{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T23:56:40Z","timestamp":1790985400263,"version":"4.1.0"},"update-to":[{"DOI":"10.1371\/journal.ppat.1011313","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2023,8,3]],"date-time":"2023-08-03T00:00:00Z","timestamp":1691020800000}}],"reference-count":58,"publisher":"Public Library of Science (PLoS)","issue":"7","license":[{"start":{"date-parts":[[2023,7,24]],"date-time":"2023-07-24T00:00:00Z","timestamp":1690156800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100006492","name":"Division of Intramural Research, National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["U01AI088752"],"award-info":[{"award-number":["U01AI088752"]}],"id":[{"id":"10.13039\/100006492","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006492","name":"Division of Intramural Research, National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01AI121207"],"award-info":[{"award-number":["R01AI121207"]}],"id":[{"id":"10.13039\/100006492","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006492","name":"Division of Intramural Research, National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R21AI163663"],"award-info":[{"award-number":["R21AI163663"]}],"id":[{"id":"10.13039\/100006492","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"}]},{"DOI":"10.13039\/501100017564","name":"Ci\u00eancia sem Fronteiras","doi-asserted-by":"publisher","award":["205952\/2014-3"],"award-info":[{"award-number":["205952\/2014-3"]}],"id":[{"id":"10.13039\/501100017564","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":["2020\/02678-8"],"award-info":[{"award-number":["2020\/02678-8"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    Leptospirosis, a zoonosis with worldwide distribution, is caused by pathogenic spirochetes belonging to the genus\n                    <jats:italic>Leptospira<\/jats:italic>\n                    . Bacterial outer membrane proteins (OMPs), particularly those with surface-exposed regions, play crucial roles in pathogen dissemination and virulence mechanisms. Here we characterized the leptospiral Membrane Protein L36 (MPL36), a rare lipoprotein A (RlpA) homolog with a C-terminal Sporulation related (SPOR) domain, as an important virulence factor in pathogenic\n                    <jats:italic>Leptospira<\/jats:italic>\n                    . Our results confirmed that MPL36 is surface exposed and expressed during infection. Using recombinant MPL36 (rMPL36) we also confirmed previous findings of its high plasminogen (PLG)-binding ability determined by lysine residues of the C-terminal region of the protein, with ability to convert bound-PLG to active plasmin. Using Koch\u2019s molecular postulates, we determined that a mutant of\n                    <jats:italic>mpl36<\/jats:italic>\n                    has a reduced PLG-binding ability, leading to a decreased capacity to adhere and translocate MDCK cell monolayers. Using recombinant protein and mutant strains, we determined that the MPL36-bound plasmin (PLA) can degrade fibrinogen. Finally, our\n                    <jats:italic>mpl36<\/jats:italic>\n                    mutant had a significant attenuated phenotype in the hamster model for acute leptospirosis. Our data indicates that MPL36 is the major PLG binding protein in pathogenic\n                    <jats:italic>Leptospira<\/jats:italic>\n                    , and crucial to the pathogen\u2019s ability to attach and interact with host tissues during infection. The MPL36 characterization contributes to the expanding field of bacterial pathogens that explore PLG for their virulence, advancing the goal to close the knowledge gap regarding leptospiral pathogenesis while offering a novel potential candidate to improve diagnostic and prevention of this important zoonotic neglected disease.