Leptospira interrogans secreted proteases degrade extracellular matrix and plasma proteins from the host

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dc.contributorLab. Bacteriologiapt_BR
dc.contributorLETA - Laboratório de Toxinologia Aplicadapt_BR
dc.contributor.authorSilva, Ludmila Bezerra dapt_BR
dc.contributor.authorMenezes, Milene Cristinapt_BR
dc.contributor.authorKitano, Eduardo Shigueopt_BR
dc.contributor.authorOliveira, Ana K.pt_BR
dc.contributor.authorAbreu, Afonso G.pt_BR
dc.contributor.authorSouza, Gisele O. dept_BR
dc.contributor.authorHeinemann, Marcos B.pt_BR
dc.contributor.authorIsaac, Lourdespt_BR
dc.contributor.authorFraga, Tatiana R.pt_BR
dc.contributor.authorSerrano, Solange Maria de Toledopt_BR
dc.contributor.authorBarbosa, Angela Silvapt_BR
dc.date.accessioned2020-07-09T21:19:09Z-
dc.date.available2020-07-09T21:19:09Z-
dc.date.issued2018pt_BR
dc.identifier.citationSilva LB, Menezes MC, Kitano ES, Oliveira AK., Abreu AG., Souza GO., et al. Leptospira interrogans secreted proteases degrade extracellular matrix and plasma proteins from the host. Front Cell Infect Microbiol. 2018 Mar;8:92. doi:10.3389/fcimb.2018.00092.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2400-
dc.description.abstractLeptospires are highly motile spirochetes equipped with strategies for efficient invasion and dissemination within the host. Our group previously demonstrated that pathogenic leptospires secrete proteases capable of cleaving and inactivating key molecules of the complement system, allowing these bacteria to circumvent host's innate immune defense mechanisms. Given the successful dissemination of leptospires during infection, we wondered if such proteases would target a broader range of host molecules. In the present study, the proteolytic activity of secreted leptospiral proteases against a panel of extracellular matrix (ECM) and plasma proteins was assessed. The culture supernatant of the virulent L. interrogans serovar Kennewicki strain Fromm (LPF) degraded human fibrinogen, plasma fibronectin, gelatin, and the proteoglycans decorin, biglycan, and lumican. Interestingly, human plasminogen was not cleaved by proteases present in the supernatants. Proteolytic activity was inhibited by 1,10-phenanthroline, suggesting the participation of metalloproteases. Moreover, production of proteases might be an important virulence determinant since culture-attenuated or saprophytic Leptospira did not display proteolytic activity against ECM or plasma components. Exoproteomic analysis allowed the identification of three metalloproteases that could be involved in the degradation of host components. The ability to cleave conjunctive tissue molecules and coagulation cascade proteins may certainly contribute to invasion and tissue destruction observed upon infection with Leptospira.pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.format.extent92pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofFrontiers in Cellular and Infection Microbiologypt_BR
dc.rightsOpen Accesspt_BR
dc.titleLeptospira interrogans secreted proteases degrade extracellular matrix and plasma proteins from the hostpt_BR
dc.typeArticlept_BR
dc.identifier.doi10.3389/fcimb.2018.00092pt_BR
dc.identifier.urlhttp://dx.doi.org/10.3389/fcimb.2018.00092pt_BR
dc.contributor.externalLaboratório Nacional de Biociências (LNBio)¦¦Brasilpt_BR
dc.contributor.externalUniversidade Ceuma¦¦Brasilpt_BR
dc.contributor.externalUniversidade Federal do Maranhão (UFMA)¦¦Brasilpt_BR
dc.contributor.externalUniversidade de São Paulo (USP)¦¦Brasilpt_BR
dc.identifier.citationvolume8pt_BR
dc.subject.keywordLeptospirapt_BR
dc.subject.keywordsecreted proteinspt_BR
dc.subject.keywordextracellular matrixpt_BR
dc.subject.keywordplasma proteinspt_BR
dc.subject.keywordhost invasionpt_BR
dc.relation.ispartofabbreviatedFront Cell Infect Microbiolpt_BR
dc.identifier.citationabntv. 8, 92, mar. 2018pt_BR
dc.identifier.citationvancouver2018 Mar;8:92pt_BR
dc.contributor.butantanKitano, Eduardo Shigueo|:Aluno|:Laboratório Especial de Toxinologia Aplicada (LETA)|:pt_BR
dc.contributor.butantanSerrano, Solange Maria de Toledo|:Pesquisador|:Docente Permanente PPGTOX|:Laboratório Especial de Toxinologia Aplicada (LETA)|:pt_BR
dc.contributor.butantanSilva, Ludmila Bezerra da|:Aluno|:Lab. Bacteriologia|:PrimeiroAutorpt_BR
dc.contributor.butantanMenezes, Milene Cristina|:|:Laboratório Especial de Toxinologia Aplicada (LETA):Laboratório Especial de Toxinologia Aplicada (LETA)|:pt_BR
dc.contributor.butantanBarbosa, Angela Silva|:Pesquisador|:Lab. Bacteriologiapt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2014/00926-3pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2013/17419-4pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
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item.languageiso639-1English-
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