ライフサイエンスコーパス: lipid IVA

1 rm tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).

2 yme preparations incubated with Kdo2-[4'-32P]lipid IVA.

3 IVA, and (3-deoxy-D-manno-octulosonic acid)2-lipid IVA.

4 that acts on the key lipid A precursor Kdo2-lipid IVA.

5 IVA and (3-deoxy-D-manno-octulosonic acid)2-lipid IVA.

6 nding in vitro glycosylation of Kdo2-[4'-32P]lipid IVA.

7 annosylated at less than 1% the rate of Kdo2-lipid IVA.

8 lated Escherichia coli LPS or tetra-acylated lipid IVA.

9 hat starts with GDP-mannose and Kdo2-[4'-32P]lipid IVA.

10 atalyzed glycosylation of the acceptor, Kdo2-lipid IVA.

11 5 mM for ADP-mannose and 4.5 microM for Kdo2-lipid IVA.

12 achment of both Kdo groups to the precursor, lipid IVA.

13 formed by HtrB, designated (Kdo)2-(lauroyl)-lipid IVA.

14 urate, activated on ACP, to (Kdo)2-(lauroyl)-lipid IVA.

15 thesis that acylates the intermediate (Kdo)2-lipid IVA.

16 lipid IVA about 100 times faster than (Kdo)2-lipid IVA.

17 from lauroyl acyl carrier protein to (Kdo)2-lipid IVA.

18 incorporated one laurate residue into (Kdo)2-lipid IVA.

19 buted to novel acylations of (Kdo)2-[4'-32P]-lipid IVA.

20 fic enzymes that recognize and modify (Kdo)2-lipid IVA.

21 ADP-mannose-dependent glycosylation of Kdo2-lipid IVA.

22 annose and then galactose to (Kdo)2-[4'-32P]-lipid IVA.

23 es mannose transfer from ADP-mannose to Kdo2-lipid IVA.

24 nsfers 27-hydroxyoctacosanoic acid to (Kdo)2-lipid IVA, a key lipid A precursor common to both E. col

25 MsbB acylates (Kdo)2-(lauroyl)-lipid IVA about 100 times faster than (Kdo)2-lipid IVA.

26 The crystal structure of cMD-1 with lipid IVa, an LPS precursor, at 2.4 A resolution reveale

27 nosaccharide lipid X at about 5% the rate of lipid IVA and (3-deoxy-D-manno-octulosonic acid)2-lipid

28 sphatases were detected using (Kdo)2-[1-32P]-lipid IVA and (Kdo)2-[4'-32P]-lipid IVA, respectively, a

29 The truncated LPS were identified as Kdo-N3-lipid IVA and (Kdo-N3)2-lipid IVA by MS analysis.

30 taxel while preserving the responsiveness to lipid IVa and lipid A.

31 d human TLR4/MD-2, whereas the tetraacylated lipid IVa and paclitaxel activate only mTLR4/MD-2 and an

32 domain, are essential for activation of with lipid IVa and paclitaxel, which, although not a structur

33 Both lipid IVA and R. sphaeroides lipid A inhibited the effec

34 The lipid A analogues lipid IVa and Rhodobacter sphaeroides lipid A (RSLA) exh

35 We then tested the effects of lipid IVA and Rhodobacter sphaeroides lipid A, compounds

36 some lipid A precursors, including lipid X, lipid IVA, and (3-deoxy-D-manno-octulosonic acid)2-lipid

37 antagonistic LPS variants including lipid A, lipid IVa, and synthetic antagonist Eritoran, and provid

38 apparent Km values for GDP-mannose and Kdo2-lipid IVA are 4.3 microM and 7.1 microM, respectively, i

39 y transfers laurate from lauroyl-ACP to Kdo2-lipid IVA are not defective in the cold-induced palmitol

40 h the conservation and versatility of (Kdo)2-lipid IVA as a lipid A precursor in bacteria.

41 lls expressing the hamster TLR4 responded to lipid IVa as an LPS mimetic, as if they were hamster in

42 into nascent lipopolysaccharide, using Kdo2-lipid IVA as the acceptor and GDP-mannose (or synthetic

43 sarum using the acylation of (Kdo)2-[4'-32P]-lipid IVA as the assay.

44 Using the intermediate (Kdo)2-lipid IVA as the laurate acceptor, extracts of strains w

45 onsistent with the inner Kdo residue of Kdo2-lipid IVA as the site of mannosylation.

46 e deacylase reaction product, generated with lipid IVA as the substrate, confirms unequivocally that

47 es not only the hydrolysis of (Kdo)2-[4'-32P]lipid IVA but also the transfer the 4'-phosphate of Kdo2

48 GDP-mannose-dependent glycosylation of Kdo2-lipid IVA, but they are active when ADP-mannose is subst

49 identified as Kdo-N3-lipid IVA and (Kdo-N3)2-lipid IVA by MS analysis.

50 Mannosylation of Kdo2-lipid IVA catalyzed by RfaC proceeds in high yield and m

51 generated in vitro from the model substrate lipid IVA confirms the selective removal of the 1-phosph

52 The analog, Kdo-lipid IVA, functions as an acceptor, but is mannosylated

53 abolites were generated from (Kdo)2-[4'-32P]-lipid IVA in a manner that was dependent upon both membr

54 now show that a single Kdo is transferred to lipid IVA in extracts of H. influenzae.

55 The specific activity of Kdo transfer to lipid IVA is 0.5-1 nmol/min/mg in H. influenzae membrane

56 ose and the conserved precursor Kdo2-[4'-32P]lipid IVA is proposed to represent a key early enzyme in

57 Like lipid IVA, Kdo-lipid IVA was an excellent substrate for

58 measurable, rate whereby MsbB acts on (Kdo)2-lipid IVA may explain why overexpression of MsbB suppres

59 4 mutants were inactive when stimulated with lipid IVa or paclitaxel, but retained significant activa

60 (Kdo)2-[1-32P]-lipid IVA and (Kdo)2-[4'-32P]-lipid IVA, respectively, as shown by release of 32Pi.

61 RSLA and lipid IVa strongly induced NF-kappaB activity and IL-6 r

62 We report the crystal structure of lipid IVA, the LpxK product, bound to the enzyme, provid

63 can also be used together with Kdo2-[4'-32P]lipid IVA to assay for the physiological donor (presumab

64 he transfer the 4'-phosphate of Kdo2-[4'-32P]lipid IVA to the inositol headgroup of phosphatidylinosi

65 B+ bearing plasmids acylate (Kdo)2-(lauroyl)-lipid IVA very rapidly compared with wild type.

66 Like lipid IVA, Kdo-lipid IVA was an excellent substrate for the bi-function

67 ranes of H. influenzae, but not E. coli, Kdo-lipid IVA was further phosphorylated in the presence of

68 enzae membranes, milligram quantities of Kdo-lipid IVA were prepared for analysis.

69 to form the phosphorylated precursor, (Kdo)2-lipid IVA, which is then processed differently.

70 e of ATP, yielding a mono-phosphorylated Kdo-lipid IVA with a parent ion (M - H)- at m/z 1703.9.