{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T17:27:11Z","timestamp":1790270831242,"version":"4.1.0"},"reference-count":29,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["131434\/2018-7"],"award-info":[{"award-number":["131434\/2018-7"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","doi-asserted-by":"publisher","award":["2018\/12896-2"],"award-info":[{"award-number":["2018\/12896-2"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Microbial Pathogenesis"],"published-print":{"date-parts":[[2021,1]]},"DOI":"10.1016\/j.micpath.2020.104704","type":"journal-article","created":{"date-parts":[[2020,12,24]],"date-time":"2020-12-24T07:19:59Z","timestamp":1608794399000},"page":"104704","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"special_numbering":"C","title":["Inactivation of the antimicrobial peptide LL-37 by pathogenic Leptospira"],"prefix":"10.1016","volume":"150","author":[{"given":"Priscila N.","family":"Oliveira","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4448-5903","authenticated-orcid":false,"given":"Daniella S.","family":"Courrol","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rosa Maria","family":"Chura-Chambi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ligia","family":"Morganti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gisele O.","family":"Souza","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcia R.","family":"Franzolin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5239-8511","authenticated-orcid":false,"suffix":"Jr.","given":"Elsio A.","family":"Wunder","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcos B.","family":"Heinemann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Angela S.","family":"Barbosa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"5","key":"10.1016\/j.micpath.2020.104704_bib1","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0007270","article-title":"Revisiting the taxonomy and evolution of pathogenicity of the genus Leptospira through the prism of genomics. Martins EAL, org","volume":"13","author":"Vincent","year":"2019","journal-title":"PLoS Neglected Trop. Dis."},{"issue":"9","key":"10.1016\/j.micpath.2020.104704_bib2","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0003898","article-title":"Global morbidity and mortality of leptospirosis: a systematic review","volume":"9","author":"Costa","year":"2015","journal-title":"PLoS Neglected Trop. Dis."},{"issue":"3","key":"10.1016\/j.micpath.2020.104704_bib3","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1111\/mmi.13403","article-title":"A novel flagellar sheath protein, FcpA, determines filament coiling, translational motility and virulence for the Leptospira spirochete","volume":"101","author":"Wunder","year":"2016","journal-title":"Mol. Microbiol."},{"issue":"4","key":"10.1016\/j.micpath.2020.104704_bib4","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/j.micpath.2005.07.003","article-title":"Regulation of complement activation at the C3-level by serum resistant leptospires","volume":"39","author":"Meri","year":"2005","journal-title":"Microb. Pathog."},{"issue":"3","key":"10.1016\/j.micpath.2020.104704_bib5","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1128\/IAI.01310-08","article-title":"Immune evasion of Leptospira species by acquisition of human complement regulator C4BP","volume":"77","author":"Barbosa","year":"2009","journal-title":"Infect. Immun."},{"issue":"6","key":"10.1016\/j.micpath.2020.104704_bib6","doi-asserted-by":"crossref","first-page":"876","DOI":"10.1093\/infdis\/jit569","article-title":"Immune evasion by pathogenic Leptospira strains: the secretion of proteases that directly cleave complement proteins","volume":"209","author":"Fraga","year":"2014","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.micpath.2020.104704_bib7","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2017.00958","article-title":"Pathogenic Leptospira secreted proteases target the membrane attack complex: a potential role for thermolysin in complement inhibition","volume":"8","author":"Amamura","year":"2017","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.micpath.2020.104704_bib8","doi-asserted-by":"crossref","DOI":"10.3389\/fcimb.2018.00092","article-title":"Leptospira interrogans secreted proteases degrade extracellular matrix and plasma proteins from the host","volume":"8","author":"da Silva","year":"2018","journal-title":"Front. Cell. Infect. Microbiol."},{"issue":"6","key":"10.1016\/j.micpath.2020.104704_bib9","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/S0045-2068(03)00080-4","article-title":"Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance","volume":"31","author":"Shinnar","year":"2003","journal-title":"Bioorg. Chem."},{"issue":"3","key":"10.1016\/j.micpath.2020.104704_bib10","first-page":"549","article-title":"Bacterial evasion of host antimicrobial peptide defenses","volume":"47","author":"Cole","year":"2016","journal-title":"Microbiol. Spectr."