Identifying putative Mycobacterium tuberculosis Rv2004c protein sequences that bind specifically to U937 macrophages and A549 epithelial cells

Virulence and immunity are still poorly understood in Mycobacterium tuberculo sis.TheH37RvM. tubercu-losis laboratory strain genome has been completely sequenced, and this along with proteomic technologyrepresent powerful tools contributing toward studying the biology of target cell interaction with...

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Tipo de recurso:
Fecha de publicación:
2005
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/27843
Acceso en línea:
https://doi.org/10.1110/ps.051592505
https://repository.urosario.edu.co/handle/10336/27843
Palabra clave:
Mycobacterium tuberculosis
Rv2004c protein
High activity binding peptides
U937 cells
A549 cells
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id EDOCUR2_02f484a700d56a168691d728e7764616
oai_identifier_str oai:repository.urosario.edu.co:10336/27843
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 84cece1e-359c-45a6-b251-f8e4b62a84eb-1f2d05f42-2948-4c51-8389-8c3817c2d0f1-1d191987c-6e13-4f7f-88bd-c34b437b85c6-134b82e95-53e0-4ba5-a5c5-d4191164afa1-1ef6547b6-3130-435a-8a09-7ca050cd7b64-1791292836002020-08-19T14:44:12Z2020-08-19T14:44:12Z2005-11Virulence and immunity are still poorly understood in Mycobacterium tuberculo sis.TheH37RvM. tubercu-losis laboratory strain genome has been completely sequenced, and this along with proteomic technologyrepresent powerful tools contributing toward studying the biology of target cell interaction with a facultativebacillus and designing new strategies for controlling tuberculosis. Rv2004c is a putative M. tuberculosisprotein that could have specific mycobacterial functions. This study has revealed that the encoding gene ispresent in all mycobacterium species belonging to the M. tuberculosis complex. Rv2004c gene transcriptionwas observed in all of this complex’s strains except Mycobacterium bovis and Mycobacterium microti.Rv2004c protein expression was confirmed by using antibodies able to recognize a 54-kDa molecule byimmunoblotting, and its location was detected on the M. tuberculosis surface by transmission electronmicroscopy, suggesting that it is a mycobacterial surface protein. Binding assays led to recognizing highactivity binding peptides (HABP); five HABPs specifically bound to U937 cells, and six specifically boundto A549 cells. HABP circular dichroism suggested that they had an a-helical structure. HABP–target cellinteraction was determined to be specific and saturable ; some of them also displayed greater affinity for A549cells than U937 cells. The critical amino acids directly involved in their interaction with U937 cells were alsodetermined. Two probable receptor molecules were found on U937 cells and five on A549 for the twoHABPs analyzed. These observations have important biological significance for studying bacillus–target cellinteractions and implications for developing strategies for controlling this diseaseapplication/pdfhttps://doi.org/10.1110/ps.051592505ISSN: 0961-8368EISSN: 1469-896Xhttps://repository.urosario.edu.co/handle/10336/27843engThe Protein SocietyJohn Wiley & Son2780No. 112767Protein ScienceVol. 14Protein Science, ISSN: 0961-8368;EISSN: 1469-896X, Vol.14, No.11 (November 2005); pp. 2767-2780https://onlinelibrary.wiley.com/doi/epdf/10.1110/ps.051592505Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2Protein Scienceinstname:Universidad del Rosarioreponame:Repositorio Institucional EdocURMycobacterium tuberculosisRv2004c proteinHigh activity binding peptidesU937 cellsA549 cellsIdentifying putative Mycobacterium tuberculosis Rv2004c protein sequences that bind specifically to U937 macrophages and A549 epithelial cellsIdentificación de secuencias de proteínas putativas de Mycobacterium tuberculosis Rv2004c que se unen específicamente a macrófagos U937 y células epiteliales A549articleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Forero, MarthaPuentes, ÁlvaroCortés, JimenaVera, RicardoRodríguez, Luis E.Castillo-Rivera, Fabio10336/27843oai:repository.urosario.edu.co:10336/278432022-05-02 07:37:15.389457https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Identifying putative Mycobacterium tuberculosis Rv2004c protein sequences that bind specifically to U937 macrophages and A549 epithelial cells
dc.title.TranslatedTitle.spa.fl_str_mv Identificación de secuencias de proteínas putativas de Mycobacterium tuberculosis Rv2004c que se unen específicamente a macrófagos U937 y células epiteliales A549
