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