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Volumn 9, Issue 1, 2013, Pages

Lipid Exchange between Borrelia burgdorferi and Host Cells

Author keywords

[No Author keywords available]

Indexed keywords

1, 6 DIPHENYL 1, 3, 5 HEXATRIENE; APOLIPOPROTEIN; CHOLESTEROL; GLYCOLIPID; LIPID TRANSFER PROTEIN; UNCLASSIFIED DRUG;

EID: 84875061571     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1003109     Document Type: Article
Times cited : (100)

References (95)
  • 3
    • 0034838652 scopus 로고    scopus 로고
    • Structural analysis of glycolipids from Borrelia burgdorferi
    • Hossain H, Wellensiek HJ, Geyer R, Lochnit G, (2001) Structural analysis of glycolipids from Borrelia burgdorferi. Biochimie 83: 683-692.
    • (2001) Biochimie , vol.83 , pp. 683-692
    • Hossain, H.1    Wellensiek, H.J.2    Geyer, R.3    Lochnit, G.4
  • 4
    • 0028297815 scopus 로고
    • Fatty acids of Treponema pallidum and Borrelia burgdorferi lipoproteins
    • Belisle JT, Brandt ME, Radolf JD, Norgard MV, (1994) Fatty acids of Treponema pallidum and Borrelia burgdorferi lipoproteins. J Bacteriol 176: 2151-2157.
    • (1994) J Bacteriol , vol.176 , pp. 2151-2157
    • Belisle, J.T.1    Brandt, M.E.2    Radolf, J.D.3    Norgard, M.V.4
  • 5
    • 0029041384 scopus 로고
    • Characterization of outer membranes isolated from Borrelia burgdorferi, the Lyme disease spirochete
    • Radolf JD, Goldberg MS, Bourell K, Baker SI, Jones JD, et al. (1995) Characterization of outer membranes isolated from Borrelia burgdorferi, the Lyme disease spirochete. Infect Immun 63: 2154-2163.
    • (1995) Infect Immun , vol.63 , pp. 2154-2163
    • Radolf, J.D.1    Goldberg, M.S.2    Bourell, K.3    Baker, S.I.4    Jones, J.D.5
  • 7
    • 0028790934 scopus 로고
    • Characterization of outer membranes isolated from Treponema pallidum, the syphilis spirochete
    • Radolf JD, Robinson EJ, Bourell KW, Akins DR, Porcella SF, et al. (1995) Characterization of outer membranes isolated from Treponema pallidum, the syphilis spirochete. Infect Immun 63: 4244-4252.
    • (1995) Infect Immun , vol.63 , pp. 4244-4252
    • Radolf, J.D.1    Robinson, E.J.2    Bourell, K.W.3    Akins, D.R.4    Porcella, S.F.5
  • 8
    • 0025264283 scopus 로고
    • Immunogenic integral membrane proteins of Borrelia burgdorferi are lipoproteins
    • Brandt ME, Riley BS, Radolf JD, Norgard MV, (1990) Immunogenic integral membrane proteins of Borrelia burgdorferi are lipoproteins. Infect Immun 58: 983-991.
    • (1990) Infect Immun , vol.58 , pp. 983-991
    • Brandt, M.E.1    Riley, B.S.2    Radolf, J.D.3    Norgard, M.V.4
  • 9
    • 67349224063 scopus 로고    scopus 로고
    • Strong IgG antibody responses to Borrelia burgdorferi glycolipids in patients with Lyme arthritis, a late manifestation of the infection
    • Jones KL, Seward RJ, Ben-Menachem G, Glickstein LJ, Costello CE, et al. (2009) Strong IgG antibody responses to Borrelia burgdorferi glycolipids in patients with Lyme arthritis, a late manifestation of the infection. Clin Immunol 132: 93-102.
    • (2009) Clin Immunol , vol.132 , pp. 93-102
    • Jones, K.L.1    Seward, R.J.2    Ben-Menachem, G.3    Glickstein, L.J.4    Costello, C.E.5
  • 10
    • 0028057599 scopus 로고
    • Analysis of Borrelia burgdorferi membrane architecture by freeze-fracture electron microscopy
    • Radolf JD, Bourell KW, Akins DR, Brusca JS, Norgard MV, (1994) Analysis of Borrelia burgdorferi membrane architecture by freeze-fracture electron microscopy. J Bacteriol 176: 21-31.
    • (1994) J Bacteriol , vol.176 , pp. 21-31
    • Radolf, J.D.1    Bourell, K.W.2    Akins, D.R.3    Brusca, J.S.4    Norgard, M.V.5
  • 11
    • 67649403602 scopus 로고    scopus 로고
    • Acylated cholesteryl galactosides are specific antigens of Borrelia causing lyme disease and frequently induce antibodies in late stages of disease
    • Stubs G, Fingerle V, Wilske B, Gobel UB, Zahringer U, et al. (2009) Acylated cholesteryl galactosides are specific antigens of Borrelia causing lyme disease and frequently induce antibodies in late stages of disease. J Biol Chem 284: 13326-13334.
    • (2009) J Biol Chem , vol.284 , pp. 13326-13334
    • Stubs, G.1    Fingerle, V.2    Wilske, B.3    Gobel, U.B.4    Zahringer, U.5
  • 12
    • 0141780838 scopus 로고    scopus 로고
    • Acylated cholesteryl galactoside as a novel immunogenic motif in Borrelia burgdorferi sensu stricto
    • Schroder NW, Schombel U, Heine H, Gobel UB, Zahringer U, et al. (2003) Acylated cholesteryl galactoside as a novel immunogenic motif in Borrelia burgdorferi sensu stricto. J Biol Chem 278: 33645-33653.
