{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T23:48:47Z","timestamp":1792540127992,"version":"4.5.0"},"reference-count":47,"publisher":"American Society for Microbiology","issue":"11","license":[{"start":{"date-parts":[[2015,11,1]],"date-time":"2015-11-01T00:00:00Z","timestamp":1446336000000},"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":[[2015,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Leptospirosis is an emerging disease with an annual occurrence of over 1 million human cases worldwide. Pathogenic\n            <jats:named-content content-type=\"genus-species\">Leptospira<\/jats:named-content>\n            bacteria are maintained in zoonotic cycles involving a diverse array of mammals, with the capacity to survive outside the host in aquatic environments. Survival in the diverse environments encountered by\n            <jats:named-content content-type=\"genus-species\">Leptospira<\/jats:named-content>\n            likely requires various adaptive mechanisms. Little is known about\n            <jats:named-content content-type=\"genus-species\">Leptospira<\/jats:named-content>\n            outer membrane modification systems, which may contribute to the capacity of these bacteria to successfully inhabit and colonize diverse environments and animal hosts.\n            <jats:named-content content-type=\"genus-species\">Leptospira<\/jats:named-content>\n            bacteria carry two genes annotated as UDP-3-\n            <jats:italic>O<\/jats:italic>\n            -[3-hydroxymyristoyl] glucosamine\n            <jats:italic>N<\/jats:italic>\n            -acyltransferase genes (la0512 and la4326 [\n            <jats:italic>lpxD1<\/jats:italic>\n            and\n            <jats:italic>lpxD2<\/jats:italic>\n            ]) that in other bacteria are involved in the early steps of biosynthesis of lipid A, the membrane lipid anchor of lipopolysaccharide. Inactivation of only one of these genes, la0512\/\n            <jats:italic>lpxD1<\/jats:italic>\n            , imparted sensitivity to the host physiological temperature (37\u00b0C) and rendered the bacteria avirulent in an animal infection model. Polymyxin B sensitivity assays revealed compromised outer membrane integrity in the\n            <jats:italic>lpxD1<\/jats:italic>\n            mutant at host physiological temperature, but structural analysis of lipid A in the mutant revealed only minor changes in the lipid A moiety compared to that found in the wild-type strain. In accordance with this, an\n            <jats:italic>in trans<\/jats:italic>\n            complementation restored the phenotypes to a level comparable to that of the wild-type strain. These results suggest that the gene annotated as\n            <jats:italic>lpxD1<\/jats:italic>\n            in\n            <jats:named-content content-type=\"genus-species\">Leptospira interrogans<\/jats:named-content>\n            plays an important role in temperature adaptation and virulence in the animal infection model.\n          <\/jats:p>","DOI":"10.1128\/iai.00897-15","type":"journal-article","created":{"date-parts":[[2015,8,17]],"date-time":"2015-08-17T22:11:24Z","timestamp":1439849484000},"page":"4314-4321","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":33,"title":["<i>Leptospira interrogans lpxD<\/i>\n            Homologue Is Required for Thermal Acclimatization and Virulence"],"prefix":"10.1128","volume":"83","author":[{"given":"Azad","family":"Eshghi","sequence":"first","affiliation":[{"name":"Institut Pasteur, Biology of Spirochetes Unit, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeremy","family":"Henderson","sequence":"additional","affiliation":[{"name":"Department of Molecular Biosciences, University of Texas at Austin, Austin, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. 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