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Chemical Compound Review

LMSL01040001     [(2R,3S,5S)-5-hydroxy-6- [[(2R,3S,5S)-6...

Synonyms: AC1NY9KN
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Disease relevance of Lipid IVA


High impact information on Lipid IVA

  • Scavenger-receptor ligands inhibit lipid IVA binding to, and metabolism by, RAW cells, and lipid IVA binds to type I and type II bovine scavenger receptors on transfected Chinese hamster ovary cells [4].
  • We report here that lipid IVA binding and subsequent metabolism to a less active form by macrophage-like RAW 264.7 cells is mediated by the macrophage scavenger receptor [4].
  • Coincubation with lipid IVA inhibited TNF release induced by Rc LPS or lipid A, but not by phorbol ester [5].
  • To determine whether the species specificity of these LPS antagonists occurred as a result of interactions with CD14, the effects of lipid IVA and RSLA were examined by using human, mouse, and hamster cell lines transfected with murine or human CD14 cDNA expression vectors [1].
  • In contrast, lipid IVA activated murine phagocytes, whereas RSLA was an LPS antagonist [1].

Chemical compound and disease context of Lipid IVA

  • An autoradiographic assay applicable to colonies immobilized on filter paper was developed for obtaining temperature-sensitive mutants of Escherichia coli defective in the transfer of 3-deoxy-D-manno-octulosonic acid (KDO) from CMP-KDO to a tetraacyldisaccharide 1,4'-bisphosphate precursor of lipid A, designated lipid IVA [6].
  • Although the lipid A domain of LPS appears to be responsible for the toxicity of endotoxin, lipid A from the photosynthetic bacterium Rhodobacter sphaeroides (RSLA) and a disaccharide precursor of lipid A from enteric bacteria, termed lipid IVA, have little activity on human cells [3].
  • Comparable E. coli extracts cannot transfer laurate from lauroyl-ACP to lipid IVA, only to (Kdo)2-lipid IVA (K. A. Brozek, and C. R. H. Raetz, J. Biol. Chem. 265:15410-15417, 1990) [7].

Biological context of Lipid IVA

  • These transfectants displayed sensitivities to lipid IVA and RSLA that reflected the sensitivities of macrophages of similar genotype (species) and were independent of the source of CD14 cDNA [1].
  • Since ELPS is particulate and lipid IVA is a fine dispersion, the identity of the binding site may depend on the physical state of the LPS [8].

Anatomical context of Lipid IVA


Associations of Lipid IVA with other chemical compounds

  • Lipid A, MPLA, lipid IVA, and lipid X exhibited decreasing capacities to stimulate production of TNF in whole blood, respectively [5].
  • P. aeruginosa extracts do not utilize myristoyl- or R-3-hydroxymyristoyl-ACP instead of lauroyl-ACP to acylate lipid IVA [7].

Gene context of Lipid IVA

  • We then tested the effects of lipid IVA and Rhodobacter sphaeroides lipid A, compounds that function as endotoxin inhibitors in human cells by interacting with a molecule thought to be a CD14-dependent LPS signal transducer [10].
  • This latter agonist activity appears to be unique to mLPS, since two previously documented LPS antagonists, Rhodobacter sphaeroides diphosphoryl lipid A and synthetic lipid IVA, did not induce MIP-1 alpha and MIP-1 beta secretion [11].
  • Furthermore, synthetic lipid IVA was an antagonist of MIP-1 alpha and MIP-1 beta induction by mLPS [11].
  • In previous studies, we cloned the gene (kdtA) encoding the E. coli Kdo transferase and demonstrated that homogeneous preparations of KdtA polypeptide catalyzed the attachment of both Kdo groups to the precursor, lipid IVA [9].
  • Both lipid IVA and R. sphaeroides lipid A inhibited the effects of LPS and LAM in THP-1 cells [10].

Analytical, diagnostic and therapeutic context of Lipid IVA


  1. CD14 enhances cellular responses to endotoxin without imparting ligand-specific recognition. Delude, R.L., Savedra, R., Zhao, H., Thieringer, R., Yamamoto, S., Fenton, M.J., Golenbock, D.T. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  2. Inhibition of lipopolysaccharide biosynthesis and cell growth following inactivation of the kdtA gene in Escherichia coli. Belunis, C.J., Clementz, T., Carty, S.M., Raetz, C.R. J. Biol. Chem. (1995) [Pubmed]
  3. Lipid A-like molecules that antagonize the effects of endotoxins on human monocytes. Golenbock, D.T., Hampton, R.Y., Qureshi, N., Takayama, K., Raetz, C.R. J. Biol. Chem. (1991) [Pubmed]
  4. Recognition and plasma clearance of endotoxin by scavenger receptors. Hampton, R.Y., Golenbock, D.T., Penman, M., Krieger, M., Raetz, C.R. Nature (1991) [Pubmed]
  5. Lipid IVA inhibits synthesis and release of tumor necrosis factor induced by lipopolysaccharide in human whole blood ex vivo. Kovach, N.L., Yee, E., Munford, R.S., Raetz, C.R., Harlan, J.M. J. Exp. Med. (1990) [Pubmed]
  6. A gene coding for 3-deoxy-D-manno-octulosonic-acid transferase in Escherichia coli. Identification, mapping, cloning, and sequencing. Clementz, T., Raetz, C.R. J. Biol. Chem. (1991) [Pubmed]
  7. Endotoxin biosynthesis in Pseudomonas aeruginosa: enzymatic incorporation of laurate before 3-deoxy-D-manno-octulosonate. Mohan, S., Raetz, C.R. J. Bacteriol. (1994) [Pubmed]
  8. Human phagocytes have multiple lipid A-binding sites. Golenbock, D.T., Hampton, R.Y., Raetz, C.R., Wright, S.D. Infect. Immun. (1990) [Pubmed]
  9. A mono-functional 3-deoxy-D-manno-octulosonic acid (Kdo) transferase and a Kdo kinase in extracts of Haemophilus influenzae. White, K.A., Kaltashov, I.A., Cotter, R.J., Raetz, C.R. J. Biol. Chem. (1997) [Pubmed]
  10. Mycobacterial lipoarabinomannan recognition requires a receptor that shares components of the endotoxin signaling system. Savedra, R., Delude, R.L., Ingalls, R.R., Fenton, M.J., Golenbock, D.T. J. Immunol. (1996) [Pubmed]
  11. Lipopolysaccharide from an Escherichia coli htrB msbB mutant induces high levels of MIP-1 alpha and MIP-1 beta secretion without inducing TNF-alpha and IL-1 beta. Hone, D.M., Powell, J., Crowley, R.W., Maneval, D., Lewis, G.K. J. Hum. Virol. (1998) [Pubmed]
  12. Aggregation behavior of lipid IVA in aqueous solutions at physiological pH. 1: Simple buffer solutions. Hofer, M., Hampton, R.Y., Raetz, C.R., Yu, H. Chem. Phys. Lipids (1991) [Pubmed]
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