Cloning, expression and characterisation of an HtrA-like serine protease produced in vivo by Mycobacterium leprae
Autor(a) principal: | |
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Data de Publicação: | 2009 |
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=S0074-02762009000800010 |
Resumo: | Members of the high temperature requirement A (HtrA) family of chaperone proteases have been shown to play a role in bacterial pathogenesis. In a recent report, we demonstrated that the gene ML0176, which codes for a predicted HtrA-like protease, a gene conserved in other species of mycobacteria, is transcribed by Mycobacterium leprae in human leprosy lesions. In the present study, the recombinant ML0176 protein was produced and its enzymatic properties investigated. M. lepraerecombinant ML0176 was able to hydrolyse a variety of synthetic and natural peptides. Similar to other HtrA proteins, this enzyme displayed maximum proteolytic activity at temperatures above 40°C and was completely inactivated by aprotinin, a protease inhibitor with high selectivity for serine proteases. Finally, analysis of M. leprae ML0176 specificity suggested a broader cleavage preference than that of previously described HtrAs homologues. In summary, we have identified an HtrA-like protease in M. lepraethat may constitute a potential new target for the development of novel prophylactic and/or therapeutic strategies against mycobacterial infections. |
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Memórias do Instituto Oswaldo Cruz |
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Cloning, expression and characterisation of an HtrA-like serine protease produced in vivo by Mycobacterium lepraeMycobacterium lepraeHtrA2proteaseenzymatic activityFRET peptidespathogenesisMembers of the high temperature requirement A (HtrA) family of chaperone proteases have been shown to play a role in bacterial pathogenesis. In a recent report, we demonstrated that the gene ML0176, which codes for a predicted HtrA-like protease, a gene conserved in other species of mycobacteria, is transcribed by Mycobacterium leprae in human leprosy lesions. In the present study, the recombinant ML0176 protein was produced and its enzymatic properties investigated. M. lepraerecombinant ML0176 was able to hydrolyse a variety of synthetic and natural peptides. Similar to other HtrA proteins, this enzyme displayed maximum proteolytic activity at temperatures above 40°C and was completely inactivated by aprotinin, a protease inhibitor with high selectivity for serine proteases. Finally, analysis of M. leprae ML0176 specificity suggested a broader cleavage preference than that of previously described HtrAs homologues. In summary, we have identified an HtrA-like protease in M. lepraethat may constitute a potential new target for the development of novel prophylactic and/or therapeutic strategies against mycobacterial infections.Instituto Oswaldo Cruz, Ministério da Saúde2009-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762009000800010Memórias do Instituto Oswaldo Cruz v.104 n.8 2009reponame:Memórias do Instituto Oswaldo Cruzinstname:Fundação Oswaldo Cruzinstacron:FIOCRUZ10.1590/S0074-02762009000800010info:eu-repo/semantics/openAccessRibeiro-Guimarães,Michelle LopesMarengo,Eliana BliniTempone,Antonio JorgeAmaral,Julio JablonskiKlitzke,Clécio FSilveira,Erika K Xavier daPortaro,Fernanda Calheta VieiraPessolani,Maria Cristina Vidaleng2020-04-25T17:50:34Zhttp://www.scielo.br/oai/scielo-oai.php0074-02761678-8060opendoar:null2020-04-26 02:16:33.348Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruztrue |
dc.title.none.fl_str_mv |
Cloning, expression and characterisation of an HtrA-like serine protease produced in vivo by Mycobacterium leprae |
title |
Cloning, expression and characterisation of an HtrA-like serine protease produced in vivo by Mycobacterium leprae |
spellingShingle |
Cloning, expression and characterisation of an HtrA-like serine protease produced in vivo by Mycobacterium leprae Ribeiro-Guimarães,Michelle Lopes Mycobacterium leprae HtrA2 protease enzymatic activity FRET peptides pathogenesis |
title_short |
Cloning, expression and characterisation of an HtrA-like serine protease produced in vivo by Mycobacterium leprae |