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1011313","type":"journal-article","created":{"date-parts":[[2023,7,24]],"date-time":"2023-07-24T13:27:47Z","timestamp":1690205267000},"page":"e1011313","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":7,"title":["MPL36, a major plasminogen (PLG) receptor in pathogenic Leptospira, has an essential role during infection"],"prefix":"10.1371","volume":"19","author":[{"given":"Weinan","family":"Zhu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Felipe J.","family":"Passalia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Camila","family":"Hamond","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cec\u00edlia M.","family":"Abe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Albert I.","family":"Ko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Angela S.","family":"Barbosa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5239-8511","authenticated-orcid":true,"given":"Elsio A.","family":"Wunder","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2023,7,24]]},"reference":[{"issue":"5","key":"ppat.1011313.ref001","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/S0168-6445(01)00067-5","article-title":"Bacterial plasminogen activators and receptors","volume":"25","author":"K Lahteenmaki","year":"2001","journal-title":"FEMS Microbiol Rev"},{"key":"ppat.1011313.ref002","doi-asserted-by":"crossref","first-page":"272148","DOI":"10.1155\/2012\/272148","article-title":"Bacterial plasminogen receptors: mediators of a multifaceted relationship","volume":"2012","author":"ML Sanderson-Smith","year":"2012","journal-title":"Journal of biomedicine & biotechnology"},{"issue":"22","key":"ppat.1011313.ref003","doi-asserted-by":"crossref","first-page":"18831","DOI":"10.1074\/jbc.M111.323287","article-title":"Plasminogen is a complement inhibitor","volume":"287","author":"D Barthel","year":"2012","journal-title":"The Journal of biological chemistry"},{"key":"ppat.1011313.ref004","doi-asserted-by":"crossref","first-page":"777709","DOI":"10.3389\/fcimb.2021.777709","article-title":"A Review on Host-Leptospira Interactions: What We Know and Future Expectations.","volume":"11","author":"BB Daroz","year":"2021","journal-title":"Frontiers in cellular and infection microbiology"},{"issue":"10","key":"ppat.1011313.ref005","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1038\/nrmicro2208","article-title":"Leptospira: the dawn of the molecular genetics era for an emerging zoonotic pathogen.","volume":"7","author":"AI Ko","year":"2009","journal-title":"Nature reviews Microbiology"},{"issue":"9","key":"ppat.1011313.ref006","doi-asserted-by":"crossref","first-page":"e0003898","DOI":"10.1371\/journal.pntd.0003898","article-title":"Global Morbidity and Mortality of Leptospirosis: A Systematic Review.","volume":"9","author":"F Costa","year":"2015","journal-title":"PLoS neglected tropical diseases"},{"issue":"6","key":"ppat.1011313.ref007","doi-asserted-by":"crossref","first-page":"1561","DOI":"10.1086\/313501","article-title":"Acute lung injury in leptospirosis: clinical and laboratory features, outcome, and factors associated with mortality. Clinical infectious diseases: an official publication of the","volume":"29","author":"PC Marotto","year":"1999","journal-title":"Infectious Diseases Society of America"},{"issue":"3","key":"ppat.1011313.ref008","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/j.jinf.2009.12.005","article-title":"Early identification of leptospirosis-associated pulmonary hemorrhage syndrome by use of a validated prediction model","volume":"60","author":"PC Marotto","year":"2010","journal-title":"The Journal of infection"},{"issue":"3","key":"ppat.1011313.ref009","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1086\/427110","article-title":"Clinical spectrum of pulmonary involvement in leptospirosis in a region of endemicity, with quantification of leptospiral burden. Clinical infectious diseases: an official publication of the","volume":"40","author":"ER Segura","year":"2005","journal-title":"Infectious Diseases Society of America"},{"issue":"3","key":"ppat.1011313.ref010","doi-asserted-by":"crossref","first-page":"505","DOI":"10.3201\/eid1403.071064","article-title":"Leptospirosis-associated severe pulmonary hemorrhagic syndrome, Salvador, Brazil","volume":"14","author":"EL Gouveia","year":"2008","journal-title":"Emerging infectious