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Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11: XN6P4

]

NCBI PubMed ID: 17943705
Publication DOI: 10.1002/chem.200701165
Publisher: Vch Verlagsgesellschaft
Correspondence: gjboons

ccrc.uga.edu
Institutions: Complex Carbohydrate Research Center, The University of Georgia, Athens, USA

Differences in the pattern and chemical nature of fatty acids of lipid A of Neisseria meningitidis lipooligosaccharides (LOS) and Escherichia coli lipopolysaccharides (LPS) may account for differences in inflammatory properties. Furthermore, there are indications that dimeric 3-deoxy-D-manno-oct-2-ulosonic acid (KDO) moieties of LOS and LPS enhance biological activities. Heterogeneity in the structure of lipid A and possible contaminations with other inflammatory components have made it difficult to confirm these observations. To address these problems, a highly convergent approach for the synthesis of a lipid A derivative containing KDO has been developed, which relies on the ability to selectively remove or unmask in a sequential manner an isopropylidene acetal, 9-fluorenylmethoxycarbonyl (Fmoc), allyloxycarbonate (Alloc), azide, and thexyldimethylsilyl (TDS) ether. The strategy was employed for the synthesis of N. meningitidis lipid A containing KDO (3). Mouse macrophages were exposed to the synthetic compound and its parent LOS, E. coli lipid A (2), and a hybrid derivative (4) that has the asymmetrical acylation pattern of E. coli lipid A, but the shorter lipids of meningococcal lipid A. The resulting supernatants were examined for tumor necrosis factor alpha (TNF-α) and interferon beta (IFN-β) production. The lipid A derivative containing KDO was much more active than lipid A alone and just slightly less active than its parent LOS, indicating that one KDO moiety is sufficient for full activity of TNF-α and IFN-β induction. The lipid A of N. meningitidis was a significantly more potent inducer of TNF-α and IFN-β than E. coli lipid A, which is due to a number of shorter fatty acids. The compounds did not demonstrate a bias towards a MyD88- or TRIF-dependent response

carbohydrates, Oligosaccharides, immunology, glycosylation

Structure type: oligomer
Location inside paper: Fig. 1, structure 4
Compound class: glycolipid
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_534864

Biological activity: compound is a potent inducer of TNF-a and IFN-b

Related record ID(s): 47801, 47802, 47803
NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases

There is only one chemically distinct structure:

CCCCCCCCCCCC(=O)O[C@H](CCCCCCCCCCC)CC(=O)N[C@H]1[C@H](OC[C@H]2O[C@H](OP(=O)(O)O)[C@H](NC(=O)C[C@H](O)CCCCCCCCCCC)[C@@H](OC(=O)C[C@H](O)CCCCCCCCC)[C@@H]2O)O[C@H](CO)[C@@H](OP(=O)(O)O)[C@@H]1OC(=O)C[C@@H](CCCCCCCCC)OC(=O)CCCCCCCCCCC

SVG MW SMILES 3D mol Ionize