{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T14:43:07Z","timestamp":1791902587202,"version":"4.3.4"},"reference-count":66,"publisher":"American Society for Microbiology","issue":"11","license":[{"start":{"date-parts":[[2012,11,1]],"date-time":"2012-11-01T00:00:00Z","timestamp":1351728000000},"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":[[2012,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The interaction of the immune system with\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Neisseria<\/jats:named-content>\n            commensals remains poorly understood. We have previously shown that phosphoethanolamine on the lipid A portion of lipooligosaccharide (LOS) plays an important role in Toll-like receptor 4 (TLR4) signaling. For pathogenic\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Neisseria<\/jats:named-content>\n            , phosphoethanolamine is added to lipid A by the phosphoethanolamine transferase specific for lipid A, which is encoded by\n            <jats:italic>lptA<\/jats:italic>\n            . Here, we report that Southern hybridizations and bioinformatics analyses of genomic sequences from all eight commensal\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Neisseria<\/jats:named-content>\n            species confirmed that\n            <jats:italic>lptA<\/jats:italic>\n            was absent in 15 of 17 strains examined but was present in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">N. lactamica<\/jats:named-content>\n            . Mass spectrometry of lipid A and intact LOS revealed the lack of both pyrophosphorylation and phosphoethanolaminylation in lipid A of commensal species lacking\n            <jats:italic>lptA<\/jats:italic>\n            . Inflammatory signaling in human THP-1 monocytic cells was much greater with pathogenic than with commensal\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Neisseria<\/jats:named-content>\n            strains that lacked\n            <jats:italic>lptA<\/jats:italic>\n            , and greater sensitivity to polymyxin B was consistent with the absence of phosphoethanolamine. Unlike the other commensals, whole bacteria of two\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">N. lactamica<\/jats:named-content>\n            commensal strains had low inflammatory potential, whereas their lipid A had high-level pyrophosphorylation and phosphoethanolaminylation and induced high-level inflammatory signaling, supporting previous studies indicating that this species uses mechanisms other than altering lipid A to support commensalism. A meningococcal\n            <jats:italic>lptA<\/jats:italic>\n            deletion mutant had reduced inflammatory potential, further illustrating the importance of lipid A pyrophosphorylation and phosphoethanolaminylation in the bioactivity of LOS. Overall, our results indicate that lack of pyrophosphorylation and phosphoethanolaminylation of lipid A contributes to the immune privilege of most commensal\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Neisseria<\/jats:named-content>\n            strains by reducing the inflammatory potential of LOS.\n          <\/jats:p>","DOI":"10.1128\/iai.00506-12","type":"journal-article","created":{"date-parts":[[2012,9,5]],"date-time":"2012-09-05T06:48:28Z","timestamp":1346827708000},"page":"4014-4026","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":53,"title":["Lack of Lipid A Pyrophosphorylation and Functional\n            <i>lptA<\/i>\n            Reduces Inflammation by Neisseria Commensals"],"prefix":"10.1128","volume":"80","author":[{"given":"Constance M.","family":"John","sequence":"first","affiliation":[{"name":"Center for Immunochemistry, Veterans Affairs Medical Center, San Francisco, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mingfeng","family":"Liu","sequence":"additional","affiliation":[{"name":"Center for Immunochemistry, Veterans Affairs Medical Center, San Francisco, California, USA"},{"name":"Department of Laboratory Medicine, University of California, San Francisco, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nancy J.","family":"Phillips","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Chemistry, University of California, San Francisco, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhijie","family":"Yang","sequence":"additional","affiliation":[{"name":"Center for Immunochemistry, Veterans Affairs Medical Center, San Francisco, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Courtney R.","family":"Funk","sequence":"additional","affiliation":[{"name":"Center for Immunochemistry, Veterans Affairs Medical Center, San Francisco, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lindsey I.","family":"Zimmerman","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J. 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