The Mycobacterium tuberculosis membrane protein Rv0180c: Evaluation of peptide sequences implicated in mycobacterial invasion of two human cell lines

The identification and characterization of hypothetical membrane proteins from Mycobacterium tuberculosis have led to a better understanding of the mechanisms used by this pathogen to invade and survive inside host cells. This study assessed the presence, transcription, localization and possible bio...

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Tipo de recurso:
Fecha de publicación:
2011
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/22787
Acceso en línea:
https://doi.org/10.1016/j.peptides.2010.09.017
https://repository.urosario.edu.co/handle/10336/22787
Palabra clave:
Bacterial protein
Membrane protein
Protein rv0180c
Unclassified drug
Amino acid sequence
Animal experiment
Article
Drug mechanism
Goat
Human
Human cell
Immunoelectron microscopy
Mycobacterium tuberculosis
Nonhuman
Polymerase chain reaction
Priority journal
Protein localization
Western blotting
Amino acid sequence
Bacterial proteins
Cell line
Circular dichroism
Humans
Membrane proteins
Molecular sequence data
Mycobacterium tuberculosis
Peptides
U937 cells
Bacilli (class)
Mycobacterium microti
Mycobacterium tuberculosis
Invasion inhibition assays
Latex bead internalization
Mycobacterium tuberculosis
Pexel motif
Rv0180c
immunoelectron
genetic
Microscopy
Transcription
Rights
License
Abierto (Texto Completo)
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dc.title.spa.fl_str_mv The Mycobacterium tuberculosis membrane protein Rv0180c: Evaluation of peptide sequences implicated in mycobacterial invasion of two human cell lines
title The Mycobacterium tuberculosis membrane protein Rv0180c: Evaluation of peptide sequences implicated in mycobacterial invasion of two human cell lines
spellingShingle The Mycobacterium tuberculosis membrane protein Rv0180c: Evaluation of peptide sequences implicated in mycobacterial invasion of two human cell lines
Bacterial protein
Membrane protein
Protein rv0180c
Unclassified drug
Amino acid sequence
Animal experiment
Article
Drug mechanism
Goat
Human
Human cell
Immunoelectron microscopy
Mycobacterium tuberculosis
Nonhuman
Polymerase chain reaction
Priority journal
Protein localization
Western blotting
Amino acid sequence
Bacterial proteins
Cell line
Circular dichroism
Humans
Membrane proteins
Molecular sequence data
Mycobacterium tuberculosis
Peptides
U937 cells
Bacilli (class)
Mycobacterium microti
Mycobacterium tuberculosis
Invasion inhibition assays
Latex bead internalization
Mycobacterium tuberculosis
Pexel motif
Rv0180c
immunoelectron
genetic
Microscopy
Transcription
title_short The Mycobacterium tuberculosis membrane protein Rv0180c: Evaluation of peptide sequences implicated in mycobacterial invasion of two human cell lines
title_full The Mycobacterium tuberculosis membrane protein Rv0180c: Evaluation of peptide sequences implicated in mycobacterial invasion of two human cell lines
title_fullStr The Mycobacterium tuberculosis membrane protein Rv0180c: Evaluation of peptide sequences implicated in mycobacterial invasion of two human cell lines
title_full_unstemmed The Mycobacterium tuberculosis membrane protein Rv0180c: Evaluation of peptide sequences implicated in mycobacterial invasion of two human cell lines
title_sort The Mycobacterium tuberculosis membrane protein Rv0180c: Evaluation of peptide sequences implicated in mycobacterial invasion of two human cell lines
dc.subject.keyword.spa.fl_str_mv Bacterial protein
Membrane protein
Protein rv0180c
Unclassified drug
Amino acid sequence
Animal experiment
Article
Drug mechanism
Goat
Human
Human cell
Immunoelectron microscopy
Mycobacterium tuberculosis
Nonhuman
Polymerase chain reaction
Priority journal
Protein localization
Western blotting
Amino acid sequence
Bacterial proteins
Cell line
Circular dichroism
Humans
Membrane proteins
Molecular sequence data
Mycobacterium tuberculosis
Peptides