diseases"},{"issue":"1","key":"ppat.1011313.ref011","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/S1201-9712(02)90137-2","article-title":"Prognostic factors of death in leptospirosis: a prospective cohort study in Khon Kaen, Thailand.","volume":"6","author":"T Panaphut","year":"2002","journal-title":"International journal of infectious diseases: IJID: official publication of the International Society for Infectious Diseases"},{"issue":"1","key":"ppat.1011313.ref012","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1186\/s12879-019-4094-0","article-title":"Sequel and therapeutic modalities of leptospirosis associated severe pulmonary haemorrhagic syndrome (SPHS); a Sri Lankan experience.","volume":"19","author":"N Herath","year":"2019","journal-title":"BMC infectious diseases"},{"issue":"12","key":"ppat.1011313.ref013","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1016\/S1473-3099(03)00830-2","article-title":"Leptospirosis: a zoonotic disease of global importance","volume":"3","author":"AR Bharti","year":"2003","journal-title":"The Lancet infectious diseases"},{"issue":"9181","key":"ppat.1011313.ref014","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1016\/S0140-6736(99)80012-9","article-title":"Urban epidemic of severe leptospirosis in Brazil. Salvador Leptospirosis Study Group","volume":"354","author":"AI Ko","year":"1999","journal-title":"Lancet"},{"issue":"5","key":"ppat.1011313.ref015","doi-asserted-by":"crossref","first-page":"e0007270","DOI":"10.1371\/journal.pntd.0007270","article-title":"Revisiting the taxonomy and evolution of pathogenicity of the genus Leptospira through the prism of genomics","volume":"13","author":"AT Vincent","year":"2019","journal-title":"PLoS neglected tropical diseases"},{"key":"ppat.1011313.ref016","first-page":"71","article-title":"Leptospira ainlahdjerensis sp. nov., Leptospira ainazelensis sp. nov., Leptospira abararensis sp. nov. and Leptospira chreensis sp. nov., four new species isolated from water sources in Algeria","author":"AA Korba","year":"2021","journal-title":"International journal of systematic and evolutionary microbiology"},{"issue":"7","key":"ppat.1011313.ref017","doi-asserted-by":"crossref","first-page":"2105","DOI":"10.1128\/IAI.00094-16","article-title":"Real-Time PCR Reveals Rapid Dissemination of Leptospira interrogans after Intraperitoneal and Conjunctival Inoculation of Hamsters","volume":"84","author":"EA Wunder","year":"2016","journal-title":"Infection and immunity"},{"issue":"1782","key":"ppat.1011313.ref018","doi-asserted-by":"crossref","first-page":"20190367","DOI":"10.1098\/rstb.2019.0367","article-title":"Mechanistic dose-response modelling of animal challenge data shows that intact skin is a crucial barrier to leptospiral infection","volume":"374","author":"KM Gostic","year":"2019","journal-title":"Philos Trans R Soc Lond B Biol Sci"},{"issue":"5","key":"ppat.1011313.ref019","doi-asserted-by":"crossref","first-page":"eaar7975","DOI":"10.1126\/sciadv.aar7975","article-title":"The mechanism of two-phase motility in the spirochete Leptospira: Swimming and crawling","volume":"4","author":"H Tahara","year":"2018","journal-title":"Sci Adv"},{"key":"ppat.1011313.ref020","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1146\/annurev-micro-092611-150145","article-title":"The unique paradigm of spirochete motility and chemotaxis","volume":"66","author":"NW Charon","year":"2012","journal-title":"Annu Rev Microbiol"},{"issue":"10","key":"ppat.1011313.ref021","doi-asserted-by":"crossref","first-page":"e1009836","DOI":"10.1371\/journal.ppat.1009836","article-title":"Pathogenesis insights from an ancient and ubiquitous spirochete","volume":"17","author":"J Coburn","year":"2021","journal-title":"PLoS pathogens"},{"issue":"2","key":"ppat.1011313.ref022","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1111\/1574-6968.12349","article-title":"Leptospiral extracellular matrix adhesins as mediators of pathogen-host interactions","volume":"352","author":"ML Vieira","year":"2014","journal-title":"FEMS microbiology letters"},{"key":"ppat.1011313.ref023","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1186\/1471-2180-11-129","article-title":"Heterologous expression