{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T18:53:13Z","timestamp":1793904793927,"version":"4.8.0"},"reference-count":76,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100004809","name":"Financiadora de Estudos e Projetos","doi-asserted-by":"publisher","award":["01.09.0278.00"],"award-info":[{"award-number":["01.09.0278.00"]}],"id":[{"id":"10.13039\/501100004809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004901","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de Minas Gerais","doi-asserted-by":"publisher","award":["APQ-00121-21"],"award-info":[{"award-number":["APQ-00121-21"]}],"id":[{"id":"10.13039\/501100004901","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005942","name":"Funda\u00e7\u00e3o Butantan","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005942","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["301974\/2019\u20135"],"award-info":[{"award-number":["301974\/2019\u20135"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["304445\/2021\u20135"],"award-info":[{"award-number":["304445\/2021\u20135"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["305961\/2019\u20135"],"award-info":[{"award-number":["305961\/2019\u20135"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["405925\/2021\u20132"],"award-info":[{"award-number":["405925\/2021\u20132"]}],"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":["2013\/50218\u20132"],"award-info":[{"award-number":["2013\/50218\u20132"]}],"id":[{"id":"10.13039\/501100001807","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\/06201\u20131"],"award-info":[{"award-number":["2018\/06201\u20131"]}],"id":[{"id":"10.13039\/501100001807","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":["2019\/17488\u20132"],"award-info":[{"award-number":["2019\/17488\u20132"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Proteomics"],"published-print":{"date-parts":[[2024,4]]},"DOI":"10.1016\/j.jprot.2024.105125","type":"journal-article","created":{"date-parts":[[2024,2,14]],"date-time":"2024-02-14T08:38:29Z","timestamp":1707899909000},"page":"105125","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":3,"special_numbering":"C","title":["Global proteome of the saprophytic strain Leptospira biflexa and comparative analysis with pathogenic strain Leptospira interrogans uncover new pathogenesis mechanisms"],"prefix":"10.1016","volume":"297","author":[{"given":"Edson G.","family":"Nascimento Filho","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M\u00f4nica L.","family":"Vieira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Meriellen","family":"Dias","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria A.","family":"Mendes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fabio B.","family":"Sanchez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jo\u00e3o C.","family":"Setubal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcos B.","family":"Heinemann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gisele O.","family":"Souza","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel C.","family":"Pimenta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana L.T.O.","family":"Nascimento","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jprot.2024.105125_bb0005","series-title":"Leptospira and Leptospirosis","author":"Faine","year":"1999"},{"issue":"10","key":"10.1016\/j.jprot.2024.105125_bb0010","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":"Ko","year":"2009","journal-title":"Nat. Rev. Microbiol."},{"issue":"12","key":"10.1016\/j.jprot.2024.105125_bb0015","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1016\/S1473-3099(03)00830-2","article-title":"Peru-United States leptospirosis consortium, leptospirosis: a zoonotic disease of global importance","volume":"3","author":"Bharti","year":"2003","journal-title":"Lancet Infect. Dis."