Peptides from the Mycobacterium tuberculosis Rv1980c protein involved in human cell infection: Insights into new synthetic subunit vaccine candidates

Mycobacterium tuberculosis infection continues to be a major cause of morbidity and mortality throughout the world. The vast complexity of the intracellular pathogen M. tuberculosis and the diverse mechanisms by which it can invade host cells highlight the importance of developing a fully protective...

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Autores:
Tipo de recurso:
Fecha de publicación:
2010
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/23522
Acceso en línea:
https://doi.org/10.1515/BC.2010.019
https://repository.urosario.edu.co/handle/10336/23522
Palabra clave:
Bacterial protein
Binding protein
High activity binding peptide 31100
High activity binding peptide 31101
High activity binding peptide 31107
Protein rv1980c
Subunit vaccine
Unclassified drug
Article
Bacterial gene
Binding affinity
Cell invasion
Cell surface
Controlled study
Genetic transcription
Host cell
Human
Human cell
Immunoelectron microscopy
Macrophage
Monocyte
Morbidity
Mortality
Mycobacterium tuberculosis
Nonhuman
Polymerase chain reaction
Priority journal
Reverse transcription polymerase chain reaction
Rv1980c gene
Tuberculosis
Bacterial proteins
Bacterial vaccines
Binding sites
Humans
Mycobacterium tuberculosis
Peptide fragments
Pneumocytes
Corynebacterineae
Mycobacterium tuberculosis
Binding interactions
Immunodetection
Internalization
Invasion inhibition
Peptide
Tuberculosis
western
synthetic
molecular
genetic
cultured
Blotting
Cells
Models
Transcription
Vaccines
Rights
License
Abierto (Texto Completo)
id EDOCUR2_cd1ee3be4c3046ae9ead4455ff9838ee
oai_identifier_str oai:repository.urosario.edu.co:10336/23522
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 5299469960051848826600796530656009de1cfc2-5d95-4925-a819-b9b2b20ff2d2-191225589-1cdd258b7-f8e9-4fd4-9db6-cd3c5b66e69f-19e3ba9df-fe89-48fe-9521-cc8f452d56f5-12020-05-26T00:02:46Z2020-05-26T00:02:46Z2010Mycobacterium tuberculosis infection continues to be a major cause of morbidity and mortality throughout the world. The vast complexity of the intracellular pathogen M. tuberculosis and the diverse mechanisms by which it can invade host cells highlight the importance of developing a fully protective vaccine. Our vaccine development strategy consists of including fragments from multiple mycobacterial proteins involved in cell invasion. The aim of this study was to identify high activity binding peptides (HABPs) in the immunogenic protein Rv1980c from M. tuberculosis H37Rv with the ability to inhibit mycobacterial invasion into U937 monocyte-derived macrophages and A549 cells. The presence and transcription of the Rv1980c gene was assessed in members belonging to the M. tuberculosis complex and other nontuberculous mycobacteria by PCR and RT-PCR, respectively. Cell surface localization was confirmed by immunoelectron microscopy. Three peptides binding with high activity to U937 cells and one to A549 cells were identified. HABPs 31100, 31101, and 31107 inhibited invasion of M. tuberculosis into A549 and U937 cells and therefore could be promising candidates for the design of a subunit-based antituberculous vaccine. © 2010 by Walter de Gruyter Berlin New York.application/pdfhttps://doi.org/10.1515/BC.2010.0191431673014374315https://repository.urosario.edu.co/handle/10336/23522eng217No. 43892207Biological ChemistryVol. 