},{"issue":"6862","key":"10.1016\/j.micpath.2020.104704_bib11","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1038\/35106587","article-title":"Innate antimicrobial peptide protects the skin from invasive bacterial infection","volume":"414","author":"Nizet","year":"2001","journal-title":"Nature"},{"issue":"3","key":"10.1016\/j.micpath.2020.104704_bib12","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1038\/nrmicro1098","article-title":"Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?","volume":"3","author":"Brogden","year":"2005","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.micpath.2020.104704_bib13","first-page":"173","article-title":"hCAP-18 , a cathelin\/pro-bactenecin-like protein of human neutrophil specific granules","volume":"368","author":"Cowland","year":"1995"},{"issue":"7","key":"10.1016\/j.micpath.2020.104704_bib14","doi-asserted-by":"crossref","first-page":"2796","DOI":"10.1182\/blood.V90.7.2796","article-title":"The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils","volume":"90","author":"S\u00f8rensen","year":"1997","journal-title":"Blood"},{"issue":"9","key":"10.1016\/j.micpath.2020.104704_bib15","doi-asserted-by":"crossref","first-page":"3086","DOI":"10.1182\/blood.V96.9.3086","article-title":"The human antimicrobial and chemotactic peptides LL-37 and \u03b1-defensins are expressed by specific lymphocyte and monocyte populations","volume":"96","author":"Agerberth","year":"2000","journal-title":"Blood"},{"issue":"5","key":"10.1016\/j.micpath.2020.104704_bib16","doi-asserted-by":"crossref","first-page":"2274","DOI":"10.4049\/jimmunol.170.5.2274","article-title":"Cutting edge: mast cell antimicrobial activity is mediated by expression of cathelicidin antimicrobial peptide","volume":"170","author":"Di Nardo","year":"2003","journal-title":"J. Immunol."},{"issue":"2","key":"10.1016\/j.micpath.2020.104704_bib17","first-page":"179","article-title":"The role of cathelicidins in the innate host defenses of mammals","volume":"7","author":"Zanetti","year":"2005","journal-title":"Curr. Issues Mol. Biol."},{"issue":"12","key":"10.1016\/j.micpath.2020.104704_bib18","doi-asserted-by":"crossref","first-page":"10957","DOI":"10.1007\/s11033-012-1997-x","article-title":"Cathelicidins: family of antimicrobial peptides. A review","volume":"39","author":"Ko\u015bciuczuk","year":"2012","journal-title":"Mol. Biol. Rep."},{"key":"10.1016\/j.micpath.2020.104704_bib19","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0014-5793(95)01050-O","article-title":"A novel protein family with a common proregion and a variable C-terminal antimicrobial domain","volume":"374","author":"Zanetti","year":"1995","journal-title":"FEBS Lett."},{"issue":"12","key":"10.1016\/j.micpath.2020.104704_bib20","doi-asserted-by":"crossref","first-page":"3951","DOI":"10.1182\/blood.V97.12.3951","article-title":"Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3","volume":"97","author":"S\u00f8rensen","year":"2001","journal-title":"Blood"},{"issue":"11","key":"10.1016\/j.micpath.2020.104704_bib21","doi-asserted-by":"crossref","first-page":"6356","DOI":"10.1128\/IAI.00460-06","article-title":"A newly identified leptospiral adhesin mediates attachment to laminin","volume":"74","author":"Barbosa","year":"2006","journal-title":"Infect. Immun."},{"issue":"5259","key":"10.1016\/j.micpath.2020.104704_bib22","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"10.1016\/j.micpath.2020.104704_bib23","doi-asserted-by":"crossref","first-page":"1103","DOI":"10.1590\/S0100-879X2004000800001","article-title":"A high-copy T7 Escherichia coli expression vector for the production of recombinant proteins with a minimal N-terminal His-tagged fusion peptide","volume":"37","author":"Ramos","year":"2004","journal-title":"Braz. J. Med. Biol. Res."},{"key":"10.1016\/j.micpath.2020.104704_bib24","article-title":"Leptospira interrogans thermolysin refolded at high pressure and alkaline pH displays proteolytic activity against complement C3","volume":"19","author":"Chura-Chambi","year":"2018","journal-title":"Biotechnol. Rep."},{"issue":"17","key":"10.1016\/j.micpath.2020.104704_bib25","doi-asserted-by":"crossref","first-page":"5421","DOI":"10.1046\/j.1432-1327.2000.01606.x","article-title":"Investigation of the Alamar Blue (resazurin) fluorescent dye for the assessment of mammalian cell cytotoxicity","volume":"267","author":"O'Brien","year":"2000","journal-title":"Eur. J. Biochem."},{"issue":"3","key":"10.1016\/j.micpath.2020.104704_bib26","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1128\/CMR.00056-05","article-title":"Peptide antimicrobial agents","volume":"19","author":"Jenssen","year":"2006","journal-title":"Clin. Microbiol. Rev."},{"issue":"7","key":"10.1016\/j.micpath.2020.104704_bib27","first-page":"3919","article-title":"The antimicrobial peptides and their potential clinical applications","volume":"11","author":"Lei","year":"2019","journal-title":"Am. J. Transl. Res."},{"issue":"6","key":"10.1016\/j.micpath.2020.104704_bib28","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1093\/jac\/dkf220","article-title":"Comparative in vitro activity of five cathelicidin-derived sythetic peptides against Leptospira, Borrelia and Treponema pallidum","volume":"50","author":"Sambri","year":"2002","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.micpath.2020.104704_bib29","volume":"vols. 1\u201321","author":"Lindow","year":"2016"}],"container-title":["Microbial Pathogenesis"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0882401020310706?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0882401020310706?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T18:52:03Z","timestamp":1777575123000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0882401020310706"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,1]]},"references-count":29,"alternative-id":["S0882401020310706"],"URL":"https:\/\/doi.org\/10.1016\/j.micpath.2020.104704","relation":{},"ISSN":["0882-4010"],"issn-type":[{"value":"0882-4010","type":"print"}],"subject":[],"published":{"date-parts":[[2021,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Inactivation of the antimicrobial peptide LL-37 by pathogenic Leptospira","name":"articletitle","label":"Article Title"},{"value":"Microbial Pathogenesis","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.micpath.2020.104704","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"104704"}}