},{"issue":"5","key":"10.1016\/j.jprot.2024.105125_bb0020","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1097\/01.qco.0000178824.05715.2c","article-title":"Leptospirosis","volume":"18","author":"McBride","year":"2005","journal-title":"Curr. Opin. Infect. Dis."},{"issue":"4","key":"10.1016\/j.jprot.2024.105125_bb0025","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/j.ijid.2007.09.011","article-title":"The globalization of leptospirosis: worldwide incidence trends","volume":"12","author":"Pappas","year":"2008","journal-title":"Int. J. Infect. Dis."},{"issue":"10","key":"10.1016\/j.jprot.2024.105125_bb0030","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0004122","article-title":"Global burden of leptospirosis: estimated in terms of disability adjusted life years","volume":"9","author":"Torgerson","year":"2015","journal-title":"PLoS Negl. Trop. Dis."},{"issue":"9","key":"10.1016\/j.jprot.2024.105125_bb0035","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 Negl. Trop. Dis."},{"issue":"2","key":"10.1016\/j.jprot.2024.105125_bb0040","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1128\/CMR.14.2.296-326.2001","article-title":"Leptospirosis","volume":"14","author":"Levett","year":"2001","journal-title":"Clin. Microbiol. Rev."},{"issue":"1 Suppl 1","key":"10.1016\/j.jprot.2024.105125_bb0045","first-page":"37","article-title":"Leptospirosis: a worldwide resurgent zoonosis and important cause of acute renal failure and death in developing nations","volume":"19","author":"Cruz","year":"2009","journal-title":"Ethn. Dis."},{"issue":"1","key":"10.1016\/j.jprot.2024.105125_bb0050","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.tmaid.2009.12.002","article-title":"Leptospirosis: an emerging disease in travellers","volume":"8","author":"Lau","year":"2010","journal-title":"Travel Med. Infect. Dis."},{"issue":"6","key":"10.1016\/j.jprot.2024.105125_bb0055","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/j.anaerobe.2011.05.016","article-title":"Climate changes, environment and infection: facts, scenarios and growing awareness from the public health community within Europe","volume":"17","author":"Bezirtzoglou","year":"2011","journal-title":"Anaerobe."},{"issue":"6","key":"10.1016\/j.jprot.2024.105125_bb0060","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1016\/S1995-7645(12)60086-8","article-title":"Leptospirosis: a re-emerging infection","volume":"5","author":"Sarkar","year":"2012","journal-title":"Asian Pac J Trop Med"},{"issue":"4","key":"10.1016\/j.jprot.2024.105125_bb0065","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1590\/S0100-879X2004000400003","article-title":"Genome features of Leptospira interrogans serovar Copenhageni","volume":"37","author":"Nascimento","year":"2004","journal-title":"Braz. J. Med. Biol. Res."},{"issue":"2","key":"10.1016\/j.jprot.2024.105125_bb0070","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0001607","article-title":"Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis","volume":"3","author":"Picardeau","year":"2008","journal-title":"PLoS One"},{"issue":"2","key":"10.1016\/j.jprot.2024.105125_bb0075","doi-asserted-by":"crossref","first-page":"e0004403","DOI":"10.1371\/journal.pntd.0004403","article-title":"What Makes a Bacterial Species Pathogenic?: Comparative Genomic Analysis of the Genus Leptospira","volume":"10","author":"Fouts","year":"2016","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.jprot.2024.105125_bb0080","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.jprot.2018.02.025","article-title":"Proteomics as a tool to understand Leptospira physiology and virulence: recent advances, challenges and clinical implications","volume":"180","author":"Nascimento Filho","year":"2018","journal-title":"J. Proteome"},{"issue":"9","key":"10.1016\/j.jprot.2024.105125_bb0085","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":"Vieira","year":"2009","journal-title":"Infect. Immun."},{"issue":"7256","key":"10.1016\/j.jprot.2024.105125_bb0090","doi-asserted-by":"crossref","first-page":"762","DOI":"10.1038\/nature08184","article-title":"Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans","volume":"460","author":"Malmstr\u00f6m","year":"2009","journal-title":"Nature."