of pathogen-specific genes ligA and ligB in the saprophyte Leptospira biflexa confers enhanced adhesion to cultured cells and fibronectin","volume":"11","author":"CP Figueira","year":"2011","journal-title":"BMC microbiology"},{"issue":"4","key":"ppat.1011313.ref024","doi-asserted-by":"crossref","first-page":"e0003712","DOI":"10.1371\/journal.pntd.0003712","article-title":"Evaluation of cell binding activities of Leptospira ECM adhesins","volume":"9","author":"GT Robbins","year":"2015","journal-title":"PLoS neglected tropical diseases"},{"key":"ppat.1011313.ref025","doi-asserted-by":"crossref","first-page":"92","DOI":"10.3389\/fcimb.2018.00092","article-title":"Leptospira interrogans Secreted Proteases Degrade Extracellular Matrix and Plasma Proteins From the Host.","volume":"8","author":"LB da Silva","year":"2018","journal-title":"Frontiers in cellular and infection microbiology"},{"issue":"5","key":"ppat.1011313.ref026","doi-asserted-by":"crossref","first-page":"2053","DOI":"10.1128\/IAI.01282-09","article-title":"Leptospiral endostatin-like protein A is a bacterial cell surface receptor for human plasminogen","volume":"78","author":"A Verma","year":"2010","journal-title":"Infection and immunity"},{"issue":"9","key":"ppat.1011313.ref027","doi-asserted-by":"crossref","first-page":"4092","DOI":"10.1128\/IAI.00353-09","article-title":"Plasminogen acquisition and activation at the surface of leptospira species lead to fibronectin degradation","volume":"77","author":"ML Vieira","year":"2009","journal-title":"Infection and immunity"},{"issue":"6","key":"ppat.1011313.ref028","doi-asserted-by":"crossref","first-page":"e11259","DOI":"10.1371\/journal.pone.0011259","article-title":"In vitro identification of novel plasminogen-binding receptors of the pathogen Leptospira interrogans","volume":"5","author":"ML Vieira","year":"2010","journal-title":"PloS one"},{"issue":"5","key":"ppat.1011313.ref029","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1016\/j.imbio.2016.01.001","article-title":"Plasmin cleaves fibrinogen and the human complement proteins C3b and C5 in the presence of Leptospira interrogans proteins: A new role of LigA and LigB in invasion and complement immune evasion","volume":"221","author":"MM Castiblanco-Valencia","year":"2016","journal-title":"Immunobiology"},{"issue":"11","key":"ppat.1011313.ref030","doi-asserted-by":"crossref","first-page":"e81818","DOI":"10.1371\/journal.pone.0081818","article-title":"Interaction of Leptospira elongation factor Tu with plasminogen and complement factor H: a metabolic leptospiral protein with moonlighting activities","volume":"8","author":"DG Wolff","year":"2013","journal-title":"PloS one"},{"issue":"2","key":"ppat.1011313.ref031","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.resmic.2016.10.005","article-title":"The multifaceted roles of Leptospira enolase","volume":"168","author":"N Salazar","year":"2017","journal-title":"Research in microbiology"},{"key":"ppat.1011313.ref032","doi-asserted-by":"crossref","first-page":"758513","DOI":"10.1155\/2012\/758513","article-title":"Plasminogen binding proteins and plasmin generation on the surface of Leptospira spp.: the contribution to the bacteria-host interactions.","volume":"2012","author":"ML Vieira","year":"2012","journal-title":"Journal of biomedicine & biotechnology"},{"issue":"1","key":"ppat.1011313.ref033","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1128\/JB.01244-09","article-title":"Discovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpA","volume":"192","author":"SJ Arends","year":"2010","journal-title":"Journal of bacteriology"},{"issue":"24","key":"ppat.1011313.ref034","doi-asserted-by":"crossref","first-page":"7383","DOI":"10.1128\/JB.00811-09","article-title":"Self-enhanced accumulation of FtsN at Division Sites and Roles for Other Proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell constriction","volume":"191","author":"MA Gerding","year":"2009","journal-title":"Journal of bacteriology"},{"issue":"14","key":"ppat.1011313.ref035","doi-asserted-by":"crossref","DOI":"10.1128\/JB.00118-17","article-title":"The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain