{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T16:33:01Z","timestamp":1791304381349,"version":"4.3.1"},"reference-count":41,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[2013,5,1]],"date-time":"2013-05-01T00:00:00Z","timestamp":1367366400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2013,5]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            We have recently reported the ability of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Leptospira<\/jats:named-content>\n            to capture plasminogen (PLG) and generate plasmin (PLA) bound on the microbial surface in the presence of exogenous activators. In this work, we examined the effects of leptospiral PLG binding for active penetration through the endothelial cell barrier and activation. The results indicate that leptospires with PLG association or PLA activation have enhanced migration activity through human umbilical vein endothelial cell (HUVEC) monolayers compared with untreated bacteria.\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Leptospira<\/jats:named-content>\n            cells coated with PLG were capable of stimulating the expression of PLG activators by HUVECs. Moreover, leptospires endowed with PLG or PLA promoted transcriptional upregulation matrix metalloprotease 9 (MMP-9). Serum samples from patients with confirmed leptospirosis showed higher levels of PLG activators and total MMP-9 than serum samples from normal (healthy) subjects. The highest level of PLG activators and total MMP-9 was detected with microscopic agglutination test (MAT)-negative serum samples, suggesting that this proteolytic activity stimulation occurs at the early stage of the disease. Furthermore, a gelatin zymography profile obtained for MMPs with serum samples from patients with leptospirosis appears to be specific to leptospiral infection because serum samples from patients with unrelated infectious diseases produced no similar degradation bands. Altogether, the data suggest that the\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Leptospira<\/jats:named-content>\n            -associated PLG or PLA might represent a mechanism that contributes to bacterial penetration of endothelial cells through an activation cascade of events that enhances the proteolytic capability of the organism. To our knowledge, this is the first proteolytic activity associated with leptospiral pathogenesis described to date.\n          <\/jats:p>","DOI":"10.1128\/iai.00020-13","type":"journal-article","created":{"date-parts":[[2013,3,12]],"date-time":"2013-03-12T00:53:09Z","timestamp":1363049589000},"page":"1764-1774","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":34,"title":["Interaction of Leptospira interrogans with Human Proteolytic Systems Enhances Dissemination through Endothelial Cells and Protease Levels"],"prefix":"10.1128","volume":"81","author":[{"given":"Monica L.","family":"Vieira","sequence":"first","affiliation":[{"name":"Centro de Biotecnologia, Instituto Butantan, S\u00e3o Paulo, SP, Brazil"},{"name":"Interunidades em Biotecnologia, Instituto de Ci\u00eancias Biom\u00e9dicas, USP, S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miryam P.","family":"Alvarez-Flores","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Bioqu\u00edmica e Biof\u00edsica, Instituto Butantan, S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karin","family":"Kirchgatter","sequence":"additional","affiliation":[{"name":"N\u00facleo de Estudos em Mal\u00e1ria, Superintend\u00eancia de Controle de Endemias\u2014SUCEN\/IMT-SP, USP, S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eliete C.","family":"Romero","sequence":"additional","affiliation":[{"name":"Centro de Bacteriologia, Instituto Adolfo Lutz, S\u00e3o Paulo, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ivy J.","family":"Alves","sequence":"additional","affiliation":[{"name":"Centro de Biotecnologia, Instituto Butantan, S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zenaide M.","family":"de Morais","sequence":"additional","affiliation":[{"name":"Laboratorio de Zoonoses Bacterianas do VPS, Faculdade de Medicina Veterin\u00e1ria e Zootecnia, USP, S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Silvio A.","family":"Vasconcellos","sequence":"additional","affiliation":[{"name":"Laboratorio de Zoonoses Bacterianas do VPS, Faculdade de Medicina Veterin\u00e1ria e Zootecnia, USP, S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana M.","family":"Chudzinski-Tavassi","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Bioqu\u00edmica e Biof\u00edsica, Instituto Butantan, S\u00e3o Paulo, SP, Brazil"},{"name":"Programa de P\u00f3s-Gradua\u00e7\u00e3o em Biologia Molecular da UNIFESP, S\u00e3o Paulo, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana L. T. O.","family":"Nascimento","sequence":"additional","affiliation":[{"name":"Centro de Biotecnologia, Instituto Butantan, S\u00e3o Paulo, SP, Brazil"},{"name":"Interunidades em Biotecnologia, Instituto de Ci\u00eancias Biom\u00e9dicas, USP, S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1473-3099(03)00830-2"},{"key":"e_1_3_2_3_2","first-page":"259","volume-title":"Leptospira and leptospirosis","author":"Faine S","year":"1999","unstructured":"FaineSAdlerBBolinCPerolatP. 