},{"issue":"8","key":"10.1016\/j.jprot.2024.105125_bb0095","doi-asserted-by":"crossref","first-page":"1210","DOI":"10.1038\/cr.2011.46","article-title":"Comparative proteogenomic analysis of the Leptospira interrogans virulence-attenuated strain IPAV against the pathogenic strain 56601","volume":"21","author":"Zhong","year":"2011","journal-title":"Cell Res."},{"key":"10.1016\/j.jprot.2024.105125_bb0100","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1002\/pmic.202000170","article-title":"Triton X-114 fractionated subcellular proteome of Leptospira interrogans shows selective enrichment of pathogenic and outer membrane proteins in the detergent fraction","volume":"20","author":"Thoduvayil","year":"2020","journal-title":"Proteomics."},{"issue":"4","key":"10.1016\/j.jprot.2024.105125_bb0105","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1128\/AEM.03056-15","article-title":"Multiple posttranslational modifications of Leptospira biflexa proteins as revealed by proteomic analysis","volume":"82","author":"Stewart","year":"2015","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.jprot.2024.105125_bb0110","series-title":"XI Congress of the Italian Society for Microbiology, Cagliari-Sassari, Italy","first-page":"408","article-title":"Studio serologico del gruppo Semaranga-Patoc di Leptospira biflexa","author":"Babudieri","year":"1961"},{"issue":"4","key":"10.1016\/j.jprot.2024.105125_bb0115","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.M111.010587","article-title":"PEAKS DB: de novo sequencing assisted database search for sensitive and accurate peptide identification","volume":"11","author":"Zhang","year":"2012","journal-title":"Mol. Cell. Proteomics"},{"issue":"D1","key":"10.1016\/j.jprot.2024.105125_bb0120","doi-asserted-by":"crossref","first-page":"D1107","DOI":"10.1093\/nar\/gkw1080","article-title":"jPOSTrepo: an international standard data repository for proteomes","volume":"45","author":"Okuda","year":"2017","journal-title":"Nucleic Acids Res."},{"issue":"24","key":"10.1016\/j.jprot.2024.105125_bb0125","doi-asserted-by":"crossref","first-page":"7696","DOI":"10.1128\/AEM.02411-13","article-title":"GET_HOMOLOGUES, a versatile software package for scalable and robust microbial pangenome analysis","volume":"79","author":"Contreras-Moreira","year":"2013","journal-title":"Appl. Environ. Microbiol."},{"issue":"2","key":"10.1016\/j.jprot.2024.105125_bb0130","doi-asserted-by":"crossref","first-page":"56","DOI":"10.3390\/microorganisms7020056","article-title":"In silico analysis of genetic VapC profiles from the toxin-antitoxin type II VapBC modules among pathogenic, intermediate, and non-pathogenic Leptospira","volume":"7","author":"Lopes","year":"2019","journal-title":"Microorganisms."},{"issue":"Database issue","key":"10.1016\/j.jprot.2024.105125_bb0135","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1093\/nar\/gku1223","article-title":"Expanded microbial genome coverage and improved protein family annotation in the COG database","volume":"43","author":"Galperin","year":"2015","journal-title":"Nucleic Acids Res."},{"issue":"13","key":"10.1016\/j.jprot.2024.105125_bb0140","doi-asserted-by":"crossref","first-page":"3613","DOI":"10.1093\/nar\/gkg602","article-title":"PSORT-B: improving protein subcellular localization prediction for gram-negative bacteria","volume":"31","author":"Gardy","year":"2013","journal-title":"Nucleic Acids Res."},{"issue":"6","key":"10.1016\/j.jprot.2024.105125_bb0145","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0099368","article-title":"CELLO2GO: a web server for protein subCELlular LOcalization prediction with functional gene ontology annotation","volume":"9","author":"Yu","year":"2014","journal-title":"PLoS One"},{"issue":"7","key":"10.1016\/j.jprot.2024.105125_bb0150","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1038\/s41587-021-01156-3","article-title":"SignalP 6.0 predicts all five types of signal peptides using protein language models","volume":"40","author":"Teufel","year":"2022","journal-title":"Nat. Biotechnol."