That Targets Proteins to the Site of Cell Division","volume":"199","author":"A Yahashiri","year":"2017","journal-title":"Journal of bacteriology"},{"issue":"1","key":"ppat.1011313.ref036","doi-asserted-by":"crossref","first-page":"5567","DOI":"10.1038\/s41467-019-13354-4","article-title":"Structural basis of denuded glycan recognition by SPOR domains in bacterial cell division","volume":"10","author":"M Alcorlo","year":"2019","journal-title":"Nat Commun"},{"issue":"1","key":"ppat.1011313.ref037","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1111\/mmi.12643","article-title":"The bacterial septal ring protein RlpA is a lytic transglycosylase that contributes to rod shape and daughter cell separation in Pseudomonas aeruginosa","volume":"93","author":"MA Jorgenson","year":"2014","journal-title":"Molecular microbiology"},{"issue":"2","key":"ppat.1011313.ref038","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1128\/IAI.01293-08","article-title":"Genome-wide transposon mutagenesis in pathogenic Leptospira species","volume":"77","author":"GL Murray","year":"2009","journal-title":"Infection and immunity"},{"issue":"7","key":"ppat.1011313.ref039","doi-asserted-by":"crossref","first-page":"3207","DOI":"10.1128\/IAI.00279-10","article-title":"Functional characterization of LcpA, a surface-exposed protein of Leptospira spp. that binds the human complement regulator C4BP","volume":"78","author":"AS Barbosa","year":"2010","journal-title":"Infection and immunity"},{"issue":"2","key":"ppat.1011313.ref040","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/j.femsle.2005.02.004","article-title":"Whole-genome analysis of Leptospira interrogans to identify potential vaccine candidates against leptospirosis","volume":"244","author":"M Gamberini","year":"2005","journal-title":"FEMS microbiology letters"},{"issue":"3","key":"ppat.1011313.ref041","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":"EA Wunder","year":"2016","journal-title":"Molecular microbiology"},{"issue":"8","key":"ppat.1011313.ref042","doi-asserted-by":"crossref","first-page":"e2396","DOI":"10.1371\/journal.pntd.0002396","article-title":"Adhesins of Leptospira interrogans mediate the interaction to fibrinogen and inhibit fibrin clot formation in vitro","volume":"7","author":"R Oliveira","year":"2013","journal-title":"PLoS neglected tropical diseases"},{"issue":"4","key":"ppat.1011313.ref043","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1007\/s00284-010-9865-1","article-title":"Characterization of the immunogenic and antigenic potential of putative lipoproteins from Leptospira interrogans","volume":"62","author":"DD Hartwig","year":"2011","journal-title":"Current microbiology"},{"issue":"5","key":"ppat.1011313.ref044","first-page":"1329","article-title":"Purification, characterization and serological properties of a glycolipid antigen reactive with a serovar-specific monoclonal antibody against Leptospira interrogans serovar canicola","volume":"133","author":"E Ono","year":"1987","journal-title":"Journal of general microbiology"},{"issue":"3","key":"ppat.1011313.ref045","doi-asserted-by":"crossref","first-page":"e1004004","DOI":"10.1371\/journal.ppat.1004004","article-title":"A model system for studying the transcriptomic and physiological changes associated with mammalian host-adaptation by Leptospira interrogans serovar Copenhageni.","volume":"10","author":"MJ Caimano","year":"2014","journal-title":"PLoS pathogens"},{"key":"ppat.1011313.ref046","doi-asserted-by":"crossref","first-page":"45","DOI":"10.3389\/fcimb.2018.00045","article-title":"Lvr, a Signaling System That Controls Global Gene Regulation and Virulence in Pathogenic Leptospira.","volume":"8","author":"H Adhikarla","year":"2018","journal-title":"Frontiers in cellular and infection microbiology"},{"key":"ppat.1011313.ref047","first-page":"10","article-title":"A live attenuated-vaccine model confers cross-protective immunity against different species of the Leptospira genus","author":"EA Wunder","year":"2021","journal-title":"Elife"},{"issue":"6","key":"ppat.1011313.ref048","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.02796-20","article-title":"SPOR