Identification of a novel protein in the genome sequences of Leptospira interrogans with the ability to interact with host's components

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dc.contributorLEDV - Laboratório de Desenvolvimento de Vacinaspt_BR
dc.contributor.authorRossini, Amanda Diazpt_BR
dc.contributor.authorTeixeira, Aline Rodrigues Florênciopt_BR
dc.contributor.authorSouza Filho, A.pt_BR
dc.contributor.authorSouza, G.O.pt_BR
dc.contributor.authorVasconcellos, S.A.pt_BR
dc.contributor.authorHeinemann, M.B.pt_BR
dc.contributor.authorRomero, E.C.pt_BR
dc.contributor.authorNascimento, Ana Lúcia Tabet Oller dopt_BR
dc.date.accessioned2020-07-09T21:27:03Z-
dc.date.available2020-07-09T21:27:03Z-
dc.date.issued2020pt_BR
dc.identifier.citationRossini AD, Teixeira ARF, Souza Filho A., Souza G.O., Vasconcellos S.A., Heinemann M.B., et al. Identification of a novel protein in the genome sequences of Leptospira interrogans with the ability to interact with host's components. J. Microbiol. Immunol. Infect.. 2020 Feb;53(1):163-175. doi:10.1016/j.jmii.2018.12.012.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2985-
dc.description.abstractBackground Leptospirosis is an infectious disease that affects humans and animals worldwide. The etiological agents of this disease are the pathogenic species of the genus Leptospira. The mechanisms involved in the leptospiral pathogenesis are not full understood. The elucidation of novel mediators of host-pathogen interaction is important in the detection of virulence factors involved in the pathogenesis of leptospirosis. Objective This work focused on identification and characterization of a hypothetical protein of Leptospira encoded by the gene LIC10920. Methods The protein of unknown function was predicted to be surface exposed. Therefore, the LIC10920 gene was cloned and the protein expressed in Escherichia coli BL21 (DE3) Star pLysS strain. The recombinant protein was purified by metal affinity chromatography and evaluated with leptospirosis human serum samples. The interaction with host components was also performed. Results The recombinant protein was recognized by antibodies present in leptopsirosis human serum, suggesting its expression during infection. Immunofluorescence and intact bacteria assays indicated that the bacterial protein is surface-exposed. The recombinant protein interacted with human laminin, in a dose-dependent and saturable manner and was named Lsa24.9, for Leptospiral surface adhesin, followed by its molecular mass. Lsa24.9 also binds plasminogen (PLG) in a dose-dependent and saturable fashion, fulfilling receptor ligand interaction. Moreover, Lsa24.9 has the ability to acquire PLG from normal human serum, exhibiting similar profile as observed with the human purified component. PLG bound Lsa24.9 was able of generating plasmin, which could increase the proteolytic power of the bacteria. Conclusions This novel leptospiral protein may function as an adhesin at the colonization steps and may help the invasion process by plasmin generation at the bacterial cell surface.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.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.format.extent163-175pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofJournal of Microbiology, Immunology and Infectionpt_BR
dc.rightsOpen Accesspt_BR
dc.titleIdentification of a novel protein in the genome sequences of Leptospira interrogans with the ability to interact with host's componentspt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1016/j.jmii.2018.12.012pt_BR
dc.identifier.urlhttps://doi.org/10.1016/j.jmii.2018.12.012pt_BR
dc.contributor.externalUniversidade de São Paulo (USP)¦¦Brasilpt_BR
dc.contributor.externalInstituto Adolfo Lutz (IAL)¦¦Brasilpt_BR
dc.identifier.citationvolume53pt_BR
dc.identifier.citationissue1pt_BR
dc.subject.keywordRecombinant proteinpt_BR
dc.subject.keywordLeptospirapt_BR
dc.subject.keywordLamininpt_BR
dc.subject.keywordPlasminogenpt_BR
dc.subject.keywordHost-pathogen interactionpt_BR
dc.relation.ispartofabbreviatedJ Microbiol Immunol Infectpt_BR
dc.identifier.citationabntv. 53, n. 1, p. 163-175, fev. 2020pt_BR
dc.identifier.citationvancouver2020 Feb;53(1):163-175pt_BR
dc.contributor.butantanRossini, Amanda Diaz|:Aluno|:LEDV - Laboratório de Desenvolvimento de Vacinas|:PrimeiroAutorpt_BR
dc.contributor.butantanTeixeira, Aline Rodrigues Florêncio|:Aluno|:LEDV - Laboratório de Desenvolvimento de Vacinas|:pt_BR
dc.contributor.butantanNascimento, Ana Lúcia Tabet Oller do|:Pesquisador|:LEDV - Laboratório de Desenvolvimento de Vacinas|:pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦302758/2013-5pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦441449/2014-0pt_BR
dc.sponsorship.butantanCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)¦¦pt_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)¦¦2016/11541 0pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
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