    • (2003) J Biol Chem , vol.278 , pp. 33645-33653
    • Schroder, N.W.1    Schombel, U.2    Heine, H.3    Gobel, U.B.4    Zahringer, U.5
  • 14
    • 84855900042 scopus 로고    scopus 로고
    • Of ticks, mice and men: understanding the dual-host lifestyle of Lyme disease spirochaetes
    • Radolf JD, Caimano MJ, Stevenson B, Hu LT, (2012) Of ticks, mice and men: understanding the dual-host lifestyle of Lyme disease spirochaetes. Nat Rev Microbiol 10: 87-99.
    • (2012) Nat Rev Microbiol , vol.10 , pp. 87-99
    • Radolf, J.D.1    Caimano, M.J.2    Stevenson, B.3    Hu, L.T.4
  • 15
    • 41649095188 scopus 로고    scopus 로고
    • Immune responses induced by spirochetal outer membrane lipoproteins and glycolipids
    • Schroder NW, Eckert J, Stubs G, Schumann RR, (2008) Immune responses induced by spirochetal outer membrane lipoproteins and glycolipids. Immunobiology 213: 329-340.
    • (2008) Immunobiology , vol.213 , pp. 329-340
    • Schroder, N.W.1    Eckert, J.2    Stubs, G.3    Schumann, R.R.4
  • 16
    • 0026052374 scopus 로고
    • Identification of an immunoreactive non-proteinaleous component in Borrelia burgdorferi
    • Eiffert H, Lotter H, Jarecki-Khan K, Thomssen R, (1991) Identification of an immunoreactive non-proteinaleous component in Borrelia burgdorferi. Med Microbiol Immunol 180: 229-237.
    • (1991) Med Microbiol Immunol , vol.180 , pp. 229-237
    • Eiffert, H.1    Lotter, H.2    Jarecki-Khan, K.3    Thomssen, R.4
  • 18
    • 34250652541 scopus 로고    scopus 로고
    • Functional analysis of a lipid galactosyltransferase synthesizing the major envelope lipid in the Lyme disease spirochete Borrelia burgdorferi
    • Ostberg Y, Berg S, Comstedt P, Wieslander A, Bergstrom S, (2007) Functional analysis of a lipid galactosyltransferase synthesizing the major envelope lipid in the Lyme disease spirochete Borrelia burgdorferi. FEMS Microbiol Lett 272: 22-29.
    • (2007) FEMS Microbiol Lett , vol.272 , pp. 22-29
    • Ostberg, Y.1    Berg, S.2    Comstedt, P.3    Wieslander, A.4    Bergstrom, S.5
  • 20
    • 80052588400 scopus 로고    scopus 로고
    • Acylated cholesteryl galactosides are ubiquitous glycolipid antigens among Borrelia burgdorferi sensu lato
    • Stubs G, Fingerle V, Zahringer U, Schumann RR, Rademann J, et al. (2011) Acylated cholesteryl galactosides are ubiquitous glycolipid antigens among Borrelia burgdorferi sensu lato. FEMS Immunol Med Microbiol 63: 140-143.
    • (2011) FEMS Immunol Med Microbiol , vol.63 , pp. 140-143
    • Stubs, G.1    Fingerle, V.2    Zahringer, U.3    Schumann, R.R.4    Rademann, J.5
  • 21
    • 0028058723 scopus 로고
    • A 14,000 MW lipoprotein and a glycolipid-like structure of Borrelia burgdorferi induce proliferation and immunoglobulin production in mouse B cells at high frequencies
    • Honarvar N, Schaible UE, Galanos C, Wallich R, Simon MM, (1994) A 14,000 MW lipoprotein and a glycolipid-like structure of Borrelia burgdorferi induce proliferation and immunoglobulin production in mouse B cells at high frequencies. Immunology 82: 389-396.
    • (1994) Immunology , vol.82 , pp. 389-396
    • Honarvar, N.1    Schaible, U.E.2    Galanos, C.3    Wallich, R.4    Simon, M.M.5
  • 22
    • 0029121025 scopus 로고
    • Experimental immunization with Borrelia burgdorferi induces development of antibodies to gangliosides
    • Garcia-Monco JC, Seidman RJ, Benach JL, (1995) Experimental immunization with Borrelia burgdorferi induces development of antibodies to gangliosides. Infect Immun 63: 4130-4137.
    • (1995) Infect Immun , vol.63 , pp. 4130-4137
    • Garcia-Monco, J.C.1    Seidman, R.J.2    Benach, J.L.3
  • 23
    • 0027164682 scopus 로고
    • Reactivity of neuroborreliosis patients (Lyme disease) to cardiolipin and gangliosides
    • Garcia Monco JC, Wheeler CM, Benach JL, Furie RA, Lukehart SA, et al. (1993) Reactivity of neuroborreliosis patients (Lyme disease) to cardiolipin and gangliosides. J Neurol Sci 117: 206-214.
    • (1993) J Neurol Sci , vol.117 , pp. 206-214
    • Garcia Monco, J.C.1    Wheeler, C.M.2    Benach, J.L.3    Furie, R.A.4    Lukehart, S.A.5
  • 24
    • 17844364491 scopus 로고    scopus 로고
    • Infection-induced marginal zone B cell production of Borrelia hermsii-specific antibody is impaired in the absence of CD1d
    • Belperron AA, Dailey CM, Bockenstedt LK, (2005) Infection-induced marginal zone B cell production of Borrelia hermsii-specific antibody is impaired in the absence of CD1d. J Immunol 174: 5681-5686.
