vaccine |
title_full_unstemmed |
Functional, biochemical and 3D studies of Mycobacterium tuberculosis protein peptides for an effective anti-tuberculosis vaccine |
title_sort |
Functional, biochemical and 3D studies of Mycobacterium tuberculosis protein peptides for an effective anti-tuberculosis vaccine |
dc.subject.keyword.spa.fl_str_mv |
Bacterial antigen Bacterial protein Bcg vaccine Rv 0180 c protein Rv 0227 c protein Rv 0679 c protein Rv 1490 protein Rv 1510 c protein Rv 1980 c protein Rv 2004 c protein Rv 2301 protein Rv 2536 protein Rv 2560 protein Rv 2707 protein Rv 2969c protein Rv 3166 c protein Rv 3481 c protein Rv 3629 c protein Rv 3630 protein Rv 3804 c protein Rv 3910 protein Synthetic peptide Unclassified drug Bioinformatics Immune response Molecular biology Mycobacterium tuberculosis Nonhuman Priority journal Protein analysis Protein binding Protein function Proteomics Review Three dimensional imaging Bacterial adhesion Bacterial proteins Cell line Epithelial cells Humans Macrophages Mycobacterium tuberculosis Tuberculosis vaccines Mycobacterium tuberculosis surface protein Receptor-ligand interaction Subunit-vaccine Synthetic-peptides |
topic |
Bacterial antigen Bacterial protein Bcg vaccine Rv 0180 c protein Rv 0227 c protein Rv 0679 c protein Rv 1490 protein Rv 1510 c protein Rv 1980 c protein Rv 2004 c protein Rv 2301 protein Rv 2536 protein Rv 2560 protein Rv 2707 protein Rv 2969c protein Rv 3166 c protein Rv 3481 c protein Rv 3629 c protein Rv 3630 protein Rv 3804 c protein Rv 3910 protein Synthetic peptide Unclassified drug Bioinformatics Immune response Molecular biology Mycobacterium tuberculosis Nonhuman Priority journal Protein analysis Protein binding Protein function Proteomics Review Three dimensional imaging Bacterial adhesion Bacterial proteins Cell line Epithelial cells Humans Macrophages Mycobacterium tuberculosis Tuberculosis vaccines Mycobacterium tuberculosis surface protein Receptor-ligand interaction Subunit-vaccine Synthetic-peptides bacterial Antigens |
dc.subject.keyword.eng.fl_str_mv |
bacterial Antigens |
description |
Tuberculosis (TB) is an air-born, transmissible disease, having an estimated 9.4 million new TB cases worldwide in 2009. Eventual control of this disease by developing a safe and efficient new vaccine able to detain its spread will have an enormous impact on public health policy. Selecting potential antigens to be included in a multi-epitope, minimal subunit-based, chemically-synthesized vaccine containing the minimum sequences needed for blocking mycobacterial interaction with host cells is a complex task due to the multiple mechanisms involved in M. tuberculosis infection and the mycobacterium's immune evasion mechanisms. Our methodology, described here takes into account a highly robust, specific, sensitive and functional approach to the search for potential epitopes to be included in an anti-TB vaccine; it has been based on identifying short mycobacterial protein fragments using synthetic peptides having high affinity interaction with alveolar epithelial cells (A549) and monocyte-derived macrophages (U937) which are able to block the microorganism's entry to target cells in in vitro assays. This manuscript presents a review of the results obtained with some of the MTB H37Rv proteins studied to date, aimed at using these high activity binding peptides (HABPs) as platforms to be included in a minimal subunit-based, multiepitope, chemically-synthesized, antituberculosis vaccine. © 2014 Informa Healthcare USA, Inc. All rights reserved: reproduction in whole or part not permitted. |
publishDate |
2014 |
dc.date.created.spa.fl_str_mv |
2014 |
dc.date.accessioned.none.fl_str_mv |
2020-05-26T00:05:21Z |
dc.date.available.none.fl_str_mv |
2020-05-26T00:05:21Z |
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/10.3109/1040841X.2013.763221 |
dc.identifier.issn.none.fl_str_mv |
15497828 1040841X |
dc.identifier.uri.none.fl_str_mv |
https://repository.urosario.edu.co/handle/10336/23782 |
url |
https://doi.org/10.3109/1040841X.2013.763221 https://repository.urosario.edu.co/handle/10336/23782 |
identifier_str_mv |
15497828 1040841X |
dc.language.iso.spa.fl_str_mv |
eng |
language |
eng |
dc.relation.citationEndPage.none.fl_str_mv |
145 |
dc.relation.citationIssue.none.fl_str_mv |
No. 2 |
dc.relation.citationStartPage.none.fl_str_mv |
117 |
dc.relation.citationTitle.none.fl_str_mv |
Critical Reviews in Microbiology |
dc.relation.citationVolume.none.fl_str_mv |
Vol. 40 |
dc.relation.ispartof.spa.fl_str_mv |
Critical Reviews in Microbiology, ISSN:15497828, 1040841X, Vol.40, No.2 (2014); pp. 117-145 |
dc.relation.uri.spa.fl_str_mv |
https://www.scopus.com/inward/record.uri?eid=2-s2.0-84891085960&doi=10.3109%2f1040841X.2013.763221&partnerID=40&md5=ed6960a662a4b4df4c6560ddc2487e93 |
dc.rights.coar.fl_str_mv |
http://purl.org/coar/access_right/c_abf2 |
dc.rights.acceso.spa.fl_str_mv |
Abierto (Texto Completo) |
rights_invalid_str_mv |
Abierto (Texto Completo) http://purl.org/coar/access_right/c_abf2 |
dc.format.mimetype.none.fl_str_mv |
application/pdf |
institution |
Universidad del Rosario |
dc.source.instname.spa.fl_str_mv |
instname:Universidad del Rosario |
dc.source.reponame.spa.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_ |
1814167724589318144 |