Mycobacterial laminin-binding histone-like protein mediates collagen-dependent cytoadherence
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Memórias do Instituto Oswaldo Cruz |
Texto Completo: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762012000900025 |
Resumo: | When grown in the presence of exogenous collagen I, Mycobacterium bovis BCG was shown to form clumps. Scanning electron microscopy examination of these clumps revealed the presence of collagen fibres cross-linking the bacilli. Since collagen is a major constituent of the eukaryotic extracellular matrices, we assayed BCG cytoadherence in the presence of exogenous collagen I. Collagen increased the interaction of the bacilli with A549 type II pneumocytes or U937 macrophages, suggesting that BCG is able to recruit collagen to facilitate its attachment to host cells. Using an affinity chromatography approach, we have isolated a BCG collagen-binding protein corresponding to the previously described mycobacterial laminin-binding histone-like protein (LBP/Hlp), a highly conserved protein associated with the mycobacterial cell wall. Moreover, Mycobacterium leprae LBP/Hlp, a well-characterized adhesin, was also able to bind collagen I. Finally, using recombinant fragments of M. leprae LBP/Hlp, we mapped the collagen-binding activity within the C-terminal domain of the adhesin. Since this protein was already shown to be involved in the recognition of laminin and heparan sulphate-containing proteoglycans, the present observations reinforce the adhesive activities of LBP/Hlp, which can be therefore considered as a multifaceted mycobacterial adhesin, playing an important role in both leprosy and tuberculosis pathogenesis. |
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Memórias do Instituto Oswaldo Cruz |
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Mycobacterial laminin-binding histone-like protein mediates collagen-dependent cytoadherencemycobacteriacytoadherencecollagenhistone-like proteinleprosytuberculosisWhen grown in the presence of exogenous collagen I, Mycobacterium bovis BCG was shown to form clumps. Scanning electron microscopy examination of these clumps revealed the presence of collagen fibres cross-linking the bacilli. Since collagen is a major constituent of the eukaryotic extracellular matrices, we assayed BCG cytoadherence in the presence of exogenous collagen I. Collagen increased the interaction of the bacilli with A549 type II pneumocytes or U937 macrophages, suggesting that BCG is able to recruit collagen to facilitate its attachment to host cells. Using an affinity chromatography approach, we have isolated a BCG collagen-binding protein corresponding to the previously described mycobacterial laminin-binding histone-like protein (LBP/Hlp), a highly conserved protein associated with the mycobacterial cell wall. Moreover, Mycobacterium leprae LBP/Hlp, a well-characterized adhesin, was also able to bind collagen I. Finally, using recombinant fragments of M. leprae LBP/Hlp, we mapped the collagen-binding activity within the C-terminal domain of the adhesin. Since this protein was already shown to be involved in the recognition of laminin and heparan sulphate-containing proteoglycans, the present observations reinforce the adhesive activities of LBP/Hlp, which can be therefore considered as a multifaceted mycobacterial adhesin, playing an important role in both leprosy and tuberculosis pathogenesis.Instituto Oswaldo Cruz, Ministério da Saúde2012-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762012000900025Memórias do Instituto Oswaldo Cruz v.107 suppl.1 2012reponame:Memórias do Instituto Oswaldo Cruzinstname:Fundação Oswaldo Cruzinstacron:FIOCRUZ10.1590/S0074-02762012000900025info:eu-repo/semantics/openAccessDias,André AlvesRaze,DominiqueLima,Cristiana Soares deMarques,Maria Angela de MeloDrobecq,HervéDebrie,Anne-SophieRibeiro-Guimarães,Michelle LopesBiet,FranckPessolani,Maria Cristina Vidaleng2020-04-25T17:51:21Zhttp://www.scielo.br/oai/scielo-oai.php0074-02761678-8060opendoar:null2020-04-26 02:18:45.929Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruztrue |
dc.title.none.fl_str_mv |
Mycobacterial laminin-binding histone-like protein mediates collagen-dependent cytoadherence |
title |
Mycobacterial laminin-binding histone-like protein mediates collagen-dependent cytoadherence |
spellingShingle |
Mycobacterial laminin-binding histone-like protein mediates collagen-dependent cytoadherence Dias,André Alves mycobacteria cytoadherence collagen histone-like protein leprosy tuberculosis |
title_short |
Mycobacterial laminin-binding histone-like protein mediates collagen-dependent cytoadherence |
title_full |
Mycobacterial laminin-binding histone-like protein mediates collagen-dependent cytoadherence |
title_fullStr |
Mycobacterial laminin-binding histone-like protein mediates collagen-dependent cytoadherence |
title_full_unstemmed |
Mycobacterial laminin-binding histone-like protein mediates collagen-dependent cytoadherence |