391Biological Chemistry, ISSN:14316730, 14374315, Vol.391, No.43892 (2010); pp. 207-217https://www.scopus.com/inward/record.uri?eid=2-s2.0-77749341488&doi=10.1515%2fBC.2010.019&partnerID=40&md5=bf7333e6188d1e8e692e93f5d7780cf9Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURBacterial proteinBinding proteinHigh activity binding peptide 31100High activity binding peptide 31101High activity binding peptide 31107Protein rv1980cSubunit vaccineUnclassified drugArticleBacterial geneBinding affinityCell invasionCell surfaceControlled studyGenetic transcriptionHost cellHumanHuman cellImmunoelectron microscopyMacrophageMonocyteMorbidityMortalityMycobacterium tuberculosisNonhumanPolymerase chain reactionPriority journalReverse transcription polymerase chain reactionRv1980c geneTuberculosisBacterial proteinsBacterial vaccinesBinding sitesHumansMycobacterium tuberculosisPeptide fragmentsPneumocytesCorynebacterineaeMycobacterium tuberculosisBinding interactionsImmunodetectionInternalizationInvasion inhibitionPeptideTuberculosiswesternsyntheticmoleculargeneticculturedBlottingCellsModelsTranscriptionVaccinesPeptides from the Mycobacterium tuberculosis Rv1980c protein involved in human cell infection: Insights into new synthetic subunit vaccine candidatesarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Rodríguez Burbano, Diana ConsueloOcampo, MarisolPatarroyo, Manuel A.Vizcaíno, CarolinaCurtidor, HernandoPinto, MartaPatarroyo, Manuel Elkin10336/23522oai:repository.urosario.edu.co:10336/235222022-05-02 07:37:14.550943https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Peptides from the Mycobacterium tuberculosis Rv1980c protein involved in human cell infection: Insights into new synthetic subunit vaccine candidates
title Peptides from the Mycobacterium tuberculosis Rv1980c protein involved in human cell infection: Insights into new synthetic subunit vaccine candidates
spellingShingle Peptides from the Mycobacterium tuberculosis Rv1980c protein involved in human cell infection: Insights into new synthetic subunit vaccine candidates
Bacterial protein
Binding protein
High activity binding peptide 31100
High activity binding peptide 31101
High activity binding peptide 31107
Protein rv1980c
Subunit vaccine
Unclassified drug
Article
Bacterial gene
Binding affinity
Cell invasion
Cell surface
Controlled study
Genetic transcription
Host cell
Human
Human cell
Immunoelectron microscopy
Macrophage
Monocyte
Morbidity
Mortality
Mycobacterium tuberculosis
Nonhuman
Polymerase chain reaction
Priority journal
Reverse transcription polymerase chain reaction
Rv1980c gene
Tuberculosis
Bacterial proteins
Bacterial vaccines
Binding sites
Humans
Mycobacterium tuberculosis
Peptide fragments
Pneumocytes
Corynebacterineae
Mycobacterium tuberculosis
Binding interactions
Immunodetection
Internalization
Invasion inhibition
Peptide
Tuberculosis
western
synthetic
molecular
genetic
cultured
Blotting
Cells
Models
Transcription
Vaccines
title_short Peptides from the Mycobacterium tuberculosis Rv1980c protein involved in human cell infection: Insights into new synthetic subunit vaccine candidates
title_full Peptides from the Mycobacterium tuberculosis Rv1980c protein involved in human cell infection: Insights into new synthetic subunit vaccine candidates
title_fullStr Peptides from the Mycobacterium tuberculosis Rv1980c protein involved in human cell infection: Insights into new synthetic subunit vaccine candidates
title_full_unstemmed Peptides from the Mycobacterium tuberculosis Rv1980c protein involved in human cell infection: Insights into new synthetic subunit vaccine candidates
title_sort Peptides from the Mycobacterium tuberculosis Rv1980c protein involved in human cell infection: Insights into new synthetic subunit vaccine candidates
dc.subject.keyword.spa.fl_str_mv Bacterial protein
Binding protein
High activity binding peptide 31100
High activity binding peptide 31101
High activity binding peptide 31107
Protein rv1980c
Subunit vaccine
Unclassified drug
Article
Bacterial gene
Binding affinity
Cell invasion
Cell surface
Controlled study
Genetic transcription
Host cell
Human
Human cell
Immunoelectron microscopy
Macrophage
Monocyte
Morbidity
