{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,1]],"date-time":"2026-07-01T07:20:35Z","timestamp":1782890435799,"version":"3.54.5"},"reference-count":47,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2020,2,1]],"date-time":"2020-02-01T00:00:00Z","timestamp":1580515200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,2,1]],"date-time":"2020-02-01T00:00:00Z","timestamp":1580515200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2018,2,9]],"date-time":"2018-02-09T00:00:00Z","timestamp":1518134400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100014238","name":"Riordan Foundation","doi-asserted-by":"publisher","award":["RSA5980036"],"award-info":[{"award-number":["RSA5980036"]}],"id":[{"id":"10.13039\/100014238","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004156","name":"Mahidol University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004156","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006439","name":"Faculty of Tropical Medicine, Mahidol University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100006439","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Microbiology, Immunology and Infection"],"published-print":{"date-parts":[[2020,2]]},"DOI":"10.1016\/j.jmii.2017.12.006","type":"journal-article","created":{"date-parts":[[2018,2,14]],"date-time":"2018-02-14T12:59:35Z","timestamp":1518613175000},"page":"11-22","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"title":["Immunodominance of LipL3293\u2013272 peptides revealed by leptospirosis sera and therapeutic monoclonal antibodies"],"prefix":"10.1016","volume":"53","author":[{"given":"Tippawan","family":"Pissawong","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Santi","family":"Maneewatchararangsri","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nonglucksanawan","family":"Ritthisunthorn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ngamphol","family":"Soonthornworasiri","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Onrapak","family":"Reamtong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Poom","family":"Adisakwattana","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8444-9689","authenticated-orcid":false,"given":"Thareerat","family":"Kalambaheti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Urai","family":"Chaisri","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Galayanee","family":"Doungchawee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"10","key":"10.1016\/j.jmii.2017.12.006_bib1","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"},{"key":"10.1016\/j.jmii.2017.12.006_bib2","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1586\/eci.12.110","article-title":"Leptospirosis: current situation and trends of specific laboratory tests","volume":"9","author":"Schreier","year":"2013","journal-title":"Expert Rev Clin Immunol"},{"key":"10.1016\/j.jmii.2017.12.006_bib3","first-page":"65","article-title":"Leptospirosis in humans","volume":"387","author":"Haake","year":"2015","journal-title":"Curr Top Microbiol Immunol"},{"issue":"2","key":"10.1016\/j.jmii.2017.12.006_bib4","first-page":"281","article-title":"Leptospirosis: an emerging health problem in Thailand","volume":"36","author":"Tangkanakul","year":"2005","journal-title":"Southeast Asian Trop Med Publ Health"},{"issue":"2","key":"10.1016\/j.jmii.2017.12.006_bib5","doi-asserted-by":"crossref","first-page":"1","DOI":"10.59096\/osir.v7i2.263289","article-title":"Epidemiology of leptospirosis from Thai national disease surveillance system, 2003\u20132012","volume":"7","author":"Hinjoy","year":"2014","journal-title":"OSIR"},{"issue":"8","key":"10.1016\/j.jmii.2017.12.006_bib6","doi-asserted-by":"crossref","first-page":"8542","DOI":"10.3390\/ijerph110808542","article-title":"Human leptospirosis trends: northeast Thailand, 2001\u20132012","volume":"11","author":"Thipmontree","year":"2014","journal-title":"Int J Environ Res Publ Health"},{"issue":"12","key":"10.1016\/j.jmii.2017.12.006_bib7","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":"Bharti","year":"2003","journal-title":"Lancet Infect Dis"},{"key":"10.1016\/j.jmii.2017.12.006_bib8","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1186\/s12992-014-0061-0","article-title":"Globalization