Proteins Are Required for Functionality of Class A Penicillin-Binding Proteins in Escherichia coli.","volume":"11","author":"M Pazos","year":"2020","journal-title":"mBio"},{"issue":"2","key":"ppat.1011313.ref049","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1007\/s00430-020-00664-4","article-title":"Leptospira interrogans Bat proteins impair host hemostasis by fibrinogen cleavage and platelet aggregation inhibition","volume":"209","author":"FJ Passalia","year":"2020","journal-title":"Medical microbiology and immunology"},{"key":"ppat.1011313.ref050","doi-asserted-by":"crossref","first-page":"20069","DOI":"10.1038\/srep20069","article-title":"Group A Streptococcus exploits human plasminogen for bacterial translocation across epithelial barrier via tricellular tight junctions","volume":"7","author":"T Sumitomo","year":"2016","journal-title":"Sci Rep"},{"issue":"2","key":"ppat.1011313.ref051","doi-asserted-by":"crossref","first-page":"e00629","DOI":"10.1128\/mBio.00629-12","article-title":"Cooperative plasminogen recruitment to the surface of Streptococcus canis via M protein and enolase enhances bacterial survival","volume":"4","author":"M Fulde","year":"2013","journal-title":"mBio"},{"issue":"3","key":"ppat.1011313.ref052","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.celrep.2012.02.012","article-title":"The X-ray crystal structure of full-length human plasminogen","volume":"1","author":"RH Law","year":"2012","journal-title":"Cell Rep"},{"issue":"1","key":"ppat.1011313.ref053","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1128\/jb.94.1.27-31.1967","article-title":"Differentiation of pathogenic and saprophytic letospires. I. Growth at low temperatures","volume":"94","author":"RC Johnson","year":"1967","journal-title":"Journal of bacteriology"},{"issue":"9","key":"ppat.1011313.ref054","doi-asserted-by":"crossref","first-page":"4936","DOI":"10.1128\/IAI.70.9.4936-4945.2002","article-title":"Characterization of the leptospiral outer membrane and description of three novel leptospiral membrane proteins","volume":"70","author":"DA Haake","year":"2002","journal-title":"Infection and immunity"},{"issue":"8","key":"ppat.1011313.ref055","first-page":"1103","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":"CR Ramos","year":"2004","journal-title":"Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas \/ Sociedade Brasileira de Biofisica"},{"issue":"12","key":"ppat.1011313.ref056","doi-asserted-by":"crossref","first-page":"22518","DOI":"10.3390\/ijms151222518","article-title":"Intrinsic tryptophan fluorescence in the detection and analysis of proteins: a focus on Forster resonance energy transfer techniques","volume":"15","author":"AB Ghisaidoobe","year":"2014","journal-title":"Int J Mol Sci"},{"key":"ppat.1011313.ref057","first-page":"141","article-title":"Toolbox of Molecular Techniques for Studying Leptospira Spp","volume":"415","author":"M. Picardeau","year":"2018","journal-title":"Current topics in microbiology and immunology"},{"issue":"7873","key":"ppat.1011313.ref058","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"J Jumper","year":"2021","journal-title":"Nature"}],"updated-by":[{"DOI":"10.1371\/journal.ppat.1011313","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2023,8,3]],"date-time":"2023-08-03T00:00:00Z","timestamp":1691020800000}}],"container-title":["PLOS Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1011313","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,8,3]],"date-time":"2023-08-03T13:53:29Z","timestamp":1691070809000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1011313"}},"subtitle":[],"editor":[{"given":"D. Scott","family":"Samuels","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2023,7,24]]},"references-count":58,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2023,7,24]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.ppat.1011313","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2023.03.24.534066","asserted-by":"object"}]},"ISSN":["1553-7374"],"issn-type":[{"value":"1553-7374","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,7,24]]}}}