    • (2005) J Immunol , vol.174 , pp. 5681-5686
    • Belperron, A.A.1    Dailey, C.M.2    Bockenstedt, L.K.3
  • 25
    • 0034327173 scopus 로고    scopus 로고
    • Cutting edge: CD1d deficiency impairs murine host defense against the spirochete, Borrelia burgdorferi
    • Kumar H, Belperron A, Barthold SW, Bockenstedt LK, (2000) Cutting edge: CD1d deficiency impairs murine host defense against the spirochete, Borrelia burgdorferi. J Immunol 165: 4797-4801.
    • (2000) J Immunol , vol.165 , pp. 4797-4801
    • Kumar, H.1    Belperron, A.2    Barthold, S.W.3    Bockenstedt, L.K.4
  • 26
    • 33747607029 scopus 로고    scopus 로고
    • Natural killer T cells recognize diacylglycerol antigens from pathogenic bacteria
    • Kinjo Y, Tupin E, Wu D, Fujio M, Garcia-Navarro R, et al. (2006) Natural killer T cells recognize diacylglycerol antigens from pathogenic bacteria. Nat Immunol 7: 978-986.
    • (2006) Nat Immunol , vol.7 , pp. 978-986
    • Kinjo, Y.1    Tupin, E.2    Wu, D.3    Fujio, M.4    Garcia-Navarro, R.5
  • 27
    • 76549103448 scopus 로고    scopus 로고
    • Lipid binding orientation within CD1d affects recognition of Borrelia burgorferi antigens by NKT cells
    • Wang J, Li Y, Kinjo Y, Mac TT, Gibson D, et al. (2010) Lipid binding orientation within CD1d affects recognition of Borrelia burgorferi antigens by NKT cells. Proc Natl Acad Sci U S A 107: 1535-1540.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 1535-1540
    • Wang, J.1    Li, Y.2    Kinjo, Y.3    Mac, T.T.4    Gibson, D.5
  • 28
    • 65449145529 scopus 로고    scopus 로고
    • Local production of IFN-gamma by invariant NKT cells modulates acute Lyme carditis
    • Olson CM Jr, Bates TC, Izadi H, Radolf JD, Huber SA, et al. (2009) Local production of IFN-gamma by invariant NKT cells modulates acute Lyme carditis. J Immunol 182: 3728-3734.
    • (2009) J Immunol , vol.182 , pp. 3728-3734
    • Olson Jr., C.M.1    Bates, T.C.2    Izadi, H.3    Radolf, J.D.4    Huber, S.A.5
  • 29
    • 77949873622 scopus 로고    scopus 로고
    • An intravascular immune response to Borrelia burgdorferi involves Kupffer cells and iNKT cells
    • Lee WY, Moriarty TJ, Wong CH, Zhou H, Strieter RM, et al. (2010) An intravascular immune response to Borrelia burgdorferi involves Kupffer cells and iNKT cells. Nat Immunol 11: 295-302.
    • (2010) Nat Immunol , vol.11 , pp. 295-302
    • Lee, W.Y.1    Moriarty, T.J.2    Wong, C.H.3    Zhou, H.4    Strieter, R.M.5
  • 30
    • 77958089989 scopus 로고    scopus 로고
    • Cholesterol lipids of Borrelia burgdorferi form lipid rafts and are required for the bactericidal activity of a complement-independent antibody
    • LaRocca TJ, Crowley JT, Cusack BJ, Pathak P, Benach J, et al. (2010) Cholesterol lipids of Borrelia burgdorferi form lipid rafts and are required for the bactericidal activity of a complement-independent antibody. Cell Host Microbe 8: 331-342.
    • (2010) Cell Host Microbe , vol.8 , pp. 331-342
    • LaRocca, T.J.1    Crowley, J.T.2    Cusack, B.J.3    Pathak, P.4    Benach, J.5
  • 31
    • 0036667737 scopus 로고    scopus 로고
    • Insights into lipid raft structure and formation from experiments in model membranes
    • London E, (2002) Insights into lipid raft structure and formation from experiments in model membranes. Curr Opin Struct Biol 12: 480-486.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 480-486
    • London, E.1
  • 32
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
    • Schroeder R, London E, Brown D, (1994) Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior. Proc Natl Acad Sci U S A 91: 12130-12134.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 12130-12134
    • Schroeder, R.1    London, E.2    Brown, D.3
  • 33
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown DA, London E, (2000) Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J Biol Chem 275: 17221-17224.
    • (2000) J Biol Chem , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 34
    • 0036195482 scopus 로고    scopus 로고
    • Structure and function of membrane rafts
    • Brown D, (2002) Structure and function of membrane rafts. Int J Med Microbiol 291: 433-437.
    • (2002) Int J Med Microbiol , vol.291 , pp. 433-437
    • Brown, D.1
  • 35
    • 0031965054 scopus 로고    scopus 로고
    • Sphingolipid organization in biomembranes: what physical studies of model membranes reveal
    • Brown RE, (1998) Sphingolipid organization in biomembranes: what physical studies of model membranes reveal. J Cell Sci 111 (Pt 1):: 1-9.
    • (1998) J Cell Sci , vol.111 , Issue.Pt 1 , pp. 1-9
    • Brown, R.E.1
  • 36
    • 66349087046 scopus 로고    scopus 로고
    • The challenge of lipid rafts
    • Pike LJ, (2009) The challenge of lipid rafts. J Lipid Res 50 Suppl: S323-328.
    • (2009) J Lipid Res , vol.50 , Issue.SUPPL.
