Isolation of heptadepsin, a novel bacterial cyclic depsipeptide that inhibits lipopolysaccharide activity

Chemistry and Biology

Volumn 11, Issue 8, 2004, Pages 1059-1070

  Ohno, Osamu ^a   Ikeda, Yoko ^b   Sawa, Ryuichi ^b   Igarashi, Masayuki ^b   Kinoshita, Naoko ^b   Suzuki, Yoshikazu ^a   Miyake, Kensuke ^c   Umezawa, Kazuo ^a  

^a KEIO UNIVERSITY   (Japan)

^b INSTITUTE OF MICROBIAL CHEMISTRY   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CD14 ANTIGEN; CELL SURFACE RECEPTOR; DEPSIPEPTIDE; HEPTADEPSIN, PAENIBACILLUS; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LIGAND; LIPOPOLYSACCHARIDE; PACLITAXEL; TLR4 PROTEIN, MOUSE; TOLL LIKE RECEPTOR 4;

ANIMAL; ARTICLE; CELL ADHESION; CELL CULTURE; CELL PROLIFERATION; CHEMICAL STRUCTURE; CHEMISTRY; CYTOLOGY; DRUG ANTAGONISM; DRUG EFFECT; EPITHELIUM CELL; GENE EXPRESSION REGULATION; GENETICS; HUMAN; ISOLATION AND PURIFICATION; LEUKEMIA; METABOLISM; MOUSE; PATHOLOGY; SIGNAL TRANSDUCTION;

ANIMALS; ANTIGENS, CD14; CELL ADHESION; CELL PROLIFERATION; CELLS, CULTURED; DEPSIPEPTIDES; EPITHELIAL CELLS; GENE EXPRESSION REGULATION; HUMANS; LEUKEMIA; LIGANDS; LIPOPOLYSACCHARIDES; MICE; MOLECULAR STRUCTURE; NF-KAPPA B; PACLITAXEL; RECEPTORS, CELL SURFACE; SIGNAL TRANSDUCTION; TOLL-LIKE RECEPTOR 4;

BACTERIA (MICROORGANISMS); PAENIBACILLUS; PAENIBACILLUS SP.;

EID: 4344714471     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2004.05.016     Document Type: Article

References (58)