Mortality
Mycobacterium tuberculosis
Nonhuman
Polymerase chain reaction
Priority journal
Reverse transcription polymerase chain reaction
Rv1980c gene
Tuberculosis
Bacterial proteins
Bacterial vaccines
Binding sites
Humans
Mycobacterium tuberculosis
Peptide fragments
Pneumocytes
Corynebacterineae
Mycobacterium tuberculosis
Binding interactions
Immunodetection
Internalization
Invasion inhibition
Peptide
Tuberculosis
topic Bacterial protein
Binding protein
High activity binding peptide 31100
High activity binding peptide 31101
High activity binding peptide 31107
Protein rv1980c
Subunit vaccine
Unclassified drug
Article
Bacterial gene
Binding affinity
Cell invasion
Cell surface
Controlled study
Genetic transcription
Host cell
Human
Human cell
Immunoelectron microscopy
Macrophage
Monocyte
Morbidity
Mortality
Mycobacterium tuberculosis
Nonhuman
Polymerase chain reaction
Priority journal
Reverse transcription polymerase chain reaction
Rv1980c gene
Tuberculosis
Bacterial proteins
Bacterial vaccines
Binding sites
Humans
Mycobacterium tuberculosis
Peptide fragments
Pneumocytes
Corynebacterineae
Mycobacterium tuberculosis
Binding interactions
Immunodetection
Internalization
Invasion inhibition
Peptide
Tuberculosis
western
synthetic
molecular
genetic
cultured
Blotting
Cells
Models
Transcription
Vaccines
dc.subject.keyword.eng.fl_str_mv western
synthetic
molecular
genetic
cultured
Blotting
Cells
Models
Transcription
Vaccines
description Mycobacterium tuberculosis infection continues to be a major cause of morbidity and mortality throughout the world. The vast complexity of the intracellular pathogen M. tuberculosis and the diverse mechanisms by which it can invade host cells highlight the importance of developing a fully protective vaccine. Our vaccine development strategy consists of including fragments from multiple mycobacterial proteins involved in cell invasion. The aim of this study was to identify high activity binding peptides (HABPs) in the immunogenic protein Rv1980c from M. tuberculosis H37Rv with the ability to inhibit mycobacterial invasion into U937 monocyte-derived macrophages and A549 cells. The presence and transcription of the Rv1980c gene was assessed in members belonging to the M. tuberculosis complex and other nontuberculous mycobacteria by PCR and RT-PCR, respectively. Cell surface localization was confirmed by immunoelectron microscopy. Three peptides binding with high activity to U937 cells and one to A549 cells were identified. HABPs 31100, 31101, and 31107 inhibited invasion of M. tuberculosis into A549 and U937 cells and therefore could be promising candidates for the design of a subunit-based antituberculous vaccine. © 2010 by Walter de Gruyter Berlin New York.
publishDate 2010
dc.date.created.spa.fl_str_mv 2010
dc.date.accessioned.none.fl_str_mv 2020-05-26T00:02:46Z
dc.date.available.none.fl_str_mv 2020-05-26T00:02:46Z
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/10.1515/BC.2010.019
dc.identifier.issn.none.fl_str_mv 14316730
14374315
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/23522
url https://doi.org/10.1515/BC.2010.019
https://repository.urosario.edu.co/handle/10336/23522
identifier_str_mv 14316730
14374315
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 217
dc.relation.citationIssue.none.fl_str_mv No. 43892
dc.relation.citationStartPage.none.fl_str_mv 207
dc.relation.citationTitle.none.fl_str_mv Biological Chemistry
dc.relation.citationVolume.none.fl_str_mv Vol. 391
dc.relation.ispartof.spa.fl_str_mv Biological Chemistry, ISSN:14316730, 14374315, Vol.391, No.43892 (2010); pp. 207-217
dc.relation.uri.spa.fl_str_mv https://www.scopus.com/inward/record.uri?eid=2-s2.0-77749341488&doi=10.1515%2fBC.2010.019&partnerID=40&md5=bf7333e6188d1e8e692e93f5d7780cf9
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_ 1814167525615730688