of leptospirosis through travel and migration","volume":"10","author":"Bandara","year":"2014","journal-title":"Global Health"},{"key":"10.1016\/j.jmii.2017.12.006_bib9","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1099\/00207713-49-1-231","article-title":"Genetic structure of the genus Leptospira by multilocus enzyme electrophoresis","volume":"49","author":"Letocart","year":"1999","journal-title":"Int J Syst Bacteriol"},{"key":"10.1016\/j.jmii.2017.12.006_bib10","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/j.vetmic.2009.03.012","article-title":"Leptospira and leptospirosis","volume":"140","author":"Adler","year":"2010","journal-title":"Vet Microbiol"},{"key":"10.1016\/j.jmii.2017.12.006_bib11","doi-asserted-by":"crossref","first-page":"120","DOI":"10.4172\/2155-9597.1000120","article-title":"LEPTOSPIRA: morphology, classification and pathogenesis","volume":"2","author":"Mohammed","year":"2011","journal-title":"J Bacteriol Parasitol"},{"key":"10.1016\/j.jmii.2017.12.006_bib12","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/j.cimid.2009.01.001","article-title":"Synthetic peptide issued from Hap1\/LipL32 for new early serodiagnosis of human leptospirosis","volume":"33","author":"Aviat","year":"2010","journal-title":"Comp Immunol Microbiol Infect Dis"},{"key":"10.1016\/j.jmii.2017.12.006_bib13","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/j.trstmh.2011.01.008","article-title":"Leptospirosis serodiagnosis by ELISA based on recombinant outer membrane protein","volume":"105","author":"Chalayon","year":"2011","journal-title":"Trans R Soc Trop Med Hyg"},{"key":"10.1016\/j.jmii.2017.12.006_bib14","first-page":"133","article-title":"LipL32, an outer membrane protein of Leptospira, as an antigen in a dipstick assay for diagnosis of leptospirosis","volume":"23","author":"Boonyod","year":"2005","journal-title":"Asian Pac J Allergy Immunol"},{"key":"10.1016\/j.jmii.2017.12.006_bib15","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1128\/JCM.40.3.480-489.2002","article-title":"Diagnosis of human leptospirosis by monoclonal antibody-based antigen detection in urine","volume":"40","author":"Saengjaruk","year":"2002","journal-title":"J Clin Microbiol"},{"key":"10.1016\/j.jmii.2017.12.006_bib16","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/j.vetmic.2005.05.002","article-title":"Evaluation of the recombinant LipL32 in enzyme-linked immunosorbent assay for the serodiagnosis of bovine leptospirosis","volume":"109","author":"Bomfim","year":"2005","journal-title":"Vet Microbiol"},{"key":"10.1016\/j.jmii.2017.12.006_bib17","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1179\/2047773213Y.0000000088","article-title":"Detection of LipL32-specific IgM by ELISA in sera of patients with a clinical diagnosis of leptospirosis","volume":"107","author":"Vedhagiri","year":"2013","journal-title":"Pathog Glob Health"},{"key":"10.1016\/j.jmii.2017.12.006_bib18","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1128\/CVI.00649-13","article-title":"Serodiagnosis of equine leptospirosis by enzyme-linked immunosorbent assay using four recombinant protein markers","volume":"21","author":"Ye","year":"2014","journal-title":"Clin Vaccine Immunol"},{"key":"10.1016\/j.jmii.2017.12.006_bib19","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/j.femsle.2005.01.007","article-title":"Polymerase chain reaction assay specific for pathogenic Leptospira based on the gene hap1 encoding the hemolysis-associated protein-1","volume":"243","author":"Branger","year":"2005","journal-title":"FEMS Microbiol Lett"},{"key":"10.1016\/j.jmii.2017.12.006_bib20","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/j.vaccine.2007.10.052","article-title":"Recombinant Mycobacterium bovis BCG expressing the LipL32 antigen of Leptospira interrogans protects hamsters from challenge","volume":"26","author":"Seixas","year":"2007","journal-title":"Vaccine"},{"key":"10.1016\/j.jmii.2017.12.006_bib21","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1128\/CVI.05720-11","article-title":"Protection against lethal leptospirosis after vaccination with LipL32 coupled or coadministered with the B subunit of Escherichia coli heat-labile