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...

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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)
id EDOCUR2_2e160c3fb9471bd3a2214c935ceff83f
oai_identifier_str oai:repository.urosario.edu.co:10336/22893
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 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
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