1. Hill G.E., Whitten C.W. The role of the vascular endothelium in inflammatory syndromes, atherogenesis, and the propagation of disease. J. Cardiothorac. Vasc. Anesth. 11:1997;316-321
2. Ross R. Cell biology of atherosclerosis. Annu. Rev. Physiol. 57:1995;791-804
3. Gibbons G.H., Dzau V.J. Molecular therapies for vascular diseases. Science. 272:1996;689-693
4. Stad R.K., Buurman W.A. Current views on structure and function of endothelial adhesion molecules. Cell Adhes. Commun. 2:1994;261-268
5. Raetz C.R., Whitfield C. Lipopolysaccharide endotoxins. Annu. Rev. Biochem. 71:2002;635-700
6. Jirik F.R., Podor T.J., Hirano T., Kishimoto T., Loskutoff D.J., Carson D.A., Lotz M. Bacterial lipopolysaccharide and inflammatory mediators augment IL-6 secretion by human endothelial cells. J. Immunol. 142:1989;144-147
7. Zhao B., Bowden R.A., Stavchansky S.A., Bowman P.D. Human endothelial cell response to gram-negative lipopolysaccharide assessed with cDNA microarrays. Am. J. Physiol. Cell Physiol. 281:2001;C1587-C1595
8. Libby P., Ordovas J.M., Auger K.R., Robbins A.H., Birinyi L.K., Dinarello C.A. Endotoxin and tumor necrosis factor induce interleukin-1 gene expression in adult human vascular endothelial cells. Am. J. Pathol. 124:1986;179-185
9. Jersmann H.P., Hii C.S., Ferrante J.V., Ferrante A. Bacterial lipopolysaccharide and tumor necrosis factor α synergistically increase expression of human endothelial adhesion molecules through activation of NF-κB and p38 mitogen-activated protein kinase signaling pathways. Infect. Immun. 69:2001;1273-1279
10. Colucci M., Balconi G., Lorenzet R., Pietra A., Locati D., Donati M.B., Semeraro N. Cultured human endothelial cells generate tissue factor in response to endotoxin. J. Clin. Invest. 71:1983;1893-1896
11. Chow J.C., Young D.W., Golenbock D.T., Christ W.J., Gusovsky F. Toll-like receptor-4 mediates lipopolysaccharide-induced signal transduction. J. Biol. Chem. 274:1999;10689-10692
12. Poltorak A., He X., Smirnova I., Liu M.Y., Van Huffel C., Du X., Birdwell D., Alejos E., Silva M., Galanos C., et al. Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice mutations in Tlr4 gene. Science. 282:1998;2085-2088
13. Qureshi S.T., Lariviere L., Leveque G., Clermont S., Moore K.J., Gros P., Malo D. Endotoxin-tolerant mice have mutations in Toll-like receptor 4 (Tlr4). J. Exp. Med. 189:1999;615-625
14. van de Stolpe A., van der Saag P.T. Intercellular adhesion molecule-1. J. Mol. Med. 74:1996;13-33
15. Rice G.E., Munro J.M., Bevilacqua M.P. Inducible cell adhesion molecule 110 (INCAM-110) is an endothelial receptor for lymphocytes. A CD11/CD18-independent adhesion mechanism. J. Exp. Med. 171:1990;1369-1374
16. Tedder T.F., Steeber D.A., Chen A., Engel P. The selectins vascular adhesion molecules. FASEB J. 9:1995;866-873
17. Risau W. Differentiation of endothelium. FASEB J. 9:1995;926-933
18. Ogura Y., Bonen D.K., Inohara N., Nicolae D.L., Chen F.F., Ramos R., Britton H., Moran T., Karaliuskas R., Duerr R.H., et al. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease. Nature. 411:2001;603-606
19. Hugot J.P., Chamaillard M., Zouali H., Lesage S., Cezard J.P., Belaiche J., Almer S., Tysk C., O'Morain C.A., Gassull M., et al. Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease. Nature. 411:2001;599-603
20. Holt S.C., Kesavalu L., Walker S., Genco C.A. Virulence factors of Porphyromonas gingivalis. Periodontol. 2000 20:2000;168-238
21. Haffajee A.D., Socransky S.S. Microbial etiological agents of destructive periodontal diseases. Periodontol. 2000 5:2000;78-111
22. Foster C.A., Dreyfuss M., Mandak B., Meingassner J.G., Naegeli H.U., Nussbaumer A., Oberer L., Scheel G., Swoboda E.M. Pharmacological modulation of endothelial cell-associated adhesion molecule expression implications for future treatment of dermatological diseases. J. Dermatol. 21:1994;847-854
23. Hommel U., Weber H.P., Oberer L., Naegeli H.U., Oberhauser B., Foster C.A. The 3D-structure of a natural inhibitor of cell adhesion molecule expression. FEBS Lett. 379:1996;69-73
24. Sakaguchi S. A new method for the colorimetric determination of arginine. J. Biochem. (Tokyo). 37:1950;231-236
25. Jepson B.J., Smith I. "Multiple dipping" procedures in paper chromatography a specific test for hydroxyl-proline. Nature. 172:1953;1100-1101
26. Kajimura Y., Kaneda M. Fusaricidin A, a new depsipeptide antibiotic produced by Bacillus polymyxa KT-8. Taxonomy, fermentation, isolation, structure elucidation and biological activity. J. Antibiot. (Tokyo). 49:1996;129-135
27. He H., Shen B., Korshalla J., Carter G.T. Circulocins, new antibacterial lipopeptides from Bacillus circulans, J2154. Tetrahedron. 57:2001;1189-1195
28. Ding A.H., Porteu F., Sanchez E., Nathan C.F. Shared actions of endotoxin and taxol on TNF receptors and TNF release. Science. 248:1990;370-372
29. Perera P.Y., Qureshi N., Vogel S.N. Paclitaxel (Taxol)-induced NF-κB translocation in murine macrophages. Infect. Immun. 64:1996;878-884
30. Kawasaki K., Akashi S., Shimazu R., Yoshida T., Miyake K., Nishijima M. Mouse toll-like receptor 4.MD-2 complex mediates lipopolysaccharide-mimetic signal transduction by Taxol. J. Biol. Chem. 275:2000;2251-2254
31. Kawasaki K., Akashi S., Shimazu R., Yoshida T., Miyake K., Nishijima M. Involvement of TLR4/MD-2 complex in species-specific lipopolysaccharide-mimetic signal transduction by Taxol. J. Endotoxin Res. 7:2001;232-236
