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...

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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)
id EDOCUR2_0dbe94a913dfd850e530d4f8ae43c059
oai_identifier_str oai:repository.urosario.edu.co:10336/23782
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 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
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