    • Pike, L.J.1
  • 37
    • 45449105538 scopus 로고    scopus 로고
    • Proteins and cholesterol-rich domains
    • Epand RM, (2008) Proteins and cholesterol-rich domains. Biochim Biophys Acta 1778: 1576-1582.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1576-1582
    • Epand, R.M.1
  • 38
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E, (1998) Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 14: 111-136.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 39
    • 0030949722 scopus 로고    scopus 로고
    • The influence of cholesterol on phospholipid membrane curvature and bending elasticity
    • Chen Z, Rand RP, (1997) The influence of cholesterol on phospholipid membrane curvature and bending elasticity. Biophys J 73: 267-276.
    • (1997) Biophys J , vol.73 , pp. 267-276
    • Chen, Z.1    Rand, R.P.2
  • 40
    • 1842484428 scopus 로고    scopus 로고
    • Lipid rafts and the regulation of exocytosis
    • Salaun C, James DJ, Chamberlain LH, (2004) Lipid rafts and the regulation of exocytosis. Traffic 5: 255-264.
    • (2004) Traffic , vol.5 , pp. 255-264
    • Salaun, C.1    James, D.J.2    Chamberlain, L.H.3
  • 41
    • 0345706824 scopus 로고    scopus 로고
    • Caveosomes and endocytosis of lipid rafts
    • Nichols B, (2003) Caveosomes and endocytosis of lipid rafts. J Cell Sci 116: 4707-4714.
    • (2003) J Cell Sci , vol.116 , pp. 4707-4714
    • Nichols, B.1
  • 42
    • 65949090768 scopus 로고    scopus 로고
    • Domains in bacterial membranes and the action of antimicrobial agents
    • Epand RM, Epand RF, (2009) Domains in bacterial membranes and the action of antimicrobial agents. Mol Biosyst 5: 580-587.
    • (2009) Mol Biosyst , vol.5 , pp. 580-587
    • Epand, R.M.1    Epand, R.F.2
  • 43
    • 0034577510 scopus 로고    scopus 로고
    • Cholesterol is required for the formation of regulated and constitutive secretory vesicles from the trans-Golgi network
    • Wang Y, Thiele C, Huttner WB, (2000) Cholesterol is required for the formation of regulated and constitutive secretory vesicles from the trans-Golgi network. Traffic 1: 952-962.
    • (2000) Traffic , vol.1 , pp. 952-962
    • Wang, Y.1    Thiele, C.2    Huttner, W.B.3
  • 45
    • 79960126040 scopus 로고    scopus 로고
    • Adhesion mechanisms of Borrelia burgdorferi
    • Antonara S, Ristow L, Coburn J, (2011) Adhesion mechanisms of Borrelia burgdorferi. Adv Exp Med Biol 715: 35-49.
    • (2011) Adv Exp Med Biol , vol.715 , pp. 35-49
    • Antonara, S.1    Ristow, L.2    Coburn, J.3
  • 46
    • 1842265645 scopus 로고
    • Adherence of the Lyme disease spirochete to glial cells and cells of glial origin
    • Garcia-Monco JC, Fernandez-Villar B, Benach JL, (1989) Adherence of the Lyme disease spirochete to glial cells and cells of glial origin. J Infect Dis 160: 497-506.
    • (1989) J Infect Dis , vol.160 , pp. 497-506
    • Garcia-Monco, J.C.1    Fernandez-Villar, B.2    Benach, J.L.3
  • 47
    • 0027205383 scopus 로고
    • Integrin alpha IIb beta 3 mediates binding of the Lyme disease agent Borrelia burgdorferi to human platelets
    • Coburn J, Leong JM, Erban JK, (1993) Integrin alpha IIb beta 3 mediates binding of the Lyme disease agent Borrelia burgdorferi to human platelets. Proc Natl Acad Sci U S A 90: 7059-7063.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 7059-7063
    • Coburn, J.1    Leong, J.M.2    Erban, J.K.3
  • 48
    • 34548694325 scopus 로고    scopus 로고
    • Borrelia burgdorferi adhesins identified using in vivo phage display
    • Antonara S, Chafel RM, LaFrance M, Coburn J, (2007) Borrelia burgdorferi adhesins identified using in vivo phage display. Mol Microbiol 66: 262-276.
    • (2007) Mol Microbiol , vol.66 , pp. 262-276
    • Antonara, S.1    Chafel, R.M.2    LaFrance, M.3    Coburn, J.4
  • 49
    • 8344262276 scopus 로고    scopus 로고
    • TROSPA, an Ixodes scapularis receptor for Borrelia burgdorferi
    • Pal U, Li X, Wang T, Montgomery RR, Ramamoorthi N, et al. (2004) TROSPA, an Ixodes scapularis receptor for Borrelia burgdorferi. Cell 119: 457-468.
    • (2004) Cell , vol.119 , pp. 457-468
    • Pal, U.1    Li, X.2    Wang, T.3    Montgomery, R.R.4    Ramamoorthi, N.5
  • 51
    • 0346666691 scopus 로고    scopus 로고
    • Adaptation of the Lyme disease spirochaete to the mammalian host environment results in enhanced glycosaminoglycan and host cell binding
    • Parveen N, Caimano M, Radolf JD, Leong JM, (2003) Adaptation of the Lyme disease spirochaete to the mammalian host environment results in enhanced glycosaminoglycan and host cell binding. Mol Microbiol 47: 1433-1444.
    • (2003) Mol Microbiol , vol.47 , pp. 1433-1444
    • Parveen, N.1    Caimano, M.2    Radolf, J.D.3    Leong, J.M.4
  • 52
    • 70350450260 scopus 로고    scopus 로고
    • Borrelia burgdorferi BmpA is a laminin-binding protein
    • Verma A, Brissette CA, Bowman A, Stevenson B, (2009) Borrelia burgdorferi BmpA is a laminin-binding protein. Infect Immun 77: 4940-4946.