1999. Leptospira and leptospirosis, 2nd ed, p 259. MediSci, Melbourne, Australia.","edition":"2"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature01597"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1590\/S0100-879X2004000400003"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0603979103"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0001607"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.vetmic.2011.02.055"},{"key":"e_1_3_2_9_2","first-page":"283","article-title":"New insights into the pathogenicity of leptospires: evasion of host defences","volume":"33","author":"Cinco M","year":"2010","unstructured":"CincoM. 2010. New insights into the pathogenicity of leptospires: evasion of host defences. New Microbiol. 33:283\u2013292.","journal-title":"New Microbiol."},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.2217\/fmb.10.102"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.70.12.6926-6932.2002"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0168-6445(01)00067-5"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.63.7.2478-2484.1995"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.00353-09"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0011259"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0021962"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.05583-11"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2180-12-50"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI107470"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.81.20.6413"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.76.11.5674"},{"key":"e_1_3_2_22_2","doi-asserted-by":"publisher","DOI":"10.2174\/1874285800903010069"},{"key":"e_1_3_2_23_2","doi-asserted-by":"publisher","DOI":"10.1006\/meth.2001.1262"},{"key":"e_1_3_2_24_2","doi-asserted-by":"publisher","DOI":"10.1038\/ng1297-439"},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.69.1.456-462.2001"},{"key":"e_1_3_2_26_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1286-4579(00)01280-6"},{"key":"e_1_3_2_27_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.01282-09"},{"key":"e_1_3_2_28_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.micpath.2011.06.008"},{"key":"e_1_3_2_29_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00284-010-9810-3"},{"key":"e_1_3_2_30_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00284-011-9886-4"},{"key":"e_1_3_2_31_2","doi-asserted-by":"publisher","DOI":"10.1002\/9780471729259.mc12e01s00"},{"key":"e_1_3_2_32_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI106927"},{"key":"e_1_3_2_33_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M110.202671"},{"key":"e_1_3_2_34_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0005780"},{"key":"e_1_3_2_35_2","doi-asserted-by":"publisher","DOI":"10.1182\/blood-2010-03-276170"},{"key":"e_1_3_2_36_2","doi-asserted-by":"publisher","DOI":"10.1161\/01.ATV.0000189309.05924.88"},{"key":"e_1_3_2_37_2","doi-asserted-by":"publisher","DOI":"10.1002\/jmv.10438"},{"key":"e_1_3_2_38_2","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.00047-08"},{"key":"e_1_3_2_39_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2249.2005.02840.x"},{"key":"e_1_3_2_40_2","first-page":"4629","article-title":"Effect of plasminogen activator (urokinase), plasmin, and thrombin on glycoprotein and collagenous components of basement membrane","volume":"41","author":"Liotta LA","year":"1981","unstructured":"LiottaLAGoldfarbRHBrundageRSiegalGPTerranovaVGarbisaS. 1981. Effect of plasminogen activator (urokinase), plasmin, and thrombin on glycoprotein and collagenous components of basement membrane. Cancer Res. 41:4629\u20134636.","journal-title":"Cancer Res."},{"key":"e_1_3_2_41_2","doi-asserted-by":"publisher","DOI":"10.1016\/0049-3848(81)90268-1"},{"key":"e_1_3_2_42_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tim.2004.12.003"}],"container-title":["Infection and Immunity"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/IAI.00020-13","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/IAI.00020-13","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,3,4]],"date-time":"2022-03-04T20:14:09Z","timestamp":1646424849000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/IAI.00020-13"}},"subtitle":[],"editor":[{"given":"A.","family":"Camilli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2013,5]]},"references-count":41,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2013,5]]}},"alternative-id":["10.1128\/IAI.00020-13"],"URL":"https:\/\/doi.org\/10.1128\/iai.00020-13","relation":{},"ISSN":["0019-9567","1098-5522"],"issn-type":[{"value":"0019-9567","type":"print"},{"value":"1098-5522","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,5]]},"assertion":[{"value":"2013-01-08","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2013-03-02","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2013-04-15","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}