{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T18:53:29Z","timestamp":1793904809133,"version":"4.8.0"},"reference-count":42,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2000,4,1]],"date-time":"2000-04-01T00:00:00Z","timestamp":954547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2000,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    We report the cloning of the gene encoding the 32-kDa lipoprotein, designated LipL32, the most prominent protein in the leptospiral protein profile. We obtained the N-terminal amino acid sequence of a staphylococcal V8 proteolytic-digest fragment to design an oligonucleotide probe. A Lambda-Zap II library containing\n                    <jats:italic>Eco<\/jats:italic>\n                    RI fragments of\n                    <jats:italic>Leptospira kirschneri<\/jats:italic>\n                    DNA was screened, and a 5.0-kb DNA fragment which contained the entire structural\n                    <jats:italic>lipL32<\/jats:italic>\n                    gene was identified. Several lines of evidence indicate that LipL32 is lipid modified in a manner similar to that of other procaryotic lipoproteins. The deduced amino acid sequence of LipL32 would encode a 272-amino-acid polypeptide with a 19-amino-acid signal peptide, followed by a lipoprotein signal peptidase cleavage site. LipL32 is intrinsically labeled during incubation of\n                    <jats:italic>L. kirschneri<\/jats:italic>\n                    in media containing [\n                    <jats:sup>3<\/jats:sup>\n                    H]palmitate. The linkage of palmitate and the amino-terminal cysteine of LipL32 is acid labile. LipL32 is completely solubilized by Triton X-114 extraction of\n                    <jats:italic>L. kirschneri<\/jats:italic>\n                    ; phase separation results in partitioning of LipL32 exclusively into the hydrophobic, detergent phase, indicating that it is a component of the leptospiral outer membrane. CaCl\n                    <jats:sub>2<\/jats:sub>\n                    (20 mM) must be present during phase separation for recovery of LipL32. LipL32 is expressed not only during cultivation but also during mammalian infection. Immunohistochemistry demonstrated intense LipL32 reactivity with\n                    <jats:italic>L. kirschneri<\/jats:italic>\n                    infecting proximal tubules of hamster kidneys. LipL32 is also a prominent immunogen during human leptospirosis. The sequence and expression of LipL32 is highly conserved among pathogenic\n                    <jats:italic>Leptospira<\/jats:italic>\n                    species. These findings indicate that LipL32 may be important in the pathogenesis, diagnosis, and prevention of leptospirosis.\n                  <\/jats:p>","DOI":"10.1128\/iai.68.4.2276-2285.2000","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T06:01:19Z","timestamp":1027749679000},"page":"2276-2285","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":339,"title":["The Leptospiral Major Outer Membrane Protein LipL32 Is a Lipoprotein Expressed during Mammalian Infection"],"prefix":"10.1128","volume":"68","author":[{"given":"David A.","family":"Haake","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Division of Infectious Diseases, Veterans Affairs Greater Los Angeles Healthcare System, Los Angeles, California 900731;"},{"name":"<!--label omitted: 2-->Department of Medicine, UCLA School of Medicine, Los Angeles, California 900952;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Garlo","family":"Chao","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Division of Infectious Diseases, Veterans Affairs Greater Los Angeles Healthcare System, Los Angeles, California 900731;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard L.","family":"Zuerner","sequence":"additional","affiliation":[{"name":"<!--label omitted: 3-->National Animal Disease Center, Agricultural Research Service, U.S. Department of Agriculture, Ames, Iowa 500103;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeanne K.","family":"Barnett","sequence":"additional","affiliation":[{"name":"<!--label omitted: 4-->Biology Department, University of Southern Indiana, Evansville, Indiana 477124; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dean","family":"Barnett","sequence":"additional","affiliation":[{"name":"<!--label omitted: 4-->Biology Department, University of Southern Indiana, Evansville, Indiana 477124; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mary","family":"Mazel","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Division of Infectious Diseases, Veterans Affairs Greater Los Angeles Healthcare System, Los Angeles, California 900731;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James","family":"Matsunaga","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Division of Infectious Diseases, Veterans Affairs Greater Los Angeles Healthcare System, Los Angeles, California 900731;"},{"name":"<!--label omitted: 2-->Department of Medicine, UCLA School of Medicine, Los Angeles, California 900952;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul N.","family":"Levett","sequence":"additional","affiliation":[{"name":"<!--label omitted: 5-->University of the West Indies School of Clinical Medicine and Research, Barbados5"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carole A.","family":"Bolin","sequence":"additional","affiliation":[{"name":"<!--label omitted: 3-->National Animal Disease Center, Agricultural Research Service, U.S. Department of Agriculture, Ames, Iowa 500103;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/25.17.3389"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.5.6.968-975.1972"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.67.2.853-861.1999"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.1989.tb00194.x"},{"key":"e_1_3_2_6_2","doi-asserted-by":"crossref","first-page":"1639","DOI":"10.2460\/ajvr.1991.52.10.1639","article-title":"Effect of vaccination with a monovalent Leptospira interrogans serovar hardjo type hardjo-bovis vaccine on type hardjo-bovis infection of cattle","volume":"52","author":"Bolin C. 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