    • (2009) Infect Immun , vol.77 , pp. 4940-4946
    • Verma, A.1    Brissette, C.A.2    Bowman, A.3    Stevenson, B.4
  • 54
    • 0042825338 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis and Anaplasma phagocytophilum lack genes for lipid A biosynthesis and incorporate cholesterol for their survival
    • Lin M, Rikihisa Y, (2003) Ehrlichia chaffeensis and Anaplasma phagocytophilum lack genes for lipid A biosynthesis and incorporate cholesterol for their survival. Infect Immun 71: 5324-5331.
    • (2003) Infect Immun , vol.71 , pp. 5324-5331
    • Lin, M.1    Rikihisa, Y.2
  • 55
    • 9244255313 scopus 로고    scopus 로고
    • Lipid profile of Helicobacter spp.: presence of cholesteryl glucoside as a characteristic feature
    • Haque M, Hirai Y, Yokota K, Mori N, Jahan I, et al. (1996) Lipid profile of Helicobacter spp.: presence of cholesteryl glucoside as a characteristic feature. J Bacteriol 178: 2065-2070.
    • (1996) J Bacteriol , vol.178 , pp. 2065-2070
    • Haque, M.1    Hirai, Y.2    Yokota, K.3    Mori, N.4    Jahan, I.5
  • 56
    • 0029165789 scopus 로고
    • Steryl glycosides: a characteristic feature of the Helicobacter spp.?
    • Haque M, Hirai Y, Yokota K, Oguma K, (1995) Steryl glycosides: a characteristic feature of the Helicobacter spp.? J Bacteriol 177: 5334-5337.
    • (1995) J Bacteriol , vol.177 , pp. 5334-5337
    • Haque, M.1    Hirai, Y.2    Yokota, K.3    Oguma, K.4
  • 57
    • 0029348972 scopus 로고
    • Lipid profiles of Helicobacter pylori and Helicobacter mustelae grown in serum-supplemented and serum-free media
    • Haque M, Hirai Y, Yokota K, Oguma K, (1995) Lipid profiles of Helicobacter pylori and Helicobacter mustelae grown in serum-supplemented and serum-free media. Acta Med Okayama 49: 205-211.
    • (1995) Acta Med Okayama , vol.49 , pp. 205-211
    • Haque, M.1    Hirai, Y.2    Yokota, K.3    Oguma, K.4
  • 58
    • 0029148371 scopus 로고
    • Unique cholesteryl glucosides in Helicobacter pylori: composition and structural analysis
    • Hirai Y, Haque M, Yoshida T, Yokota K, Yasuda T, et al. (1995) Unique cholesteryl glucosides in Helicobacter pylori: composition and structural analysis. J Bacteriol 177: 5327-5333.
    • (1995) J Bacteriol , vol.177 , pp. 5327-5333
    • Hirai, Y.1    Haque, M.2    Yoshida, T.3    Yokota, K.4    Yasuda, T.5
  • 60
    • 0015175106 scopus 로고
    • Biosynthesis of cholesteryl glucoside by Mycoplasma gallinarum
    • Smith PF, (1971) Biosynthesis of cholesteryl glucoside by Mycoplasma gallinarum. J Bacteriol 108: 986-991.
    • (1971) J Bacteriol , vol.108 , pp. 986-991
    • Smith, P.F.1
  • 61
    • 33748462851 scopus 로고    scopus 로고
    • Cholesterol glucosylation promotes immune evasion by Helicobacter pylori
    • Wunder C, Churin Y, Winau F, Warnecke D, Vieth M, et al. (2006) Cholesterol glucosylation promotes immune evasion by Helicobacter pylori. Nat Med 12: 1030-1038.
    • (2006) Nat Med , vol.12 , pp. 1030-1038
    • Wunder, C.1    Churin, Y.2    Winau, F.3    Warnecke, D.4    Vieth, M.5
  • 62
    • 84155167763 scopus 로고    scopus 로고
    • Helicobacter pylori cholesteryl glucosides interfere with host membrane phase and affect type IV secretion system function during infection in AGS cells
    • Wang HJ, Cheng WC, Cheng HH, Lai CH, Wang WC, (2012) Helicobacter pylori cholesteryl glucosides interfere with host membrane phase and affect type IV secretion system function during infection in AGS cells. Mol Microbiol 83: 67-84.
    • (2012) Mol Microbiol , vol.83 , pp. 67-84
    • Wang, H.J.1    Cheng, W.C.2    Cheng, H.H.3    Lai, C.H.4    Wang, W.C.5
  • 63
    • 67649352970 scopus 로고    scopus 로고
    • Membrane fluidity and lipid order in ternary giant unilamellar vesicles using a new bodipy-cholesterol derivative
    • Ariola FS, Li Z, Cornejo C, Bittman R, Heikal AA, (2009) Membrane fluidity and lipid order in ternary giant unilamellar vesicles using a new bodipy-cholesterol derivative. Biophys J 96: 2696-2708.
    • (2009) Biophys J , vol.96 , pp. 2696-2708
    • Ariola, F.S.1    Li, Z.2    Cornejo, C.3    Bittman, R.4    Heikal, A.A.5
  • 64
    • 53849130991 scopus 로고    scopus 로고
    • BODIPY-cholesterol: a new tool to visualize sterol trafficking in living cells and organisms
    • Holtta-Vuori M, Uronen RL, Repakova J, Salonen E, Vattulainen I, et al. (2008) BODIPY-cholesterol: a new tool to visualize sterol trafficking in living cells and organisms. Traffic 9: 1839-1849.