title Identifying putative Mycobacterium tuberculosis Rv2004c protein sequences that bind specifically to U937 macrophages and A549 epithelial cells
spellingShingle Identifying putative Mycobacterium tuberculosis Rv2004c protein sequences that bind specifically to U937 macrophages and A549 epithelial cells
Mycobacterium tuberculosis
Rv2004c protein
High activity binding peptides
U937 cells
A549 cells
title_short Identifying putative Mycobacterium tuberculosis Rv2004c protein sequences that bind specifically to U937 macrophages and A549 epithelial cells
title_full Identifying putative Mycobacterium tuberculosis Rv2004c protein sequences that bind specifically to U937 macrophages and A549 epithelial cells
title_fullStr Identifying putative Mycobacterium tuberculosis Rv2004c protein sequences that bind specifically to U937 macrophages and A549 epithelial cells
title_full_unstemmed Identifying putative Mycobacterium tuberculosis Rv2004c protein sequences that bind specifically to U937 macrophages and A549 epithelial cells
title_sort Identifying putative Mycobacterium tuberculosis Rv2004c protein sequences that bind specifically to U937 macrophages and A549 epithelial cells
dc.subject.keyword.spa.fl_str_mv Mycobacterium tuberculosis
Rv2004c protein
High activity binding peptides
U937 cells
A549 cells
topic Mycobacterium tuberculosis
Rv2004c protein
High activity binding peptides
U937 cells
A549 cells
description Virulence and immunity are still poorly understood in Mycobacterium tuberculo sis.TheH37RvM. tubercu-losis laboratory strain genome has been completely sequenced, and this along with proteomic technologyrepresent powerful tools contributing toward studying the biology of target cell interaction with a facultativebacillus and designing new strategies for controlling tuberculosis. Rv2004c is a putative M. tuberculosisprotein that could have specific mycobacterial functions. This study has revealed that the encoding gene ispresent in all mycobacterium species belonging to the M. tuberculosis complex. Rv2004c gene transcriptionwas observed in all of this complex’s strains except Mycobacterium bovis and Mycobacterium microti.Rv2004c protein expression was confirmed by using antibodies able to recognize a 54-kDa molecule byimmunoblotting, and its location was detected on the M. tuberculosis surface by transmission electronmicroscopy, suggesting that it is a mycobacterial surface protein. Binding assays led to recognizing highactivity binding peptides (HABP); five HABPs specifically bound to U937 cells, and six specifically boundto A549 cells. HABP circular dichroism suggested that they had an a-helical structure. HABP–target cellinteraction was determined to be specific and saturable ; some of them also displayed greater affinity for A549cells than U937 cells. The critical amino acids directly involved in their interaction with U937 cells were alsodetermined. Two probable receptor molecules were found on U937 cells and five on A549 for the twoHABPs analyzed. These observations have important biological significance for studying bacillus–target cellinteractions and implications for developing strategies for controlling this disease
publishDate 2005
dc.date.created.spa.fl_str_mv 2005-11
dc.date.accessioned.none.fl_str_mv 2020-08-19T14:44:12Z
dc.date.available.none.fl_str_mv 2020-08-19T14:44:12Z
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.051592505
dc.identifier.issn.none.fl_str_mv ISSN: 0961-8368
EISSN: 1469-896X
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/27843
url https://doi.org/10.1110/ps.051592505
https://repository.urosario.edu.co/handle/10336/27843
identifier_str_mv ISSN: 0961-8368
EISSN: 1469-896X
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 2780
dc.relation.citationIssue.none.fl_str_mv No. 11
dc.relation.citationStartPage.none.fl_str_mv 2767
dc.relation.citationTitle.none.fl_str_mv Protein Science
dc.relation.citationVolume.none.fl_str_mv Vol. 14
dc.relation.ispartof.spa.fl_str_mv Protein Science, ISSN: 0961-8368;EISSN: 1469-896X, Vol.14, No.11 (November 2005); pp. 2767-2780
dc.relation.uri.spa.fl_str_mv https://onlinelibrary.wiley.com/doi/epdf/10.1110/ps.051592505
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
dc.publisher.spa.fl_str_mv The Protein Society
John Wiley & Son
dc.source.spa.fl_str_mv Protein Science
institution Universidad del Rosario
dc.source.instname.none.fl_str_mv instname:Universidad del Rosario
dc.source.reponame.none.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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