The interaction of two novel putative proteins of Leptospira interrogans with E-cadherin, plasminogen and complement components with potential role in bacterial infection

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dc.contributorLEDV - Laboratório de Desenvolvimento de Vacinaspt_BR
dc.contributor.authorKochi, Leandro Toshiopt_BR
dc.contributor.authorFernandes, Luis Guilherme Vírgíliopt_BR
dc.contributor.authorSouza, Gisele O.pt_BR
dc.contributor.authorVasconcellos, Silvio A.pt_BR
dc.contributor.authorHeinemann, Marcos B.pt_BR
dc.contributor.authorRomero, Eliete C.pt_BR
dc.contributor.authorKirchgatter, Karinpt_BR
dc.contributor.authorNascimento, Ana Lúcia Tabet Oller dopt_BR
dc.date.accessioned2020-07-09T21:24:52Z-
dc.date.available2020-07-09T21:24:52Z-
dc.date.issued2019pt_BR
dc.identifier.citationKochi LT, Fernandes LGV, Souza GO., Vasconcellos SA., Heinemann MB., Romero EC., et al. The interaction of two novel putative proteins of Leptospira interrogans with E-cadherin, plasminogen and complement components with potential role in bacterial infection. Virulence. 2019 Aug; 10(1):734-753. doi:10.1080/21505594.2019.1650613.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2815-
dc.description.abstractLeptospirosis is a worldwide zoonosis caused by pathogenic species of Leptospira. Leptospires are able to adhere to exposed extracellular matrix in injured tissues and, once in the bloodstream, can survive the attack of the immune system and spread to colonize target organs. In this work, we report that two novel putative proteins, coded by the genes LIC11711 and LIC12587 of L. interrogans serovar Copenhageni are conserved among pathogenic strains, and probably exposed in the bacterial surface. Soluble recombinant proteins were expressed in Escherichia coli, purified and characterized. Both recombinant proteins bound to laminin and E-cadherin, suggesting an initial adhesion function in host epithelial cells. The recombinant protein LIC11711 (rLIC11711) was able to capture plasminogen (PLG) from normal human serum and convert to enzymatically active plasmin (PLA), in the presence of PLG activator. rLIC12587 (recombinant protein LIC12587) displayed a dose dependent and saturable interaction with components C7, C8, and C9 of the complement system, reducing the bactericidal effect of the complement. Binding to C9 may have consequences such as C9 polymerization inhibition, interfering with the membrane attack complex formation. Blocking LIC11711 and LIC12587 on bacterial cells by the respective antiserum reduced leptospiral cell viability when exposed to normal human serum (NHS). Both recombinant proteins could be recognized by serum samples of confirmed leptospirosis, but not of unrelated diseases, suggesting that the native proteins are immunogenic and expressed during leptospirosis. Taken together, our data suggest that these proteins may have a role in leptospiral pathogenesis, participating in immune evasion strategies.pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.format.extent734-753pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofVirulencept_BR
dc.rightsOpen Accesspt_BR
dc.titleThe interaction of two novel putative proteins of Leptospira interrogans with E-cadherin, plasminogen and complement components with potential role in bacterial infectionpt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1080/21505594.2019.1650613pt_BR
dc.identifier.urlhttps://doi.org/10.1080/21505594.2019.1650613pt_BR
dc.contributor.externalUniversidade de São Paulo (USP)¦¦Brasilpt_BR
dc.contributor.externalInstituto Adolfo Lutz (IAL)¦¦Brasilpt_BR
dc.identifier.citationvolume10pt_BR
dc.identifier.citationissue1pt_BR
dc.subject.keywordLeptospirapt_BR
dc.subject.keywordleptospirosispt_BR
dc.subject.keywordrecombinant proteinspt_BR
dc.subject.keywordadhesionpt_BR
dc.subject.keywordimmune evasionpt_BR
dc.relation.ispartofabbreviatedVirulencept_BR
dc.identifier.citationabntv. 10, n. 1, p. 734-753, aug. 2019pt_BR
dc.identifier.citationvancouver2019 Aug; 10(1):734-753pt_BR
dc.contributor.butantanKochi, Leandro Toshio|:Aluno|:LEDV - Laboratório de Desenvolvimento de Vacinas|:PrimeiroAutorpt_BR
dc.contributor.butantanFernandes, Luis Guilherme Virgílio|:Aluno|:LEDV - Laboratório de Desenvolvimento de Vacinas|:pt_BR
dc.contributor.butantanNascimento, Ana Lúcia Tabet Oller do|:Pesquisador|:LEDV - Laboratório de Desenvolvimento de Vacinas|:Autor de correspondênciapt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦301229/2017-1pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦14/50981-0pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2016/01384-5pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2017/06731-8pt_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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