{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T08:06:36Z","timestamp":1791273996237,"version":"4.1.0"},"reference-count":42,"publisher":"SAGE Publications","issue":"6","license":[{"start":{"date-parts":[[2007,12,1]],"date-time":"2007-12-01T00:00:00Z","timestamp":1196467200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Endotoxin Research"],"published-print":{"date-parts":[[2007,12]]},"abstract":"<jats:p>\n                    Meningococcal endotoxin is the major contributor to the pathogenesis of fulminant sepsis and meningitis of meningococcal disease and is a potent activator of the MyD88-dependent and MyD88-independent pathways via the MD-2\/TLR4 receptor. To understand better the biological properties of meningococcal endotoxin that initiates these events, the physicochemical structure of Neisseria meningitidis lipopoly(oligo)saccharide (LOS) of the serogroup B wild-type strain NMB (NeuNAc-Gal\u03b2-GlcNAc-Gal\u03b2-Glc\u03b2-Hep\n                    <jats:sub>2<\/jats:sub>\n                    (GlcNAc,Glc\u03b1)PEA-Kdo\n                    <jats:sub>2<\/jats:sub>\n                    -lipid A, 1,4\u2032-bisphosphorylated \u00b1 PEA, PEtN) and the genetically-defined mutants ( gmhB, Kdo\n                    <jats:sub>2<\/jats:sub>\n                    -lipid A; kdtA, meningococcal lipid A; gmhB\u2014lpxL1, Kdo\n                    <jats:sub>2<\/jats:sub>\n                    penta-acylated lipid A and NMB\u2014 lpx1, penta-acylated meningococcal LOS) were assessed in relation to bioactivity. Confirming previous work, Kdo\n                    <jats:sub>2<\/jats:sub>\n                    -lipid A was the minimal structure required for optimal activation of the MD-2\/TLR4 pathway of human macrophages. Meningococcal lipid A alone was a very weak agonist in stimulating human macrophages, even at high doses. Penta-acylated LOS structures demonstrated a moderate reduction in TLR4\/MyD88-dependent signaling and a dramatic decrease in TLR4-TRIF-dependent signaling. For a better understanding of these results, we have performed an analysis of physicochemical parameters of the LOS structures such as the gel-to-liquid crystalline phase transition of the acyl chains, the inclination angle of the diglucosamine backbone with respect to the membrane surface, and the aggregate structure, and have found a very significant correlation of these parameters with biological activities extending our concept of endotoxicity.\n                  <\/jats:p>","DOI":"10.1177\/0968051907084435","type":"journal-article","created":{"date-parts":[[2008,1,8]],"date-time":"2008-01-08T10:29:58Z","timestamp":1199788198000},"page":"343-357","source":"Crossref","is-referenced-by-count":18,"title":["Physicochemical characterization and biological activity of                 lipooligosaccharides and lipid A from\n                    <i>Neisseria meningitidis<\/i>"],"prefix":"10.1177","volume":"13","author":[{"given":"Susu M.","family":"Zughaier","sequence":"first","affiliation":[{"name":"Division of Infectious Diseases, Department of Medicine, Emory University                         School of Medicine, Atlanta, Georgia, USA,"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Buko","family":"Lindner","sequence":"additional","affiliation":[{"name":"Forschungszentrum Borstel, Leibniz-Zentrum f\u00fcr Medizin und                         Biowissenschaften, Borstel, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J\u00f6rg","family":"Howe","sequence":"additional","affiliation":[{"name":"Forschungszentrum Borstel, Leibniz-Zentrum f\u00fcr Medizin und                         Biowissenschaften, Borstel, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick","family":"Garidel","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Physikalische Chemie,                         Martin-Luther-Universit\u00e4t Halle-Wittenberg, Halle\/Saale,                     Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michel H.J.","family":"Koch","sequence":"additional","affiliation":[{"name":"European Molecular Biology Laboratory c\/o DESY, Hamburg Outstation,                         Hamburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Klaus","family":"Brandenburg","sequence":"additional","affiliation":[{"name":"Forschungszentrum Borstel, Leibniz-Zentrum f\u00fcr Medizin und                         Biowissenschaften, Borstel, Germany,"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David S.","family":"Stephens","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, Department of Medicine, Emory University                         School of Medicine, Atlanta, Georgia, USA, Laboratories of Microbial                         Pathogenesis, Department of Veterans Affairs Medical Center, Atlanta,                         Georgia, 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