enterotoxin","volume":"19","author":"Grassmann","year":"2012","journal-title":"Clin Vaccine Immunol"},{"key":"10.1016\/j.jmii.2017.12.006_bib22","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.jmii.2017.12.006_bib23","doi-asserted-by":"crossref","first-page":"526","DOI":"10.4014\/jmb.1408.08007","article-title":"Immunogenicity of a DNA and recombinant protein vaccine combining LipL32 and Loa22 for leptospirosis using chitosan as a delivery system","volume":"25","author":"Umthong","year":"2015","journal-title":"J Microbiol Biotechnol"},{"key":"10.1016\/j.jmii.2017.12.006_bib24","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1089\/hyb.2008.0056","article-title":"Monoclonal antibodies to LipL32 protect against heterologous Leptospira spp. challenge","volume":"27","author":"Maneewatch","year":"2008","journal-title":"Hybridoma (Larchmt)"},{"key":"10.1016\/j.jmii.2017.12.006_bib25","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1093\/protein\/gzp008","article-title":"Humanized-monoclonal antibody against heterologous Leptospira infection","volume":"22","author":"Maneewatch","year":"2009","journal-title":"Protein Eng Des Sel"},{"key":"10.1016\/j.jmii.2017.12.006_bib26","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1093\/protein\/gzu006","article-title":"Therapeutic epitopes of Leptospira LipL32 protein and their characteristics","volume":"27","author":"Maneewatch","year":"2014","journal-title":"Protein Eng Des Sel"},{"issue":"2","key":"10.1016\/j.jmii.2017.12.006_bib27","doi-asserted-by":"crossref","DOI":"10.16966\/2473-1846.114","article-title":"Therapeutic monoclonal antibodies and their engineered antibody fragments specific to LipL32 for passive immunotherapy of leptospirosis","volume":"2","author":"Maneewatchararangsri","year":"2016","journal-title":"J Emerg Dis Virol"},{"key":"10.1016\/j.jmii.2017.12.006_bib28","doi-asserted-by":"crossref","first-page":"1824","DOI":"10.1128\/jcm.26.9.1824-1830.1988","article-title":"Detection with monoclonal antibody of Salmonella typhi antigen 9 in specimens from patients","volume":"26","author":"Chaicumpa","year":"1988","journal-title":"J Clin Microbiol"},{"issue":"3","key":"10.1016\/j.jmii.2017.12.006_bib29","first-page":"576","article-title":"Development of enzyme-linked immunosorbent assay for human leptospirosis serodiagnosis using Leptospira secretome antigen","volume":"48","author":"Maneewatchararangsri","year":"2017","journal-title":"Southeast Asian J Trop Med Publ Health"},{"key":"10.1016\/j.jmii.2017.12.006_bib30","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1128\/JCM.41.3.1041-1047.2003","article-title":"Epitope-blocking enzyme-linked immunosorbent assays for the detection of serum antibodies to West Nile virus in multiple avian species","volume":"41","author":"Blitvich","year":"2003","journal-title":"J Clin Microbiol"},{"key":"10.1016\/j.jmii.2017.12.006_bib31","doi-asserted-by":"crossref","first-page":"4853","DOI":"10.1128\/IAI.73.8.4853-4863.2005","article-title":"Surfaceome of Leptospira spp","volume":"73","author":"Cullen","year":"2005","journal-title":"Infect Immun"},{"key":"10.1016\/j.jmii.2017.12.006_bib32","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"},{"key":"10.1016\/j.jmii.2017.12.006_bib33","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"},{"key":"10.1016\/j.jmii.2017.12.006_bib34","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1128\/iai.44.2.459-464.1984","article-title":"Interaction of leptospires with human polymorphonuclear neutrophils","volume":"44","author":"Wang","year":"1984","journal-title":"Infect Immun"},{"key":"10.1016\/j.jmii.2017.12.006_bib35","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"},{"key":"10.1016\/j.jmii.2017.12.006_bib36","doi-asserted-by":"crossref","first-page":"2063","DOI":"10.1128\/IAI.01643-07","article-title":"LipL32 is an extracellular matrix-interacting protein of Leptospira spp. and Pseudoalteromonas tunicata","volume":"76","author":"Hoke","year":"2008","journal-title":"Infect Immun"},{"key":"10.1016\/j.jmii.2017.12.006_bib37","doi-asserted-by":"crossref","first-page":"5528","DOI":"10.1128\/IAI.00546-09","article-title":"Leptospira interrogans binds to human cell surface receptors including