U937 cells
Bacilli (class)
Mycobacterium microti
Mycobacterium tuberculosis
Invasion inhibition assays
Latex bead internalization
Mycobacterium tuberculosis
Pexel motif
Rv0180c
topic Bacterial protein
Membrane protein
Protein rv0180c
Unclassified drug
Amino acid sequence
Animal experiment
Article
Drug mechanism
Goat
Human
Human cell
Immunoelectron microscopy
Mycobacterium tuberculosis
Nonhuman
Polymerase chain reaction
Priority journal
Protein localization
Western blotting
Amino acid sequence
Bacterial proteins
Cell line
Circular dichroism
Humans
Membrane proteins
Molecular sequence data
Mycobacterium tuberculosis
Peptides
U937 cells
Bacilli (class)
Mycobacterium microti
Mycobacterium tuberculosis
Invasion inhibition assays
Latex bead internalization
Mycobacterium tuberculosis
Pexel motif
Rv0180c
immunoelectron
genetic
Microscopy
Transcription
dc.subject.keyword.eng.fl_str_mv immunoelectron
genetic
Microscopy
Transcription
description The identification and characterization of hypothetical membrane proteins from Mycobacterium tuberculosis have led to a better understanding of the mechanisms used by this pathogen to invade and survive inside host cells. This study assessed the presence, transcription, localization and possible biological activity of the conserved hypothetical protein Rv0180c from M. tuberculosis. Bioinformatics analyses indicated that Rv0180c contains a signal peptide, six possible transmembrane helices and a Plasmodium Export Element (PEXEL)-like motif. PCR analyses showed the presence of the Rv0180c gene in strains from the M. tuberculosis complex; but transcription was not detected in Mycobacterium microti. Sera against synthetic peptides of Rv0180c recognized two protein bands in M. tuberculosis H37Rv sonicate: a ?48-kDa band close to the predicted molecular mass of Rv0180c (47.6 kDa), and a 63-kDa band probably caused by protein modifications. Moreover, the same sera located the protein on the surface of M. tuberculosis H37Rv bacilli by immunoelectron microscopy. Twenty-three synthetic peptides spanning the entire length of Rv0180c were tested for their ability to bind to U937 and A549 cells, finding nine high-activity binding peptides (HABPs) specific for both cell types, two HABPs specific for A549 cells (namely 31032 and 31044) and two HABPs specific for U937 cells (namely 31025 and 31041). HABPs inhibited invasion of M. tuberculosis H37Rv into A549 or U937 cells by significant percentages and facilitated internalization of latex beads in A549 cells. The Rv0180c HABPs herein reported could be preliminary candidates to be assessed as components of a multiepitope, chemically synthesized, subunit-based vaccine against tuberculosis. © 2010 Elsevier Inc. All rights reserved.
publishDate 2011
dc.date.created.spa.fl_str_mv 2011
dc.date.accessioned.none.fl_str_mv 2020-05-25T23:58:01Z
dc.date.available.none.fl_str_mv 2020-05-25T23:58:01Z
dc.type.eng.fl_str_mv article
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dc.type.spa.spa.fl_str_mv Artículo
dc.identifier.doi.none.fl_str_mv https://doi.org/10.1016/j.peptides.2010.09.017
dc.identifier.issn.none.fl_str_mv 1969781
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/22787
url https://doi.org/10.1016/j.peptides.2010.09.017
https://repository.urosario.edu.co/handle/10336/22787
identifier_str_mv 1969781
dc.language.iso.spa.fl_str_mv eng
language eng
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dc.relation.citationIssue.none.fl_str_mv No. 1
dc.relation.citationStartPage.none.fl_str_mv 1
dc.relation.citationTitle.none.fl_str_mv Peptides
dc.relation.citationVolume.none.fl_str_mv Vol. 32
dc.relation.ispartof.spa.fl_str_mv Peptides, ISSN:1969781, Vol.32, No.1 (2011); pp. 1-10