    • (2008) Traffic , vol.9 , pp. 1839-1849
    • Holtta-Vuori, M.1    Uronen, R.L.2    Repakova, J.3    Salonen, E.4    Vattulainen, I.5
  • 65
    • 54049110711 scopus 로고    scopus 로고
    • Use of Bodipy-labeled sphingolipid and cholesterol analogs to examine membrane microdomains in cells
    • Marks DL, Bittman R, Pagano RE, (2008) Use of Bodipy-labeled sphingolipid and cholesterol analogs to examine membrane microdomains in cells. Histochem Cell Biol 130: 819-832.
    • (2008) Histochem Cell Biol , vol.130 , pp. 819-832
    • Marks, D.L.1    Bittman, R.2    Pagano, R.E.3
  • 66
    • 77952315637 scopus 로고    scopus 로고
    • High density lipoprotein structure-function and role in reverse cholesterol transport
    • Lund-Katz S, Phillips MC, (2010) High density lipoprotein structure-function and role in reverse cholesterol transport. Subcell Biochem 51: 183-227.
    • (2010) Subcell Biochem , vol.51 , pp. 183-227
    • Lund-Katz, S.1    Phillips, M.C.2
  • 67
    • 7044253307 scopus 로고    scopus 로고
    • Extracellular secretion of the Borrelia burgdorferi Oms28 porin and Bgp, a glycosaminoglycan binding protein
    • Cluss RG, Silverman DA, Stafford TR, (2004) Extracellular secretion of the Borrelia burgdorferi Oms28 porin and Bgp, a glycosaminoglycan binding protein. Infect Immun 72: 6279-6286.
    • (2004) Infect Immun , vol.72 , pp. 6279-6286
    • Cluss, R.G.1    Silverman, D.A.2    Stafford, T.R.3
  • 68
    • 0034595617 scopus 로고    scopus 로고
    • Lack of a role for iron in the Lyme disease pathogen
    • Posey JE, Gherardini FC, (2000) Lack of a role for iron in the Lyme disease pathogen. Science 288: 1651-1653.
    • (2000) Science , vol.288 , pp. 1651-1653
    • Posey, J.E.1    Gherardini, F.C.2
  • 69
    • 0031587871 scopus 로고    scopus 로고
    • Plasminogen is required for efficient dissemination of B. burgdorferi in ticks and for enhancement of spirochetemia in mice
    • Coleman JL, Gebbia JA, Piesman J, Degen JL, Bugge TH, et al. (1997) Plasminogen is required for efficient dissemination of B. burgdorferi in ticks and for enhancement of spirochetemia in mice. Cell 89: 1111-1119.
    • (1997) Cell , vol.89 , pp. 1111-1119
    • Coleman, J.L.1    Gebbia, J.A.2    Piesman, J.3    Degen, J.L.4    Bugge, T.H.5
  • 70
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh EG, Dyer WJ, (1959) A rapid method of total lipid extraction and purification. Can J Biochem Physiol 37: 911-917.
    • (1959) Can J Biochem Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 71
    • 33645467256 scopus 로고    scopus 로고
    • Sigma factor selectivity in Borrelia burgdorferi: RpoS recognition of the ospE/ospF/elp promoters is dependent on the sequence of the -10 region
    • Eggers CH, Caimano MJ, Radolf JD, (2006) Sigma factor selectivity in Borrelia burgdorferi: RpoS recognition of the ospE/ospF/elp promoters is dependent on the sequence of the -10 region. Mol Microbiol 59: 1859-1875.
    • (2006) Mol Microbiol , vol.59 , pp. 1859-1875
    • Eggers, C.H.1    Caimano, M.J.2    Radolf, J.D.3
  • 72
    • 0018254265 scopus 로고
    • A convenient and sensitive fluorescence assay for phospholipid vesicles using diphenylhexatriene
    • London E, Feligenson GW, (1978) A convenient and sensitive fluorescence assay for phospholipid vesicles using diphenylhexatriene. Anal Biochem 88: 203-211.
    • (1978) Anal Biochem , vol.88 , pp. 203-211
    • London, E.1    Feligenson, G.W.2
  • 73
    • 84857066761 scopus 로고    scopus 로고
    • The enolase of Borrelia burgdorferi is a plasminogen receptor released in outer membrane vesicles
    • Toledo A, Coleman JL, Kuhlow CJ, Crowley JT, Benach JL, (2012) The enolase of Borrelia burgdorferi is a plasminogen receptor released in outer membrane vesicles. Infect Immun 80: 359-368.
    • (2012) Infect Immun , vol.80 , pp. 359-368
    • Toledo, A.1    Coleman, J.L.2    Kuhlow, C.J.3    Crowley, J.T.4    Benach, J.L.5
  • 74
    • 84862539845 scopus 로고    scopus 로고
    • Lipid acquisition by intracellular Chlamydiae
    • Elwell CA, Engel JN, (2012) Lipid acquisition by intracellular Chlamydiae. Cell Microbiol 14: 1010-1018.
    • (2012) Cell Microbiol , vol.14 , pp. 1010-1018
    • Elwell, C.A.1    Engel, J.N.2
  • 75
    • 33745727558 scopus 로고    scopus 로고
    • Replication of Coxiella burnetii is inhibited in CHO K-1 cells treated with inhibitors of cholesterol metabolism
    • Howe D, Heinzen RA, (2005) Replication of Coxiella burnetii is inhibited in CHO K-1 cells treated with inhibitors of cholesterol metabolism. Ann N Y Acad Sci 1063: 123-129.