title_sort |
Mycobacterial laminin-binding histone-like protein mediates collagen-dependent cytoadherence |
author |
Dias,André Alves |
author_facet |
Dias,André Alves Raze,Dominique Lima,Cristiana Soares de Marques,Maria Angela de Melo Drobecq,Hervé Debrie,Anne-Sophie Ribeiro-Guimarães,Michelle Lopes Biet,Franck Pessolani,Maria Cristina Vidal |
author_role |
author |
author2 |
Raze,Dominique Lima,Cristiana Soares de Marques,Maria Angela de Melo Drobecq,Hervé Debrie,Anne-Sophie Ribeiro-Guimarães,Michelle Lopes Biet,Franck Pessolani,Maria Cristina Vidal |
author2_role |
author author author author author author author author |
dc.contributor.author.fl_str_mv |
Dias,André Alves Raze,Dominique Lima,Cristiana Soares de Marques,Maria Angela de Melo Drobecq,Hervé Debrie,Anne-Sophie Ribeiro-Guimarães,Michelle Lopes Biet,Franck Pessolani,Maria Cristina Vidal |
dc.subject.por.fl_str_mv |
mycobacteria cytoadherence collagen histone-like protein leprosy tuberculosis |
topic |
mycobacteria cytoadherence collagen histone-like protein leprosy tuberculosis |
dc.description.none.fl_txt_mv |
When grown in the presence of exogenous collagen I, Mycobacterium bovis BCG was shown to form clumps. Scanning electron microscopy examination of these clumps revealed the presence of collagen fibres cross-linking the bacilli. Since collagen is a major constituent of the eukaryotic extracellular matrices, we assayed BCG cytoadherence in the presence of exogenous collagen I. Collagen increased the interaction of the bacilli with A549 type II pneumocytes or U937 macrophages, suggesting that BCG is able to recruit collagen to facilitate its attachment to host cells. Using an affinity chromatography approach, we have isolated a BCG collagen-binding protein corresponding to the previously described mycobacterial laminin-binding histone-like protein (LBP/Hlp), a highly conserved protein associated with the mycobacterial cell wall. Moreover, Mycobacterium leprae LBP/Hlp, a well-characterized adhesin, was also able to bind collagen I. Finally, using recombinant fragments of M. leprae LBP/Hlp, we mapped the collagen-binding activity within the C-terminal domain of the adhesin. Since this protein was already shown to be involved in the recognition of laminin and heparan sulphate-containing proteoglycans, the present observations reinforce the adhesive activities of LBP/Hlp, which can be therefore considered as a multifaceted mycobacterial adhesin, playing an important role in both leprosy and tuberculosis pathogenesis. |
description |
When grown in the presence of exogenous collagen I, Mycobacterium bovis BCG was shown to form clumps. Scanning electron microscopy examination of these clumps revealed the presence of collagen fibres cross-linking the bacilli. Since collagen is a major constituent of the eukaryotic extracellular matrices, we assayed BCG cytoadherence in the presence of exogenous collagen I. Collagen increased the interaction of the bacilli with A549 type II pneumocytes or U937 macrophages, suggesting that BCG is able to recruit collagen to facilitate its attachment to host cells. Using an affinity chromatography approach, we have isolated a BCG collagen-binding protein corresponding to the previously described mycobacterial laminin-binding histone-like protein (LBP/Hlp), a highly conserved protein associated with the mycobacterial cell wall. Moreover, Mycobacterium leprae LBP/Hlp, a well-characterized adhesin, was also able to bind collagen I. Finally, using recombinant fragments of M. leprae LBP/Hlp, we mapped the collagen-binding activity within the C-terminal domain of the adhesin. Since this protein was already shown to be involved in the recognition of laminin and heparan sulphate-containing proteoglycans, the present observations reinforce the adhesive activities of LBP/Hlp, which can be therefore considered as a multifaceted mycobacterial adhesin, playing an important role in both leprosy and tuberculosis pathogenesis. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-12-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762012000900025 |
url |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762012000900025 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0074-02762012000900025 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Instituto Oswaldo Cruz, Ministério da Saúde |
publisher.none.fl_str_mv |
Instituto Oswaldo Cruz, Ministério da Saúde |
dc.source.none.fl_str_mv |
Memórias do Instituto Oswaldo Cruz v.107 suppl.1 2012 reponame:Memórias do Instituto Oswaldo Cruz instname:Fundação Oswaldo Cruz instacron:FIOCRUZ |
reponame_str |
Memórias do Instituto Oswaldo Cruz |
collection |
Memórias do Instituto Oswaldo Cruz |
instname_str |
Fundação Oswaldo Cruz |
instacron_str |
FIOCRUZ |
institution |
FIOCRUZ |
repository.name.fl_str_mv |
Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruz |
repository.mail.fl_str_mv |
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1669937713033248768 |