proteoglycans","volume":"77","author":"Breiner","year":"2009","journal-title":"Infect Immun"},{"key":"10.1016\/j.jmii.2017.12.006_bib38","first-page":"283","article-title":"New insights into the pathogenicity of leptospires: evasion of host defences","volume":"33","author":"Cinco","year":"2010","journal-title":"New Microbiol"},{"key":"10.1016\/j.jmii.2017.12.006_bib39","doi-asserted-by":"crossref","first-page":"1413","DOI":"10.2217\/fmb.10.102","article-title":"Leptospira as an emerging pathogen: a review of its biology, pathogenesis and host immune responses","volume":"5","author":"Evangelista","year":"2010","journal-title":"Future Microbiol"},{"key":"10.1016\/j.jmii.2017.12.006_bib40","first-page":"317950","article-title":"Leptospira and inflammation","author":"Gon\u00e7alves-de-Albuquerque","year":"2012","journal-title":"Mediators Inflamm"},{"key":"10.1016\/j.jmii.2017.12.006_bib41","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"},{"key":"10.1016\/j.jmii.2017.12.006_bib42","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1016\/j.jmb.2009.02.038","article-title":"Crystal structure of LipL32, the most abundant surface protein of pathogenic Leptospira spp","volume":"387","author":"Vivian","year":"2009","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jmii.2017.12.006_bib43","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1111\/j.1472-765X.2009.02723.x","article-title":"Epitope mapping of pathogenic Leptospira LipL32","volume":"49","author":"Lottersburger","year":"2009","journal-title":"Lett Appl Microbiol"},{"key":"10.1016\/j.jmii.2017.12.006_bib44","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1128\/CVI.00405-09","article-title":"Identification of immunodominant B- and T-cell combined epitopes in outer membrane lipoproteins LipL32 and LipL21 of Leptospira interrogans","volume":"17","author":"Lin","year":"2010","journal-title":"Clin Vaccine Immunol"},{"key":"10.1016\/j.jmii.2017.12.006_bib45","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1089\/hyb.2006.033","article-title":"Monoclonal antibodies against LipL32, the major outer membrane protein of pathogenic Leptospira: production, characterization, and testing in diagnostic applications","volume":"26","author":"Fernandes","year":"2007","journal-title":"Hybridoma (Larchmt)"},{"key":"10.1016\/j.jmii.2017.12.006_bib46","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1128\/CVI.05622-11","article-title":"Analysis of multiple Leptospira interrogans serovar Canicola vaccine proteomes and identification of LipL32 as a biomarker for potency","volume":"19","author":"Humphryes","year":"2012","journal-title":"Clin Vaccine Immunol"},{"key":"10.1016\/j.jmii.2017.12.006_bib47","doi-asserted-by":"crossref","first-page":"3413","DOI":"10.1016\/j.vaccine.2011.02.084","article-title":"Recombinant LipL32 and LigA from Leptospira are unable to stimulate protective immunity against leptospirosis in the hamster model","volume":"29","author":"Deveson-Lucas","year":"2011","journal-title":"Vaccine"}],"container-title":["Journal of Microbiology, Immunology and Infection"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1684118218300264?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1684118218300264?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T13:25:10Z","timestamp":1761657910000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1684118218300264"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,2]]},"references-count":47,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2020,2]]}},"alternative-id":["S1684118218300264"],"URL":"https:\/\/doi.org\/10.1016\/j.jmii.2017.12.006","relation":{},"ISSN":["1684-1182"],"issn-type":[{"value":"1684-1182","type":"print"}],"subject":[],"published":{"date-parts":[[2020,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Immunodominance of LipL3293\u2013272 peptides revealed by leptospirosis sera and therapeutic monoclonal antibodies","name":"articletitle","label":"Article Title"},{"value":"Journal of Microbiology, Immunology and Infection","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmii.2017.12.006","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Taiwan Society of Microbiology. Published by Elsevier Taiwan LLC.","name":"copyright","label":"Copyright"}]}}