    • (2005) Ann N Y Acad Sci , vol.1063 , pp. 123-129
    • Howe, D.1    Heinzen, R.A.2
  • 76
    • 33644817117 scopus 로고    scopus 로고
    • Coxiella burnetii inhabits a cholesterol-rich vacuole and influences cellular cholesterol metabolism
    • Howe D, Heinzen RA, (2006) Coxiella burnetii inhabits a cholesterol-rich vacuole and influences cellular cholesterol metabolism. Cell Microbiol 8: 496-507.
    • (2006) Cell Microbiol , vol.8 , pp. 496-507
    • Howe, D.1    Heinzen, R.A.2
  • 77
    • 84866329972 scopus 로고    scopus 로고
    • Host HDL biogenesis machinery is recruited to the inclusion of Chlamydia trachomatis-infected cells and regulates chlamydial growth
    • Cox JV, Naher N, Abdelrahman YM, Belland RJ, (2012) Host HDL biogenesis machinery is recruited to the inclusion of Chlamydia trachomatis-infected cells and regulates chlamydial growth. Cell Microbiol 14: 1497-1512.
    • (2012) Cell Microbiol , vol.14 , pp. 1497-1512
    • Cox, J.V.1    Naher, N.2    Abdelrahman, Y.M.3    Belland, R.J.4
  • 78
    • 0029034043 scopus 로고
    • Lipid metabolism in Chlamydia trachomatis-infected cells: directed trafficking of Golgi-derived sphingolipids to the chlamydial inclusion
    • Hackstadt T, Scidmore MA, Rockey DD, (1995) Lipid metabolism in Chlamydia trachomatis-infected cells: directed trafficking of Golgi-derived sphingolipids to the chlamydial inclusion. Proc Natl Acad Sci U S A 92: 4877-4881.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 4877-4881
    • Hackstadt, T.1    Scidmore, M.A.2    Rockey, D.D.3
  • 79
    • 0037974695 scopus 로고    scopus 로고
    • Golgi-dependent transport of cholesterol to the Chlamydia trachomatis inclusion
    • Carabeo RA, Mead DJ, Hackstadt T, (2003) Golgi-dependent transport of cholesterol to the Chlamydia trachomatis inclusion. Proc Natl Acad Sci U S A 100: 6771-6776.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6771-6776
    • Carabeo, R.A.1    Mead, D.J.2    Hackstadt, T.3
  • 80
    • 78649356212 scopus 로고    scopus 로고
    • Coxiella burnetii expresses a functional Delta24 sterol reductase
    • Gilk SD, Beare PA, Heinzen RA, (2010) Coxiella burnetii expresses a functional Delta24 sterol reductase. J Bacteriol 192: 6154-6159.
    • (2010) J Bacteriol , vol.192 , pp. 6154-6159
    • Gilk, S.D.1    Beare, P.A.2    Heinzen, R.A.3
  • 81
    • 0031932921 scopus 로고    scopus 로고
    • Isolation and characterization of the outer membrane of Borrelia hermsii
    • Shang ES, Skare JT, Exner MM, Blanco DR, Kagan BL, et al. (1998) Isolation and characterization of the outer membrane of Borrelia hermsii. Infect Immun 66: 1082-1091.
    • (1998) Infect Immun , vol.66 , pp. 1082-1091
    • Shang, E.S.1    Skare, J.T.2    Exner, M.M.3    Blanco, D.R.4    Kagan, B.L.5
  • 82
    • 0028826186 scopus 로고
    • Virulent strain associated outer membrane proteins of Borrelia burgdorferi
    • Skare JT, Shang ES, Foley DM, Blanco DR, Champion CI, et al. (1995) Virulent strain associated outer membrane proteins of Borrelia burgdorferi. J Clin Invest 96: 2380-2392.
    • (1995) J Clin Invest , vol.96 , pp. 2380-2392
    • Skare, J.T.1    Shang, E.S.2    Foley, D.M.3    Blanco, D.R.4    Champion, C.I.5
  • 83
    • 0028067942 scopus 로고
    • Isolation and partial characterization of Borrelia burgdorferi inner and outer membranes by using isopycnic centrifugation
    • Bledsoe HA, Carroll JA, Whelchel TR, Farmer MA, Dorward DW, et al. (1994) Isolation and partial characterization of Borrelia burgdorferi inner and outer membranes by using isopycnic centrifugation. J Bacteriol 176: 7447-7455.
    • (1994) J Bacteriol , vol.176 , pp. 7447-7455
    • Bledsoe, H.A.1    Carroll, J.A.2    Whelchel, T.R.3    Farmer, M.A.4    Dorward, D.W.5
  • 84
    • 0026596492 scopus 로고
    • Interactions between extracellular Borrelia burgdorferi proteins and non-Borrelia-directed immunoglobulin M antibodies
    • Dorward DW, Huguenel ED, Davis G, Garon CF, (1992) Interactions between extracellular Borrelia burgdorferi proteins and non-Borrelia-directed immunoglobulin M antibodies. Infect Immun 60: 838-844.
    • (1992) Infect Immun , vol.60 , pp. 838-844
    • Dorward, D.W.1    Huguenel, E.D.2    Davis, G.3    Garon, C.F.4
  • 85
    • 0026010650 scopus 로고
    • Immune capture and detection of Borrelia burgdorferi antigens in urine, blood, or tissues from infected ticks, mice, dogs, and humans
    • Dorward DW, Schwan TG, Garon CF, (1991) Immune capture and detection of Borrelia burgdorferi antigens in urine, blood, or tissues from infected ticks, mice, dogs, and humans. J Clin Microbiol 29: 1162-1170.
