Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ

Science

Volumn 276, Issue 5310, 1997, Pages 250-253

  Guo, Lin ^a   Lim, Kheng B ^a   Gunn, John S ^a   Bainbridge, Brian ^b   Darveau, Richard P ^b   Hackett, Murray ^a   Miller, Samuel I ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

^b BRISTOL MYERS SQUIBB   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENDOTHELIAL LEUKOCYTE ADHESION MOLECULE 1; LIPID A;

ARTICLE; BACTERIAL GENE; BACTERIAL VIRULENCE; GENE EXPRESSION REGULATION; GENETIC TRANSCRIPTION; NONHUMAN; PRIORITY JOURNAL; SALMONELLA TYPHIMURIUM;

ACYLATION; ARABINOSE; BACTERIAL PROTEINS; E-SELECTIN; ENDOTHELIUM, VASCULAR; FATTY ACIDS; GENES, BACTERIAL; HUMANS; LIPID A; LIPOPOLYSACCHARIDES; MONOCYTES; SALMONELLA TYPHIMURIUM; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TUMOR NECROSIS FACTOR-ALPHA; VIRULENCE;

BACTERIA (MICROORGANISMS); SALMONELLA; SALMONELLA TYPHIMURIUM; TYPHIMURIUM;

EID: 0030984298     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.276.5310.250     Document Type: Article

References (46)

