Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines
The Rv2707 gene encoding a putative alanine- and leucine-rich protein was found to be present in all Mycobacterium tuberculosis complex strains (by PCR) and its transcription was shown by RT-PCR in all but M. bovis and M. microti. Antibodies raised against Rv2707 peptides specifically recognized the...
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2008
- Institución:
- Universidad del Rosario
- Repositorio:
- Repositorio EdocUR - U. Rosario
- Idioma:
- eng
- OAI Identifier:
- oai:repository.urosario.edu.co:10336/22893
- Acceso en línea:
- https://doi.org/10.1110/ps.073083308
https://repository.urosario.edu.co/handle/10336/22893
- Palabra clave:
- Bacterial protein
Protein rv2707
Unclassified drug
Amino acid sequence
Article
Controlled study
Gene location
Gene sequence
Human
Human cell
Mycobacterium tuberculosis
Nonhuman
Priority journal
Reverse transcription polymerase chain reaction
Amino acid sequence
Bacterial proteins
Computational biology
Humans
Molecular sequence data
Mycobacterium tuberculosis
Peptide fragments
Protein binding
U937 cells
Mycobacterium tuberculosis
Mycobacterium tuberculosis complex
A549 cell
High activity binding peptide (habp)
Invasion
Mycobacterium tuberculosis
Rv2707
U937 cell
tumor
immunoelectron
Cell line
Microscopy
- Rights
- License
- Abierto (Texto Completo)
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89d3e5c4-5f74-4e70-a942-c0fb7b05d57b-14f4f34c8-2d4c-491e-813c-5d61ee2d1048-191225589-184cece1e-359c-45a6-b251-f8e4b62a84eb-151721018-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-179653065-12020-05-25T23:58:36Z2020-05-25T23:58:36Z2008The Rv2707 gene encoding a putative alanine- and leucine-rich protein was found to be present in all Mycobacterium tuberculosis complex strains (by PCR) and its transcription was shown by RT-PCR in all but M. bovis and M. microti. Antibodies raised against Rv2707 peptides specifically recognized the native protein by Western blot and were able to locate this protein on the M. tuberculosis membrane by immunoelectron microscopy. A549 and U937 cells lines were used in binding assays involving synthetic peptides covering the whole Rv2707 protein. High A549 cell-binding peptide 16083 ( 281QEEWPAPATHAHRLGNWLKAY300) was identified. Peptides 16072 (61LFGPDTLPAIEKSALSTAHSY80) and 16084 ( 301RIGVGTTTYSSTAQHSAVAA320) presented high specific binding to both A549 and U937 cells. Cross-linking assays revealed that peptide 16084 specifically bound to a 40-kDa and a 50-kDa U937 cell membrane protein. High activity binding peptides (HABPs) 16083 and 16084 were able to inhibit M. tuberculosis invasion of A549 cells. Our results suggest that these sequences could be part of the binding sites used by the bacillus for interacting with target cells, and thus represent good candidates to be tested in a future subunit-based, multiepitope, antituberculosis vaccine. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society.application/pdfhttps://doi.org/10.1110/ps.0730833089618368https://repository.urosario.edu.co/handle/10336/22893eng351No. 2342Protein ScienceVol. 17Protein Science, ISSN:9618368, Vol.17, No.2 (2008); pp. 342-351https://www.scopus.com/inward/record.uri?eid=2-s2.0-38649085597&doi=10.1110%2fps.073083308&partnerID=40&md5=cbe73a4fab2ccb62d7cf0f2fd23f15d5Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURBacterial proteinProtein rv2707Unclassified drugAmino acid sequenceArticleControlled studyGene locationGene sequenceHumanHuman cellMycobacterium tuberculosisNonhumanPriority journalReverse transcription polymerase chain reactionAmino acid sequenceBacterial proteinsComputational biologyHumansMolecular sequence dataMycobacterium tuberculosisPeptide fragmentsProtein bindingU937 cellsMycobacterium tuberculosisMycobacterium tuberculosis complexA549 cellHigh activity binding peptide (habp)InvasionMycobacterium tuberculosisRv2707U937 celltumorimmunoelectronCell lineMicroscopyCharacterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell linesarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Chapeton?Montes, Julie A.Plaza, David F.Curtidor, HernandoForero, MarthaVanegas, MagnoliaPatarroyo, Manuel E.Patarroyo, Manuel A.10336/22893oai:repository.urosario.edu.co:10336/228932022-05-02 07:37:20.810861https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co |
dc.title.spa.fl_str_mv |
Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines |
title |
Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines |
spellingShingle |
Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines Bacterial protein Protein rv2707 Unclassified drug Amino acid sequence Article Controlled study Gene location Gene sequence Human Human cell Mycobacterium tuberculosis Nonhuman Priority journal Reverse transcription polymerase chain reaction Amino acid sequence Bacterial proteins Computational biology Humans Molecular sequence data Mycobacterium tuberculosis Peptide fragments Protein binding U937 cells Mycobacterium tuberculosis Mycobacterium tuberculosis complex A549 cell High activity binding peptide (habp) Invasion Mycobacterium tuberculosis Rv2707 U937 cell tumor immunoelectron Cell line Microscopy |
title_short |
Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines |
title_full |
Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines |
title_fullStr |
Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines |
title_full_unstemmed |
Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines |
title_sort |
Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines |
dc.subject.keyword.spa.fl_str_mv |
Bacterial protein Protein rv2707 Unclassified drug Amino acid sequence Article Controlled study Gene location Gene sequence Human Human cell Mycobacterium tuberculosis Nonhuman Priority journal Reverse transcription polymerase chain reaction Amino acid sequence Bacterial proteins Computational biology Humans Molecular sequence data Mycobacterium tuberculosis Peptide fragments Protein binding U937 cells Mycobacterium tuberculosis Mycobacterium tuberculosis complex A549 cell High activity binding peptide (habp) Invasion Mycobacterium tuberculosis Rv2707 U937 cell |
topic |
Bacterial protein Protein rv2707 Unclassified drug Amino acid sequence Article Controlled study Gene location Gene sequence Human Human cell Mycobacterium tuberculosis Nonhuman Priority journal Reverse transcription polymerase chain reaction Amino acid sequence Bacterial proteins Computational biology Humans Molecular sequence data Mycobacterium tuberculosis Peptide fragments Protein binding U937 cells Mycobacterium tuberculosis Mycobacterium tuberculosis complex A549 cell High activity binding peptide (habp) Invasion Mycobacterium tuberculosis Rv2707 U937 cell tumor immunoelectron Cell line Microscopy |
dc.subject.keyword.eng.fl_str_mv |
tumor immunoelectron Cell line Microscopy |
description |
The Rv2707 gene encoding a putative alanine- and leucine-rich protein was found to be present in all Mycobacterium tuberculosis complex strains (by PCR) and its transcription was shown by RT-PCR in all but M. bovis and M. microti. Antibodies raised against Rv2707 peptides specifically recognized the native protein by Western blot and were able to locate this protein on the M. tuberculosis membrane by immunoelectron microscopy. A549 and U937 cells lines were used in binding assays involving synthetic peptides covering the whole Rv2707 protein. High A549 cell-binding peptide 16083 ( 281QEEWPAPATHAHRLGNWLKAY300) was identified. Peptides 16072 (61LFGPDTLPAIEKSALSTAHSY80) and 16084 ( 301RIGVGTTTYSSTAQHSAVAA320) presented high specific binding to both A549 and U937 cells. Cross-linking assays revealed that peptide 16084 specifically bound to a 40-kDa and a 50-kDa U937 cell membrane protein. High activity binding peptides (HABPs) 16083 and 16084 were able to inhibit M. tuberculosis invasion of A549 cells. Our results suggest that these sequences could be part of the binding sites used by the bacillus for interacting with target cells, and thus represent good candidates to be tested in a future subunit-based, multiepitope, antituberculosis vaccine. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society. |
publishDate |
2008 |
dc.date.created.spa.fl_str_mv |
2008 |
dc.date.accessioned.none.fl_str_mv |
2020-05-25T23:58:36Z |
dc.date.available.none.fl_str_mv |
2020-05-25T23:58:36Z |
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/10.1110/ps.073083308 |
dc.identifier.issn.none.fl_str_mv |
9618368 |
dc.identifier.uri.none.fl_str_mv |
https://repository.urosario.edu.co/handle/10336/22893 |
url |
https://doi.org/10.1110/ps.073083308 https://repository.urosario.edu.co/handle/10336/22893 |
identifier_str_mv |
9618368 |
dc.language.iso.spa.fl_str_mv |
eng |
language |
eng |
dc.relation.citationEndPage.none.fl_str_mv |
351 |
dc.relation.citationIssue.none.fl_str_mv |
No. 2 |
dc.relation.citationStartPage.none.fl_str_mv |
342 |
dc.relation.citationTitle.none.fl_str_mv |
Protein Science |
dc.relation.citationVolume.none.fl_str_mv |
Vol. 17 |
dc.relation.ispartof.spa.fl_str_mv |
Protein Science, ISSN:9618368, Vol.17, No.2 (2008); pp. 342-351 |
dc.relation.uri.spa.fl_str_mv |
https://www.scopus.com/inward/record.uri?eid=2-s2.0-38649085597&doi=10.1110%2fps.073083308&partnerID=40&md5=cbe73a4fab2ccb62d7cf0f2fd23f15d5 |
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_ |
1814167570440257536 |