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spelling 5bba3b6a-0bf5-4981-ac32-116820b32ca5-129ed545e-1ec1-4586-800c-4a2758cab090-172114b23-9a0b-4914-a288-3ac7305d4eed-10b11362c-9b7a-44d8-b34d-7f310ab176a7-176e03223-040d-4e46-864f-3bdecc8d2790-19fc64f6d-a903-48f1-ac2e-4e55fd2ed9af-12020-05-25T23:58:01Z2020-05-25T23:58:01Z2011The identification and characterization of hypothetical membrane proteins from Mycobacterium tuberculosis have led to a better understanding of the mechanisms used by this pathogen to invade and survive inside host cells. This study assessed the presence, transcription, localization and possible biological activity of the conserved hypothetical protein Rv0180c from M. tuberculosis. Bioinformatics analyses indicated that Rv0180c contains a signal peptide, six possible transmembrane helices and a Plasmodium Export Element (PEXEL)-like motif. PCR analyses showed the presence of the Rv0180c gene in strains from the M. tuberculosis complex; but transcription was not detected in Mycobacterium microti. Sera against synthetic peptides of Rv0180c recognized two protein bands in M. tuberculosis H37Rv sonicate: a ?48-kDa band close to the predicted molecular mass of Rv0180c (47.6 kDa), and a 63-kDa band probably caused by protein modifications. Moreover, the same sera located the protein on the surface of M. tuberculosis H37Rv bacilli by immunoelectron microscopy. Twenty-three synthetic peptides spanning the entire length of Rv0180c were tested for their ability to bind to U937 and A549 cells, finding nine high-activity binding peptides (HABPs) specific for both cell types, two HABPs specific for A549 cells (namely 31032 and 31044) and two HABPs specific for U937 cells (namely 31025 and 31041). HABPs inhibited invasion of M. tuberculosis H37Rv into A549 or U937 cells by significant percentages and facilitated internalization of latex beads in A549 cells. The Rv0180c HABPs herein reported could be preliminary candidates to be assessed as components of a multiepitope, chemically synthesized, subunit-based vaccine against tuberculosis. © 2010 Elsevier Inc. All rights reserved.application/pdfhttps://doi.org/10.1016/j.peptides.2010.09.0171969781https://repository.urosario.edu.co/handle/10336/22787eng10No. 11PeptidesVol. 32Peptides, ISSN:1969781, Vol.32, No.1 (2011); pp. 1-10https://www.scopus.com/inward/record.uri?eid=2-s2.0-78650523266&doi=10.1016%2fj.peptides.2010.09.017&partnerID=40&md5=2be7762b7feada53607dee795ba47e8eAbierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURBacterial proteinMembrane proteinProtein rv0180cUnclassified drugAmino acid sequenceAnimal experimentArticleDrug mechanismGoatHumanHuman cellImmunoelectron microscopyMycobacterium tuberculosisNonhumanPolymerase chain reactionPriority journalProtein localizationWestern blottingAmino acid sequenceBacterial proteinsCell lineCircular dichroismHumansMembrane proteinsMolecular sequence dataMycobacterium tuberculosisPeptidesU937 cellsBacilli (class)Mycobacterium microtiMycobacterium tuberculosisInvasion inhibition assaysLatex bead internalizationMycobacterium tuberculosisPexel motifRv0180cimmunoelectrongeneticMicroscopyTranscriptionThe Mycobacterium tuberculosis membrane protein Rv0180c: Evaluation of peptide sequences implicated in mycobacterial invasion of two human cell linesarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Cáceres S.M.Ocampo M.Arévalo-Pinzón G.Jimenez R.A.Patarroyo M.E.Patarroyo M.A.ORIGINAL1-s2-0-S0196978110004031-main.pdfapplication/pdf746250https://repository.urosario.edu.co/bitstreams/94d3311b-a773-4901-806f-257207119873/download7e5bf5db63269e1903efa029fc26084eMD51TEXT1-s2-0-S0196978110004031-main.pdf.txt1-s2-0-S0196978110004031-main.pdf.txtExtracted texttext/plain60948https://repository.urosario.edu.co/bitstreams/143c63c8-9f7c-4d74-8ce2-7405bf4583c9/download5644cfd15405f2c06f4f4fcf5cc00f98MD52THUMBNAIL1-s2-0-S0196978110004031-main.pdf.jpg1-s2-0-S0196978110004031-main.pdf.jpgGenerated Thumbnailimage/jpeg4739https://repository.urosario.edu.co/bitstreams/258c49f8-1257-4e0a-bda5-ff1396618ebd/download26726c60ef6944a0f367a429ef425c75MD5310336/22787oai:repository.urosario.edu.co:10336/227872022-05-02 07:37:14.367983https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co