},{"issue":"8","key":"10.1016\/j.jprot.2024.105125_bb0155","doi-asserted-by":"crossref","first-page":"1652","DOI":"10.1110\/ps.0303703","article-title":"Prediction of lipoprotein signal peptides in gram-negative bacteria","volume":"12","author":"Juncker","year":"2003","journal-title":"Protein Sci."},{"issue":"D1","key":"10.1016\/j.jprot.2024.105125_bb0160","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1093\/nar\/gkaa937","article-title":"SMART: recent updates, new developments and status in 2020","volume":"49","author":"Letunic","year":"2021","journal-title":"Nucleic Acids Res."},{"issue":"1","key":"10.1016\/j.jprot.2024.105125_bb0165","first-page":"213","article-title":"Novel domains of the prokaryotic two-component signal transduction systems","volume":"204","author":"Galperin","year":"2001","journal-title":"FEMS Microbiol. Lett."},{"key":"10.1016\/j.jprot.2024.105125_bb0170","series-title":"Essentials of Glycobiology","article-title":"Chapter 14: Sialic Acids","author":"Varki","year":"2009"},{"key":"10.1016\/j.jprot.2024.105125_bb0175","first-page":"12","article-title":"Expression of sialic acids and other nonulosonic acids in Leptospira","volume":"161","author":"Ricaldi","year":"2012","journal-title":"BMC Microbiol."},{"issue":"3","key":"10.1016\/j.jprot.2024.105125_bb0180","doi-asserted-by":"crossref","DOI":"10.1099\/mic.0.001157","article-title":"How bacteria utilize sialic acid during interactions with the host: snip, snatch, dispatch, match and attach","volume":"168","author":"Jennings","year":"2022","journal-title":"Microbiology (Reading)."},{"issue":"1","key":"10.1016\/j.jprot.2024.105125_bb0185","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1007479","article-title":"To B12 or not to B12: five questions on the role of cobalamin in host-microbial interactions","volume":"15","author":"Rowley","year":"2019","journal-title":"PLoS Pathog."},{"issue":"5962","key":"10.1016\/j.jprot.2024.105125_bb0190","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1126\/science.1179555","article-title":"CRISPR\/Cas, the immune system of bacteria and archaea","volume":"327","author":"Horvath","year":"2010","journal-title":"Science."},{"issue":"4","key":"10.1016\/j.jprot.2024.105125_bb0195","doi-asserted-by":"crossref","first-page":"908","DOI":"10.1016\/j.jmb.2009.12.021","article-title":"Crystal structure of the LasA virulence factor from Pseudomonas aeruginosa: substrate specificity and mechanism of M23 metallopeptidases","volume":"396","author":"Spencer","year":"2010","journal-title":"J. Mol. Biol."},{"issue":"7","key":"10.1016\/j.jprot.2024.105125_bb0200","first-page":"1684","article-title":"Evidence for cleavage of the metalloprotease Vsm from Vibrio splendidus strain JZ6 by an M20 peptidase (PepT-like protein) at low temperature","volume":"25","author":"Liu","year":"2016","journal-title":"Front. Microbiol."},{"issue":"9","key":"10.1016\/j.jprot.2024.105125_bb0205","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0007023","article-title":"The NlpD lipoprotein is a novel Yersinia pestis virulence factor essential for the development of plague","volume":"4","author":"Tidhar","year":"2009","journal-title":"PLoS One"},{"issue":"2","key":"10.1016\/j.jprot.2024.105125_bb0210","doi-asserted-by":"crossref","DOI":"10.1128\/JB.00434-20","article-title":"Structure-function characterization of the conserved regulatory mechanism of the Escherichia coli M48 metalloprotease BepA","volume":"203","author":"Bryant","year":"2020","journal-title":"J. Bacteriol."},{"issue":"2","key":"10.1016\/j.jprot.2024.105125_bb0215","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1111\/j.1574-695X.2007.00323.x","article-title":"Peptidase N encoded by salmonella enterica serovar typhimurium modulates systemic infection in mice","volume":"51","author":"Patil","year":"2007","journal-title":"FEMS Immunol. Med. Microbiol."