Surface protein dispersin of enteroaggregative escherichia coli binds plasminogen that Is converted Into active plasmin

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dc.contributorLab. Bacteriologiapt_BR
dc.contributorLab. Biofísicapt_BR
dc.contributorLETA - Laboratório de Toxinologia Aplicadapt_BR
dc.contributorCentro de Toxinas, Resposta-imune e Sinalização Celular (CeTICS)pt_BR
dc.contributor.authorMoraes, Claudia Trigo Pedroso dept_BR
dc.contributor.authorLongo, Jonathanpt_BR
dc.contributor.authorSilva, Ludmila Bezerra dapt_BR
dc.contributor.authorPimenta, Daniel Carvalhopt_BR
dc.contributor.authorCarvalho, Eneaspt_BR
dc.contributor.authorMorone, Mariana Salgado Loureiro de Caldaspt_BR
dc.contributor.authorRós, Nancy dapt_BR
dc.contributor.authorSerrano, Solange Maria de Toledopt_BR
dc.contributor.authorSantos, Ana Carolina M.pt_BR
dc.contributor.authorPiazza, Roxane Maria Fontespt_BR
dc.contributor.authorBarbosa, Angela Silvapt_BR
dc.contributor.authorElias, Waldir Pereirapt_BR
dc.date.accessioned2020-08-03T13:33:12Z-
dc.date.available2020-08-03T13:33:12Z-
dc.date.issued2020pt_BR
dc.identifier.citationMoraes CTP, Longo J, Silva LB, Pimenta DC, Carvalho E, Morone MSLC, et al. Surface protein dispersin of enteroaggregative escherichia coli binds plasminogen that Is converted Into active plasmin. Front. Microbiol.. 2020 June;11:1222. doi:10.3389/fmicb.2020.01222.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/3092-
dc.description.abstractDispersin is a 10.2 kDa-immunogenic protein secreted by enteroaggregative Escherichia coli (EAEC). In the prototypical EAEC strain 042, dispersin is non-covalently bound to the outer membrane, assisting dispersion across the intestinal mucosa by overcoming electrostatic attraction between the AAF/II fimbriae and the bacterial surface. Also, dispersin facilitates penetration of the intestinal mucus layer. Initially characterized in EAEC, dispersin has been detected in other E. coli pathotypes, including those isolated from extraintestinal sites. In this study we investigated the binding capacity of purified dispersin to extracellular matrix (ECM), since dispersin is exposed on the bacterial surface and is involved in intestinal colonization. Binding to plasminogen was also investigated due to the presence of conserved carboxy-terminal lysine residues in dispersin sequences, which are involved in plasminogen binding in several bacterial proteins. Moreover, some E. coli components can interact with this host protease, as well as with tissue plasminogen activator, leading to plasmin production. Recombinant dispersin was produced and used in binding assays with ECM molecules and coagulation cascade compounds. Purified dispersin bound specifically to laminin and plasminogen. Interaction with plasminogen occurred in a dose-dependent and saturable manner. In the presence of plasminogen activator, bound plasminogen was converted into plasmin, its active form, leading to fibrinogen and vitronectin cleavage. A collection of E. coli strains isolated from human bacteremia was screened for the presence of aap, the dispersin-encoding gene. Eight aap-positive strains were detected and dispersin production could be observed in four of them. Our data describe new attributes for dispersin and points out to possible roles in mechanisms of tissue adhesion and dissemination, considering the binding capacity to laminin, and the generation of dispersin-bound plasmin(ogen), which may facilitate E. coli spread from the colonization site to other tissues and organs. The cleavage of fibrinogen in the bloodstream, may also contribute to the pathogenesis of sepsis caused by dispersin-producing E. coli.pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipFinanciadora de Estudos e Projetos (FINEP)pt_BR
dc.format.extent1222pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofFrontiers in Microbiologypt_BR
dc.rightsOpen Accesspt_BR
dc.titleSurface protein dispersin of enteroaggregative escherichia coli binds plasminogen that Is converted Into active plasminpt_BR
dc.typeArticlept_BR
dc.identifier.doi10.3389/fmicb.2020.01222pt_BR
dc.identifier.urlhttps://doi.org/10.3389/fmicb.2020.01222pt_BR
dc.contributor.externalUniversidade Federal de São Paulo (UNIFESP)pt_BR
dc.identifier.citationvolume11pt_BR
dc.subject.keywordEAECpt_BR
dc.subject.keyworddispersinpt_BR
dc.subject.keywordplasminogenpt_BR
dc.subject.keywordplasminpt_BR
dc.subject.keywordECMpt_BR
dc.relation.ispartofabbreviatedFront Microbiolpt_BR
dc.identifier.citationabntv. 11, 1222, jun. 2020pt_BR
dc.identifier.citationvancouver2020 June;11:1222pt_BR
dc.contributor.butantanMoraes, Claudia Trigo Pedroso de|:Técnico|:Lab. Bacteriologia|:PrimeiroAutorpt_BR
dc.contributor.butantanLongo, Jonathan|:Aluno|:Lab. Bacteriologiapt_BR
dc.contributor.butantanSilva, Ludmila Bezerra da|:Aluno|:Lab. Bacteriologiapt_BR
dc.contributor.butantanPimenta, Daniel Carvalho|:Pesquisador:Docente Permanente PPGTOX|:Lab. Biofísicapt_BR
dc.contributor.butantanCarvalho, Eneas|:Pesquisador|:Lab. Bacteriologiapt_BR
dc.contributor.butantanMorone, Mariana Salgado Loureiro de Caldas|:Técnico|:Laboratório Especial de Toxinologia Aplicada (LETA):Centro de Toxinas, Resposta-imune e Sinalização Celular (CeTICS)pt_BR
dc.contributor.butantanRós, Nancy da|:Técnico|:Laboratório Especial de Toxinologia Aplicada (LETA):Centro de Toxinas, Resposta-imune e Sinalização Celular (CeTICS)pt_BR
dc.contributor.butantanSerrano, Solange Maria de Toledo|:Pesquisador:Docente Permanente PPGTOX|:Laboratório Especial de Toxinologia Aplicada (LETA):Centro de Toxinas, Resposta-imune e Sinalização Celular (CeTICS)pt_BR
dc.contributor.butantanPiazza, Roxane Maria Fontes:Docente Permanente PPGTOX|:Pesquisador|:Lab. Bacteriologiapt_BR
dc.contributor.butantanBarbosa, Angela Silva|:Pesquisador|:Lab. Bacteriologia|:Autor de correspondênciapt_BR
dc.contributor.butantanElias, Waldir Pereira|:Pesquisador|:Lab. Bacteriologia|:Autor de correspondênciapt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦72097/2009-1pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦303792/2016-7pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2018/06610-9pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2016/18583-0pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2013/17419-4pt_BR
dc.sponsorship.butantanFinanciadora de Estudos e Projetos (FINEP)¦¦01.09.0278.04pt_BR
dc.sponsorship.butantanFinanciadora de Estudos e Projetos (FINEP)¦¦01.12.0450.03pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
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