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30. - (molecular anion) at m/z 323. The 3-phospho product was not stable and was observed to undergo a spontaneous net gain of two mass units, to m/z 325, followed by elimination of phosphate. Fragmentation of synthetic 2-phosphomyristate observed in the triple-quadrupole MS and ion trap did not support assigning such a side chain to the modified lipid A structure. However, a structure containing 4′ phosphate cannot be ruled out.
31. J. E. Somerville, L. Cassiano, B. Bainbridge, M. D. Cunningham, R. P. Darveau, J. Clin. Invest. 97, 359 (1996); R. P. Darveau et al., Infect. Immun. 63, 1311 (1995).
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33. Two serum proteins are also involved in this process: LPS-binding protein (LBP) and either soluble or membrane-bound CD14 [S. D. Wright, R. A. Ramos, P. S. Tobias, R. J. Ulevitch, J. C. Mathison, Science 249, 1431 (1990); E. A. Frey et al., J. Exp. Med. 176, 1665 (1992); J. Pugin et al., Proc. Natl. Acad. Sci. U.S.A. 90, 2744 (1993)].
34. Two serum proteins are also involved in this process: LPS-binding protein (LBP) and either soluble or membrane-bound CD14 [S. D. Wright, R. A. Ramos, P. S. Tobias, R. J. Ulevitch, J. C. Mathison, Science 249, 1431 (1990); E. A. Frey et al., J. Exp. Med. 176, 1665 (1992); J. Pugin et al., Proc. Natl. Acad. Sci. U.S.A. 90, 2744 (1993)].
35. Two serum proteins are also involved in this process: LPS-binding protein (LBP) and either soluble or membrane-bound CD14 [S. D. Wright, R. A. Ramos, P. S. Tobias, R. J. Ulevitch, J. C. Mathison, Science 249, 1431 (1990); E. A. Frey et al., J. Exp. Med. 176, 1665 (1992); J. Pugin et al., Proc. Natl. Acad. Sci. U.S.A. 90, 2744 (1993)].
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38. P. I. Fields, E. A. Groisman, F. Heffron, ibid. 243, 1059 (1989); S. I. Miller, W. S. Pulkkinen, M. E. Selsted, J. J. Mekalanos, Infect. Immun. 58, 3706 (1990).
39. For previous electrospray negative-ion studies of the diphosphoryl form of lipid A, see S. Chan and V. N. Reinhold, Anal. Biochem. 218, 63 (1994); A. K. Harrata, L. N. Domelsmith, R. B. Cole, Biol. Mass Spectrom. 22, 59 (1993). For previous studies that used proton nuclear magnetic resonance (NMR) MS and positive-ion fast atom bombardment (FAB) MS, see K. Takayama, N. Qureshi, P. Mascagni, J. Biol. Chem. 258, 12801 (1983); N. Qureshi, K. Takayama, D. Heller, C. Fenselau, ibid., p. 12947; N. Qureshi, K. Takayama, E. Ribi, ibid. 257, 11808 (1982). For a review of the biosynthesis, structure, and function of lipid A, see C. R. H. Raetz, J. Bacteriol. 175, 5745 (1993). The attachment of aminoarabinose to the glucosamine dimer cannot be assigned unequivocally on the basis of our data alone. Because the bond linking aminoarabinose to 4′ phosphate is highly labile, we have been unable to isolate an ion containing aminoarabinose linked to a fragment of lipid A, other than the molecular ion itself. However, there are other studies that support assigning the aminoarabinose substitution at the 4′ phosphate position (18).
40. For previous electrospray negative-ion studies of the diphosphoryl form of lipid A, see S. Chan and V. N. Reinhold, Anal. Biochem. 218, 63 (1994); A. K. Harrata, L. N. Domelsmith, R. B. Cole, Biol. Mass Spectrom. 22, 59 (1993). For previous studies that used proton nuclear magnetic resonance (NMR) MS and positive-ion fast atom bombardment (FAB) MS, see K. Takayama, N. Qureshi, P. Mascagni, J. Biol. Chem. 258, 12801 (1983); N. Qureshi, K. Takayama, D. Heller, C. Fenselau, ibid., p. 12947; N. Qureshi, K. Takayama, E. Ribi, ibid. 257, 11808 (1982). For a review of the biosynthesis, structure, and function of lipid A, see C. R. H. Raetz, J. Bacteriol. 175, 5745 (1993). The attachment of aminoarabinose to the glucosamine dimer cannot be assigned unequivocally on the basis of our data alone. Because the bond linking aminoarabinose to 4′ phosphate is highly labile, we have been unable to isolate an ion containing aminoarabinose linked to a fragment of lipid A, other than the molecular ion itself. However, there are other studies that support assigning the aminoarabinose substitution at the 4′ phosphate position (18).