title_full |
Cloning, expression and characterisation of an HtrA-like serine protease produced in vivo by Mycobacterium leprae |
title_fullStr |
Cloning, expression and characterisation of an HtrA-like serine protease produced in vivo by Mycobacterium leprae |
title_full_unstemmed |
Cloning, expression and characterisation of an HtrA-like serine protease produced in vivo by Mycobacterium leprae |
title_sort |
Cloning, expression and characterisation of an HtrA-like serine protease produced in vivo by Mycobacterium leprae |
author |
Ribeiro-Guimarães,Michelle Lopes |
author_facet |
Ribeiro-Guimarães,Michelle Lopes Marengo,Eliana Blini Tempone,Antonio Jorge Amaral,Julio Jablonski Klitzke,Clécio F Silveira,Erika K Xavier da Portaro,Fernanda Calheta Vieira Pessolani,Maria Cristina Vidal |
author_role |
author |
author2 |
Marengo,Eliana Blini Tempone,Antonio Jorge Amaral,Julio Jablonski Klitzke,Clécio F Silveira,Erika K Xavier da Portaro,Fernanda Calheta Vieira Pessolani,Maria Cristina Vidal |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
Ribeiro-Guimarães,Michelle Lopes Marengo,Eliana Blini Tempone,Antonio Jorge Amaral,Julio Jablonski Klitzke,Clécio F Silveira,Erika K Xavier da Portaro,Fernanda Calheta Vieira Pessolani,Maria Cristina Vidal |
dc.subject.por.fl_str_mv |
Mycobacterium leprae HtrA2 protease enzymatic activity FRET peptides pathogenesis |
topic |
Mycobacterium leprae HtrA2 protease enzymatic activity FRET peptides pathogenesis |
dc.description.none.fl_txt_mv |
Members of the high temperature requirement A (HtrA) family of chaperone proteases have been shown to play a role in bacterial pathogenesis. In a recent report, we demonstrated that the gene ML0176, which codes for a predicted HtrA-like protease, a gene conserved in other species of mycobacteria, is transcribed by Mycobacterium leprae in human leprosy lesions. In the present study, the recombinant ML0176 protein was produced and its enzymatic properties investigated. M. lepraerecombinant ML0176 was able to hydrolyse a variety of synthetic and natural peptides. Similar to other HtrA proteins, this enzyme displayed maximum proteolytic activity at temperatures above 40°C and was completely inactivated by aprotinin, a protease inhibitor with high selectivity for serine proteases. Finally, analysis of M. leprae ML0176 specificity suggested a broader cleavage preference than that of previously described HtrAs homologues. In summary, we have identified an HtrA-like protease in M. lepraethat may constitute a potential new target for the development of novel prophylactic and/or therapeutic strategies against mycobacterial infections. |
description |
Members of the high temperature requirement A (HtrA) family of chaperone proteases have been shown to play a role in bacterial pathogenesis. In a recent report, we demonstrated that the gene ML0176, which codes for a predicted HtrA-like protease, a gene conserved in other species of mycobacteria, is transcribed by Mycobacterium leprae in human leprosy lesions. In the present study, the recombinant ML0176 protein was produced and its enzymatic properties investigated. M. lepraerecombinant ML0176 was able to hydrolyse a variety of synthetic and natural peptides. Similar to other HtrA proteins, this enzyme displayed maximum proteolytic activity at temperatures above 40°C and was completely inactivated by aprotinin, a protease inhibitor with high selectivity for serine proteases. Finally, analysis of M. leprae ML0176 specificity suggested a broader cleavage preference than that of previously described HtrAs homologues. In summary, we have identified an HtrA-like protease in M. lepraethat may constitute a potential new target for the development of novel prophylactic and/or therapeutic strategies against mycobacterial infections. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-12-01 |
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=S0074-02762009000800010 |
url |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762009000800010 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0074-02762009000800010 |
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.104 n.8 2009 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 |
|
_version_ |
1669937706741792768 |