    • (1991) J Clin Microbiol , vol.29 , pp. 1162-1170
    • Dorward, D.W.1    Schwan, T.G.2    Garon, C.F.3
  • 86
    • 0027228235 scopus 로고
    • Specific adherence of Borrelia burgdorferi extracellular vesicles to human endothelial cells in culture
    • Shoberg RJ, Thomas DD, (1993) Specific adherence of Borrelia burgdorferi extracellular vesicles to human endothelial cells in culture. Infect Immun 61: 3892-3900.
    • (1993) Infect Immun , vol.61 , pp. 3892-3900
    • Shoberg, R.J.1    Thomas, D.D.2
  • 87
    • 0028875297 scopus 로고
    • Borrelia burgdorferi vesicle production occurs via a mechanism independent of immunoglobulin M involvement
    • Shoberg RJ, Thomas DD, (1995) Borrelia burgdorferi vesicle production occurs via a mechanism independent of immunoglobulin M involvement. Infect Immun 63: 4857-4861.
    • (1995) Infect Immun , vol.63 , pp. 4857-4861
    • Shoberg, R.J.1    Thomas, D.D.2
  • 88
    • 80053895756 scopus 로고    scopus 로고
    • Characterization of multiprotein complexes of the Borrelia burgdorferi outer membrane vesicles
    • Yang X, Promnares K, Qin J, He M, Shroder DY, et al. (2011) Characterization of multiprotein complexes of the Borrelia burgdorferi outer membrane vesicles. J Proteome Res 10: 4556-4566.
    • (2011) J Proteome Res , vol.10 , pp. 4556-4566
    • Yang, X.1    Promnares, K.2    Qin, J.3    He, M.4    Shroder, D.Y.5
  • 89
    • 0033945432 scopus 로고    scopus 로고
    • Comparison of protection in rabbits against host-adapted and cultivated Borrelia burgdorferi following infection-derived immunity or immunization with outer membrane vesicles or outer surface protein A
    • Shang ES, Champion CI, Wu XY, Skare JT, Blanco DR, et al. (2000) Comparison of protection in rabbits against host-adapted and cultivated Borrelia burgdorferi following infection-derived immunity or immunization with outer membrane vesicles or outer surface protein A. Infect Immun 68: 4189-4199.
    • (2000) Infect Immun , vol.68 , pp. 4189-4199
    • Shang, E.S.1    Champion, C.I.2    Wu, X.Y.3    Skare, J.T.4    Blanco, D.R.5
  • 90
    • 77749309281 scopus 로고    scopus 로고
    • Virulence and immunomodulatory roles of bacterial outer membrane vesicles
    • Ellis TN, Kuehn MJ, (2010) Virulence and immunomodulatory roles of bacterial outer membrane vesicles. Microbiol Mol Biol Rev 74: 81-94.
    • (2010) Microbiol Mol Biol Rev , vol.74 , pp. 81-94
    • Ellis, T.N.1    Kuehn, M.J.2
  • 91
    • 0031014146 scopus 로고    scopus 로고
    • Release of lipopolysaccharide from intracellular compartments containing Salmonella typhimurium to vesicles of the host epithelial cell
    • Garcia-del Portillo F, Stein MA, Finlay BB, (1997) Release of lipopolysaccharide from intracellular compartments containing Salmonella typhimurium to vesicles of the host epithelial cell. Infect Immun 65: 24-34.
    • (1997) Infect Immun , vol.65 , pp. 24-34
    • Garcia-del Portillo, F.1    Stein, M.A.2    Finlay, B.B.3
  • 92
    • 42949174067 scopus 로고    scopus 로고
    • Proteomic characterization of the whole secretome of Legionella pneumophila and functional analysis of outer membrane vesicles
    • Galka F, Wai SN, Kusch H, Engelmann S, Hecker M, et al. (2008) Proteomic characterization of the whole secretome of Legionella pneumophila and functional analysis of outer membrane vesicles. Infect Immun 76: 1825-1836.
    • (2008) Infect Immun , vol.76 , pp. 1825-1836
    • Galka, F.1    Wai, S.N.2    Kusch, H.3    Engelmann, S.4    Hecker, M.5
  • 93
    • 0037303720 scopus 로고    scopus 로고
    • Interaction of Actinobacillus actinomycetemcomitans outer membrane vesicles with HL60 cells does not require leukotoxin
    • Demuth DR, James D, Kowashi Y, Kato S, (2003) Interaction of Actinobacillus actinomycetemcomitans outer membrane vesicles with HL60 cells does not require leukotoxin. Cell Microbiol 5: 111-121.
    • (2003) Cell Microbiol , vol.5 , pp. 111-121
    • Demuth, D.R.1    James, D.2    Kowashi, Y.3    Kato, S.4
  • 94
    • 0021671855 scopus 로고
    • Isolation and cultivation of Lyme disease spirochetes
    • Barbour AG, (1984) Isolation and cultivation of Lyme disease spirochetes. Yale J Biol Med 57: 521-525.
    • (1984) Yale J Biol Med , vol.57 , pp. 521-525
    • Barbour, A.G.1
  • 95
    • 0026721358 scopus 로고
    • Selection of an escape variant of Borrelia burgdorferi by use of bactericidal monoclonal antibodies to OspB
    • Coleman JL, Rogers RC, Benach JL, (1992) Selection of an escape variant of Borrelia burgdorferi by use of bactericidal monoclonal antibodies to OspB. Infect Immun 60: 3098-3104.
    • (1992) Infect Immun , vol.60 , pp. 3098-3104
    • Coleman, J.L.1    Rogers, R.C.2    Benach, J.L.3


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