41. For previous electrospray negative-ion studies of the diphosphoryl form of lipid A, see S. Chan and V. N. Reinhold, Anal. Biochem. 218, 63 (1994); A. K. Harrata, L. N. Domelsmith, R. B. Cole, Biol. Mass Spectrom. 22, 59 (1993). For previous studies that used proton nuclear magnetic resonance (NMR) MS and positive-ion fast atom bombardment (FAB) MS, see K. Takayama, N. Qureshi, P. Mascagni, J. Biol. Chem. 258, 12801 (1983); N. Qureshi, K. Takayama, D. Heller, C. Fenselau, ibid., p. 12947; N. Qureshi, K. Takayama, E. Ribi, ibid. 257, 11808 (1982). For a review of the biosynthesis, structure, and function of lipid A, see C. R. H. Raetz, J. Bacteriol. 175, 5745 (1993). The attachment of aminoarabinose to the glucosamine dimer cannot be assigned unequivocally on the basis of our data alone. Because the bond linking aminoarabinose to 4′ phosphate is highly labile, we have been unable to isolate an ion containing aminoarabinose linked to a fragment of lipid A, other than the molecular ion itself. However, there are other studies that support assigning the aminoarabinose substitution at the 4′ phosphate position (18).
42. For previous electrospray negative-ion studies of the diphosphoryl form of lipid A, see S. Chan and V. N. Reinhold, Anal. Biochem. 218, 63 (1994); A. K. Harrata, L. N. Domelsmith, R. B. Cole, Biol. Mass Spectrom. 22, 59 (1993). For previous studies that used proton nuclear magnetic resonance (NMR) MS and positive-ion fast atom bombardment (FAB) MS, see K. Takayama, N. Qureshi, P. Mascagni, J. Biol. Chem. 258, 12801 (1983); N. Qureshi, K. Takayama, D. Heller, C. Fenselau, ibid., p. 12947; N. Qureshi, K. Takayama, E. Ribi, ibid. 257, 11808 (1982). For a review of the biosynthesis, structure, and function of lipid A, see C. R. H. Raetz, J. Bacteriol. 175, 5745 (1993). The attachment of aminoarabinose to the glucosamine dimer cannot be assigned unequivocally on the basis of our data alone. Because the bond linking aminoarabinose to 4′ phosphate is highly labile, we have been unable to isolate an ion containing aminoarabinose linked to a fragment of lipid A, other than the molecular ion itself. However, there are other studies that support assigning the aminoarabinose substitution at the 4′ phosphate position (18).
43. For previous electrospray negative-ion studies of the diphosphoryl form of lipid A, see S. Chan and V. N. Reinhold, Anal. Biochem. 218, 63 (1994); A. K. Harrata, L. N. Domelsmith, R. B. Cole, Biol. Mass Spectrom. 22, 59 (1993). For previous studies that used proton nuclear magnetic resonance (NMR) MS and positive-ion fast atom bombardment (FAB) MS, see K. Takayama, N. Qureshi, P. Mascagni, J. Biol. Chem. 258, 12801 (1983); N. Qureshi, K. Takayama, D. Heller, C. Fenselau, ibid., p. 12947; N. Qureshi, K. Takayama, E. Ribi, ibid. 257, 11808 (1982). For a review of the biosynthesis, structure, and function of lipid A, see C. R. H. Raetz, J. Bacteriol. 175, 5745 (1993). The attachment of aminoarabinose to the glucosamine dimer cannot be assigned unequivocally on the basis of our data alone. Because the bond linking aminoarabinose to 4′ phosphate is highly labile, we have been unable to isolate an ion containing aminoarabinose linked to a fragment of lipid A, other than the molecular ion itself. However, there are other studies that support assigning the aminoarabinose substitution at the 4′ phosphate position (18).
44. For previous electrospray negative-ion studies of the diphosphoryl form of lipid A, see S. Chan and V. N. Reinhold, Anal. Biochem. 218, 63 (1994); A. K. Harrata, L. N. Domelsmith, R. B. Cole, Biol. Mass Spectrom. 22, 59 (1993). For previous studies that used proton nuclear magnetic resonance (NMR) MS and positive-ion fast atom bombardment (FAB) MS, see K. Takayama, N. Qureshi, P. Mascagni, J. Biol. Chem. 258, 12801 (1983); N. Qureshi, K. Takayama, D. Heller, C. Fenselau, ibid., p. 12947; N. Qureshi, K. Takayama, E. Ribi, ibid. 257, 11808 (1982). For a review of the biosynthesis, structure, and function of lipid A, see C. R. H. Raetz, J. Bacteriol. 175, 5745 (1993). The attachment of aminoarabinose to the glucosamine dimer cannot be assigned unequivocally on the basis of our data alone. Because the bond linking aminoarabinose to 4′ phosphate is highly labile, we have been unable to isolate an ion containing aminoarabinose linked to a fragment of lipid A, other than the molecular ion itself. However, there are other studies that support assigning the aminoarabinose substitution at the 4′ phosphate position (18).
45. K. B. Lim and M. Hackett, data not shown. Both m/z 159 and 177 lost phosphate when fragmented in the ion trap.
46. We thank K. A. Walsh and L. H. Ericsson for MALDITOF and triple-quadrupole mass spectrometers; J. R. Yates III for the ion trap; M. Sanders and W. Loyd for assistance with the ion trap experiments; W. N. Howald for the GC-MS analyses; F. Turecek and W. L. Nelson for reviewing the MS results; M. Gelb for suggesting the synthesis scheme in (21); and J. Kowalak, H. Wang, J. Somerville, J. Eng, A. R. Dongre, and E. Carmack for their assistance. Supported by NIH grant R01 Al30479 (S.I.M.) and the School of Pharmacy and Department of Medicinal Chemistry, University of Washington (M.H.).