32. Kawasaki K., Nogawa H., Nishijima M. Identification of mouse MD-2 residues important for forming the cell surface TLR4-MD-2 complex recognized by anti-TLR4-MD-2 antibodies, and for conferring LPS and taxol responsiveness on mouse TLR4 by alanine-scanning mutagenesis. J. Immunol. 170:2003;413-420
33. Kadrmas J.L., Raetz C.R. Enzymatic synthesis of lipopolysaccharide in Escherichia coli. Purification and properties of heptosyltransferase I. J. Biol. Chem. 273:1998;2799-2807
34. Morath S., Geyer A., Spreitzer I., Hermann C., Hartung T. Structural decomposition and heterogeneity of commercial lipoteichoic acid preparations. Infect. Immun. 70:2002;938-944
35. Konz D., Doekel S., Marahiel M.A. Molecular and biochemical characterization of the protein template controlling biosynthesis of the lipopeptide lichenysin. J. Bacteriol. 181:1999;133-140
36. Arima K., Kakinuma A., Tamura G. Surfactin, a crystalline peptidelipid surfactant produced by Bacillus subtilis isolation, characterization and its inhibition of fibrin clot formation. Biochem. Biophys. Res. Commun. 31:1968;488-494
37. Yakimov M.M., Timmis K.N., Wray V., Fredrickson H.L. Characterization of a new lipopeptide surfactant produced by thermotolerant and halotolerant subsurface Bacillus licheniformis BAS50. Appl. Environ. Microbiol. 61:1995;1706-1713
38. Quentin M.J., Besson F., Peypoux F., Michel G. Action of peptidolipidic antibiotics of the iturin group on erythrocytes. Effect of some lipids on hemolysis. Biochim. Biophys. Acta. 684:1982;207-211
39. Peypoux F., Besson F., Michel G., Delcambe L. Structure of bacillomycin D, a new antibiotic of the iturin group. Eur. J. Biochem. 118:1981;323-327
40. Nishikiori T., Naganawa H., Muraoka Y., Aoyagi T., Umezawa H. Plipastatins new inhibitors of phospholipase A2, produced by Bacillus cereus BMG302-fF67. III. Structural elucidation of plipastatins. J. Antibiot. (Tokyo). 39:1986;755-761
41. Suzuki T., Hayashi K., Fujikawa K. Studies on the chemical structure of colistin. III. Enzymatic hydrolysis of colistin A. J. Biochem. (Tokyo). 54:1963;412-418
42. Puar M.S. Carbon-13 NMR studies of EM 49 and related octapeptins. J. Antibiot. (Tokyo). 33:1980;760-763
43. Rifkind D. Prevention by polymyxin B of endotoxin lethality in mice. J. Bacteriol. 93:1967;1463-1464
44. Storm D.R., Rosenthal K.S., Swanson P.E. Polymyxin and related peptide antibiotics. Annu. Rev. Biochem. 46:1977;723-763
45. Moore R.A., Bates N.C., Hancock R.E. Interaction of polycationic antibiotics with Pseudomonas aeruginosa lipopolysaccharide and lipid A studied by using dansyl-polymyxin. Antimicrob. Agents Chemother. 29:1986;496-500
46. Thomas C.J., Surolia N., Surolia A. Surface plasmon resonance studies resolve the enigmatic endotoxin neutralizing activity of polymyxin B. J. Biol. Chem. 274:1999;29624-29627
47. Thomas C.J., Surolia A. Kinetics of the interaction of endotoxin with polymyxin B and its analogs a surface plasmon resonance analysis. FEBS Lett. 445:1999;420-424
48. Tsubery H., Ofek I., Cohen S., Fridkin M. The functional association of polymyxin B with bacterial lipopolysaccharide is stereospecific studies on polymyxin B nonapeptide. Biochemistry. 39:2000;11837-11844
49. Zanetti M., Gennaro R., Romeo D. Cathelicidins a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett. 374:1995;1-5
50. Nagaoka I., Hirota S., Niyonsaba F., Hirata M., Adachi Y., Tamura H., Tanaka S., Heumann D. Augmentation of the lipopolysaccharide-neutralizing activities of human cathelicidin CAP18/LL-37-derived antimicrobial peptides by replacement with hydrophobic and cationic amino acid residues. Clin. Diagn. Lab. Immunol. 9:2002;972-982
51. Bals R., Wilson J.M. Cathelicidins - a family of multifunctional antimicrobial peptides. Cell. Mol. Life Sci. 60:2003;711-720
52. Kirikae T., Hirata M., Yamasu H., Kirikae F., Tamura H., Kayama F., Nakatsuka K., Yokochi T., Nakano M. Protective effects of a human 18-kilodalton cationic antimicrobial protein (CAP18)-derived peptide against murine endotoxemia. Infect. Immun. 66:1998;1861-1868
53. Nagaoka I., Hirota S., Niyonsaba F., Hirata M., Adachi Y., Tamura H., Heumann D. Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-α by blocking the binding of LPS to CD14(+) cells. J. Immunol. 167:2001;3329-3338
54. Le Roy D., Di Padova F., Tees R., Lengacher S., Landmann R., Glauser M.P., Calandra T., Heumann D. Monoclonal antibodies to murine lipopolysaccharide (LPS)-binding protein (LBP) protect mice from lethal endotoxemia by blocking either the binding of LPS to LBP or the presentation of LPS/LBP complexes to CD14. J. Immunol. 162:1999;7454-7460
55. Di Padova F.E., Brade H., Barclay G.R., Poxton I.R., Liehl E., Schuetze E., Kocher H.P., Ramsay G., Schreier M.H., McClelland D.B. A broadly cross-protective monoclonal antibody binding to Escherichia coli and Salmonella lipopolysaccharides. Infect. Immun. 61:1993;3863-3872
56. Pollack M., Espinoza A.M., Guelde G., Koles N.L., Wahl L.M., Ohl C.A. Lipopolysaccharide (LPS)-specific monoclonal antibodies regulate LPS uptake and LPS-induced tumor necrosis factor-α responses by human monocytes. J. Infect. Dis. 172:1995;794-804
57. Akashi S., Shimazu R., Ogata H., Nagai Y., Takeda K., Kimoto M., Miyake K. Cutting edge cell surface expression and lipopolysaccharide signaling via the toll-like receptor 4-MD-2 complex on mouse peritoneal macrophages. J. Immunol. 164:2000;3471-3475
58. Zhu Y., Ho B., Ding J.L. Sequence and structural diversity in endotoxin-binding dodecapeptides. Biochim. Biophys. Acta. 1611:2003;234-242