},{"issue":"2","key":"10.1016\/j.jprot.2024.105125_bb0220","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.mam.2011.10.015","article-title":"Human matrix metalloproteinases: an ubiquitarian class of enzymes involved in several pathological processes","volume":"33","author":"Sbardella","year":"2012","journal-title":"Mol. Asp. Med."},{"key":"10.1016\/j.jprot.2024.105125_bb0225","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.micpath.2013.04.011","article-title":"Evaluation of the elastinolytic activity and protective effect of Leptallo I, a protein composed by metalloprotease and FA5\/8C domains, from Leptospira interrogans Copenhageni","volume":"61-62","author":"Hashimoto","year":"2013","journal-title":"Microb. Pathog."},{"key":"10.1016\/j.jprot.2024.105125_bb0230","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. Report."},{"issue":"6","key":"10.1016\/j.jprot.2024.105125_bb0235","doi-asserted-by":"crossref","first-page":"1008","DOI":"10.1093\/infdis\/jiaa176","article-title":"M16-type metallopeptidases are involved in virulence for invasiveness and diffusion of Leptospira interrogans and transmission of leptospirosis","volume":"222","author":"Ge","year":"2020","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.jprot.2024.105125_bb0240","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1146\/annurev.biochem.74.082803.133347","article-title":"NOD-LRR proteins: role in host-microbial interactions and inflammatory disease","volume":"74","author":"Inohara","year":"2005","journal-title":"Annu. Rev. Biochem."},{"issue":"9","key":"10.1016\/j.jprot.2024.105125_bb0245","doi-asserted-by":"crossref","first-page":"1082","DOI":"10.4161\/auto.7.9.16464","article-title":"Leucine-rich repeat (LRR) proteins: integrators of pattern recognition and signaling in immunity","volume":"7","author":"Ng","year":"2011","journal-title":"Autophagy."},{"issue":"2","key":"10.1016\/j.jprot.2024.105125_bb0250","doi-asserted-by":"crossref","DOI":"10.1111\/cmi.12949","article-title":"An extracellular Leptospira interrogans leucine-rich repeat protein binds human E- and VE-cadherins","volume":"21","author":"Eshghi","year":"2019","journal-title":"Cell. Microbiol."},{"issue":"1","key":"10.1016\/j.jprot.2024.105125_bb0255","doi-asserted-by":"crossref","first-page":"6","DOI":"10.3390\/tropicalmed8010006","article-title":"Leptospira borgpetersenii leucine-rich repeat proteins provide strong protective efficacy as novel Leptospiral vaccine candidates","volume":"8","author":"Prapong","year":"2022","journal-title":"Trop. Med. Infect. Dis."},{"issue":"3","key":"10.1016\/j.jprot.2024.105125_bb0260","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1128\/IAI.01035-12","article-title":"Tetratricopeptide repeat motifs in the world of bacterial pathogens: role in virulence mechanisms","volume":"81","author":"Cerveny","year":"2013","journal-title":"Infect. Immun."},{"key":"10.1016\/j.jprot.2024.105125_bb0265","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.sbi.2018.12.004","article-title":"The tetratricopeptide-repeat motif is a versatile platform that enables diverse modes of molecular recognition","volume":"54","author":"Perez-Riba","year":"2019","journal-title":"Curr. Opin. Struct. Biol."},{"issue":"12","key":"10.1016\/j.jprot.2024.105125_bb0270","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0083246","article-title":"LipL41, a hemin binding protein from Leptospira santarosai serovar Shermani","volume":"8","author":"Lin","year":"2013","journal-title":"PLoS One"},{"issue":"3","key":"10.1016\/j.jprot.2024.105125_bb0275","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.tim.2009.11.004","article-title":"Functional diversity of ankyrin repeats in microbial proteins","volume":"18","author":"Al-Khodor","year":"2010","journal-title":"Trends Microbiol."