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DC Field | Value | Language |
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dc.contributor | Sistema FMUSP-HC: Faculdade de Medicina da Universidade de São Paulo (FMUSP) e Hospital das Clínicas da FMUSP | |
dc.contributor.author | KOCHI, Leandro T. | |
dc.contributor.author | V, Luis G. Fernandes | |
dc.contributor.author | SOUZA, Gisele O. | |
dc.contributor.author | VASCONCELLOS, Silvio A. | |
dc.contributor.author | HEINEMANN, Marcos B. | |
dc.contributor.author | ROMERO, Eliete C. | |
dc.contributor.author | KIRCHGATTER, Karin | |
dc.contributor.author | NASCIMENTO, Ana L. T. O. | |
dc.date.accessioned | 2019-09-23T14:26:51Z | - |
dc.date.available | 2019-09-23T14:26:51Z | - |
dc.date.issued | 2019 | |
dc.identifier.citation | VIRULENCE, v.10, n.1, p.734-753, 2019 | |
dc.identifier.issn | 2150-5594 | |
dc.identifier.uri | https://observatorio.fm.usp.br/handle/OPI/33665 | - |
dc.description.abstract | Leptospirosis 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. | eng |
dc.description.sponsorship | Fundacao de Amparo a Pesquisa do Estado Sao Paulo - FAPESP [14/50981-0] | |
dc.description.sponsorship | Conselho Nacional de Desenvolvimento Cientifico e Tecnologico - CNPq [301229/2017-1] | |
dc.description.sponsorship | Fundacao Butantan | |
dc.description.sponsorship | FAPESP [2016/01384-5, 2017/06731-8] | |
dc.language.iso | eng | |
dc.publisher | TAYLOR & FRANCIS INC | eng |
dc.relation.ispartof | Virulence | |
dc.rights | openAccess | eng |
dc.subject | Leptospira | eng |
dc.subject | leptospirosis | eng |
dc.subject | recombinant proteins | eng |
dc.subject | adhesion | eng |
dc.subject | immune evasion | eng |
dc.subject.other | secondary structure prediction | eng |
dc.subject.other | extracellular-matrix | eng |
dc.subject.other | immune-response | eng |
dc.subject.other | outer-membrane | eng |
dc.subject.other | binds laminin | eng |
dc.subject.other | activation | eng |
dc.subject.other | adhesin | eng |
dc.subject.other | surface | eng |
dc.subject.other | serum | eng |
dc.subject.other | attachment | eng |
dc.title | The interaction of two novel putative proteins of Leptospira interrogans with E-cadherin, plasminogen and complement components with potential role in bacterial infection | eng |
dc.type | article | eng |
dc.rights.holder | Copyright TAYLOR & FRANCIS INC | eng |
dc.identifier.doi | 10.1080/21505594.2019.1650613 | |
dc.identifier.pmid | 31422744 | |
dc.subject.wos | Immunology | eng |
dc.subject.wos | Infectious Diseases | eng |
dc.subject.wos | Microbiology | eng |
dc.type.category | original article | eng |
dc.type.version | publishedVersion | eng |
hcfmusp.author.external | KOCHI, Leandro T.:Inst Butantan, Lab Especial Desenvolvimento Vacinas, Sao Paulo, Brazil; Inst Ciencias Biomed, Programa Posgrad Interunidades Biotecnol, Sao Paulo, Brazil | |
hcfmusp.author.external | V, Luis G. Fernandes:Inst Butantan, Lab Especial Desenvolvimento Vacinas, Sao Paulo, Brazil | |
hcfmusp.author.external | SOUZA, Gisele O.:Fac Med Vet & Zootecnia, Lab Zoonoses Bacterianas, Sao Paulo, Brazil | |
hcfmusp.author.external | VASCONCELLOS, Silvio A.:Fac Med Vet & Zootecnia, Lab Zoonoses Bacterianas, Sao Paulo, Brazil | |
hcfmusp.author.external | HEINEMANN, Marcos B.:Fac Med Vet & Zootecnia, Lab Zoonoses Bacterianas, Sao Paulo, Brazil | |
hcfmusp.author.external | ROMERO, Eliete C.:Adolfo Lutz Inst, Ctr Bacteriol, Sao Paulo, Brazil | |
hcfmusp.author.external | NASCIMENTO, Ana L. T. O.:Inst Butantan, Lab Especial Desenvolvimento Vacinas, Sao Paulo, Brazil | |
hcfmusp.description.beginpage | 734 | |
hcfmusp.description.endpage | 753 | |
hcfmusp.description.issue | 1 | |
hcfmusp.description.volume | 10 | |
hcfmusp.origem | WOS | |
hcfmusp.origem.id | WOS:000481739900001 | |
hcfmusp.origem.id | 2-s2.0-85070969718 | |
hcfmusp.publisher.city | PHILADELPHIA | eng |
hcfmusp.publisher.country | USA | eng |
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dc.description.index | MEDLINE | eng |
dc.identifier.eissn | 2150-5608 | |
hcfmusp.citation.scopus | 24 | - |
hcfmusp.scopus.lastupdate | 2024-02-23 | - |
Appears in Collections: | Artigos e Materiais de Revistas Científicas - IMT Artigos e Materiais de Revistas Científicas - LIM/49 |
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art_KOCHI_The_interaction_of_two_novel_putative_proteins_of_2019.PDF | publishedVersion (English) | 6.12 MB | Adobe PDF | View/Open |
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