},{"issue":"8","key":"10.1016\/j.jprot.2024.105125_bb0280","doi-asserted-by":"crossref","first-page":"875","DOI":"10.3390\/pathogens11080875","article-title":"Poxviral ANKR\/F-box proteins: substrate adapters for Ubiquitylation and more","volume":"11","author":"Ingham","year":"2022","journal-title":"Pathogens."},{"issue":"7","key":"10.1016\/j.jprot.2024.105125_bb0285","doi-asserted-by":"crossref","DOI":"10.1128\/jb.00182-22","article-title":"The Ankyrin repeat protein RARP-1 is a periplasmic factor that supports rickettsia parkeri growth and host cell invasion","volume":"204","author":"Sanderlin","year":"2022","journal-title":"J. Bacteriol."},{"issue":"11","key":"10.1016\/j.jprot.2024.105125_bb0290","doi-asserted-by":"crossref","first-page":"4727","DOI":"10.1128\/iai.62.11.4727-4738.1994","article-title":"Cloning and sequencing of a Bordetella pertussis serum resistance locus","volume":"62","author":"Fernandez","year":"1994","journal-title":"Infect. Immun."},{"issue":"1","key":"10.1016\/j.jprot.2024.105125_bb0295","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1128\/IAI.69.1.400-404.2001","article-title":"Temperature-regulated protein synthesis by Leptospira interrogans","volume":"69","author":"Nally","year":"2001","journal-title":"Infect. Immun."},{"issue":"5","key":"10.1016\/j.jprot.2024.105125_bb0300","doi-asserted-by":"crossref","first-page":"2441","DOI":"10.1128\/IAI.01635-06","article-title":"Physiological osmotic induction of Leptospira interrogans adhesion: LigA and LigB bind extracellular matrix proteins and fibrinogen","volume":"75","author":"Choy","year":"2007","journal-title":"Infect. Immun."},{"issue":"70","key":"10.1016\/j.jprot.2024.105125_bb0305","first-page":"1","article-title":"Lsa21, a novel leptospiral protein binding adhesive matrix molecules and present during human infection","volume":"8","author":"Atzingen","year":"2008","journal-title":"BMC Microbiol."},{"issue":"9","key":"10.1016\/j.jprot.2024.105125_bb0310","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0000815","article-title":"The OmpL37 surface-exposed protein is expressed by pathogenic Leptospira during infection and binds skin and vascular elastin","volume":"4","author":"Pinne","year":"2010","journal-title":"PLoS Negl. Trop. Dis."},{"issue":"2","key":"10.1016\/j.jprot.2024.105125_bb0315","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0016879","article-title":"The multifunctional LigB adhesin binds homeostatic proteins with potential roles in cutaneous infection by pathogenic Leptospira interrogans","volume":"6","author":"Choy","year":"2011","journal-title":"PLoS One"},{"issue":"4","key":"10.1016\/j.jprot.2024.105125_bb0320","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0003712","article-title":"Evaluation of cell binding activities of Leptospira ECM adhesins","volume":"9","author":"Robbins","year":"2015","journal-title":"PLoS Negl. Trop. Dis."},{"issue":"783","key":"10.1016\/j.jprot.2024.105125_bb0325","first-page":"1","article-title":"Temperature and oxidative stress as triggers for virulence gene expression in pathogenic Leptospira spp","volume":"8","author":"Fraser","year":"2017","journal-title":"Front. Microbiol."},{"issue":"6","key":"10.1016\/j.jprot.2024.105125_bb0330","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1111\/lam.13461","article-title":"Evaluation of the diagnostic potential of recombinant leptospiral OMP A-like protein (Loa22) and transmembrane (OmpL37) protein in latex agglutination test for serodiagnosis of leptospirosis in animals","volume":"72","author":"Balamurugan","year":"2021","journal-title":"Lett. Appl. Microbiol."},{"issue":"1","key":"10.1016\/j.jprot.2024.105125_bb0335","doi-asserted-by":"crossref","first-page":"2798","DOI":"10.1080\/21505594.2021.1993427","article-title":"The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components","volume":"12","author":"Takahashi","year":"2021","journal-title":"Virulence."},{"issue":"7","key":"10.1016\/j.jprot.2024.105125_bb0340","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0180004","article-title":"Immunoprotective properties of recombinant LigA and LigB in a hamster model of acute leptospirosis","volume":"12","author":"Evangelista","year":"2017","journal-title":"PLoS One"},{"issue":"6","key":"10.1016\/j.jprot.2024.105125_bb0345","doi-asserted-by":"crossref","first-page":"2642","DOI":"10.1128\/IAI.01639-07","article-title":"In LipL32, the major leptospiral lipoprotein, the C terminus is the primary immunogenic domain and mediates interaction with collagen IV and plasma fibronectin","volume":"76","author":"Hauk","year":"2008","journal-title":"Infect. Immun."},{"issue":"2\u20134","key":"10.1016\/j.jprot.2024.105125_bb0350","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/j.vetmic.2012.11.005","article-title":"The lipoprotein LipL32, an enigma of leptospiral biology","volume":"162","author":"Murray","year":"2013","journal-title":"Vet. Microbiol."},{"issue":"4","key":"10.1016\/j.jprot.2024.105125_bb0355","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1128\/CVI.00719-13","article-title":"Vaccination with leptospiral outer membrane lipoprotein LipL32 reduces kidney invasion of Leptospira interrogans serovar canicola in hamsters","volume":"21","author":"Humphryes","year":"2014","journal-title":"Clin. Vaccine Immunol."},{"key":"10.1016\/j.jprot.2024.105125_bb0360","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2021.799012","article-title":"Evaluation of LipL32 and LigA\/LigB knockdown mutants in Leptospira interrogans Serovar Copenhageni: impacts to proteome and virulence","volume":"12","author":"Fernandes","year":"2022","journal-title":"Front. Microbiol."},{"issue":"12","key":"10.1016\/j.jprot.2024.105125_bb0365","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1006725","article-title":"LipL21 lipoprotein binding to peptidoglycan enables Leptospira interrogans to escape NOD1 and NOD2 recognition","volume":"13","author":"Ratet","year":"2017","journal-title":"PLoS Pathog."},{"issue":"1","key":"10.1016\/j.jprot.2024.105125_bb0370","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1080\/21505594.2017.1407484","article-title":"Leptospira interrogans outer membrane protein LipL21 is a potent inhibitor of neutrophil myeloperoxidase","volume":"9","author":"Vieira","year":"2018","journal-title":"Virulence."},{"issue":"24","key":"10.1016\/j.jprot.2024.105125_bb0375","doi-asserted-by":"crossref","first-page":"15550","DOI":"10.3390\/ijms232415550","article-title":"Host cell binding mediated by Leptospira interrogans Adhesins","volume":"23","author":"Takahashi","year":"2022","journal-title":"Int. J. Mol. Sci."},{"issue":"7","key":"10.1016\/j.jprot.2024.105125_bb0380","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.0030097","article-title":"The OmpA-like protein Loa22 is essential for leptospiral virulence","volume":"3","author":"Ristow","year":"2007","journal-title":"PLoS Pathog."}],"container-title":["Journal of Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874391924000575?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874391924000575?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T12:17:40Z","timestamp":1761740260000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874391924000575"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,4]]},"references-count":76,"alternative-id":["S1874391924000575"],"URL":"https:\/\/doi.org\/10.1016\/j.jprot.2024.105125","relation":{},"ISSN":["1874-3919"],"issn-type":[{"value":"1874-3919","type":"print"}],"subject":[],"published":{"date-parts":[[2024,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Global proteome of the saprophytic strain Leptospira biflexa and comparative analysis with pathogenic strain Leptospira interrogans uncover new pathogenesis mechanisms","name":"articletitle","label":"Article Title"},{"value":"Journal of Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jprot.2024.105125","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"105125"}}