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Volumn 5, Issue 2, 2014, Pages

Selective association of outer surface lipoproteins with the lipid rafts of Borrelia burgdorferi

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; OUTER SURFACE PROTEIN A; OUTER SURFACE PROTEIN B; OUTER SURFACE PROTEIN C; UNCLASSIFIED DRUG;

EID: 84899742408     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00899-14     Document Type: Article
Times cited : (31)

References (73)
  • 3
    • 0017355270 scopus 로고
    • The Spirochetes
    • Johnson RC. 1977. The Spirochetes. Annu. Rev. Microbiol. 31:89-106. http://dx.doi.org/10.1146/annurev.mi.31.100177.000513.
    • (1977) Annu. Rev. Microbiol. , vol.31 , pp. 89-106
    • Johnson, R.C.1
  • 4
  • 5
    • 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
  • 6
    • 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
  • 7
    • 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
  • 8
    • 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, Norgard MV. 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    Norgard, M.V.6
  • 9
    • 0029054274 scopus 로고
    • Membrane topology of Borrelia burgdorferi and Treponema pallidum lipoproteins
    • Jones JD, Bourell KW, Norgard MV, Radolf JD. 1995. Membrane topology of Borrelia burgdorferi and Treponema pallidum lipoproteins. Infect. Immun. 63:2424-2434.
    • (1995) Infect. Immun. , vol.63 , pp. 2424-2434
    • Jones, J.D.1    Bourell, K.W.2    Norgard, M.V.3    Radolf, J.D.4
  • 11
    • 0141780838 scopus 로고    scopus 로고
    • Acylated cholesteryl galactoside as a novel immunogenic motif in Borrelia burgdorferi sensu stricto
    • Schröder NW, Schombel U, Heine H, Göbel UB, Zähringer U, Schumann RR. 2003. Acylated cholesteryl galactoside as a novel immunogenic motif in Borrelia burgdorferi sensu stricto. J. Biol. Chem. 278: 33645-33653. http://dx.doi.org/10.1074/jbc.M305799200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 33645-33653
    • Schröder, N.W.1    Schombel, U.2    Heine, H.3    Göbel, U.B.4    Zähringer, U.5    Schumann, R.R.6
  • 12
    • 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
    • Stübs G, Fingerle V, Wilske B, Göbel UB, Zähringer U, Schumann RR, Schröder NW. 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. http://dx.doi.org/ 10.1074/jbc.M809575200.
    • (2009) J. Biol. Chem. , vol.284 , pp. 13326-13334
    • Stübs, G.1    Fingerle, V.2    Wilske, B.3    Göbel, U.B.4    Zähringer, U.5    Schumann, R.R.6    Schröder, N.W.7
  • 13
    • 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. http://dx.doi.org/ 10.1128/IAI.71.9.5324-5331.2003.
    • (2003) Infect. Immun. , vol.71 , pp. 5324-5331
    • Lin, M.1    Rikihisa, Y.2
  • 14
    • 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
  • 15
    • 0029148371 scopus 로고
    • Unique cholesteryl glucosides in Helicobacter pylori: Composition and structural analysis
    • Hirai Y, Haque M, Yoshida T, Yokota K, Yasuda T, Oguma K. 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    Oguma, K.6
  • 16
    • 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
  • 18
    • 77956292192 scopus 로고    scopus 로고
    • Functional microdomains in bacterial membranes
    • López D, Kolter R. 2010. Functional microdomains in bacterial membranes. Genes Dev. 24:1893-1902. http://dx.doi.org/10.1101/ gad.1945010.
    • (2010) Genes Dev. , vol.24 , pp. 1893-1902
    • López, D.1    Kolter, R.2
  • 19
    • 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. http:// dx.doi.org/10.1074/jbc.R000005200.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 20
    • 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. http://dx.doi.org/10.1016/S0959-440X(02)00351-2.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 480-486
    • London, E.1
  • 21
    • 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.PART 1 , pp. 1-9
    • Brown, R.E.1
  • 22
    • 45449105538 scopus 로고    scopus 로고
    • Proteins and cholesterol-rich domains
    • Epand RM. 2008. Proteins and cholesterol-rich domains. Biochim. Biophys. Acta 1778:1576-1582. http://dx.doi.org/10.1016/ j.bbamem.2008.03.016.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1576-1582
    • Epand, R.M.1
  • 23
    • 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. http://dx.doi.org/10.1016/S0006-3495(97)78067-6.
    • (1997) Biophys. J. , vol.73 , pp. 267-276
    • Chen, Z.1    Rand, R.P.2
  • 24
    • 0035424718 scopus 로고    scopus 로고
    • Implications of lipid microdomains for membrane curvature, budding and fission
    • Huttner WB, Zimmerberg J. 2001. Implications of lipid microdomains for membrane curvature, budding and fission. Curr. Opin. Cell Biol. 13: 478-484. http://dx.doi.org/10.1016/S0955-0674(00)00239-8.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 478-484
    • Huttner, W.B.1    Zimmerberg, J.2
  • 25
    • 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. http://dx.doi.org/10.1242/jcs.00840.
    • (2003) J. Cell Sci. , vol.116 , pp. 4707-4714
    • Nichols, B.1
  • 26
    • 1842484428 scopus 로고    scopus 로고
    • Lipid rafts and the regulation of exocytosis
    • Salaün C, James DJ, Chamberlain LH. 2004. Lipid rafts and the regulation of exocytosis. Traffic 5:255-264. http://dx.doi.org/10.1111/j.1600-0854.2004.0162.x.
    • (2004) Traffic , vol.5 , pp. 255-264
    • Salaün, C.1    James, D.J.2    Chamberlain, L.H.3
  • 27
    • 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, London E, Garcia-Monco JC, Benach JL. 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. http:// dx.doi.org/10.1016/j.chom.2010.09.001.
    • (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    London, E.6    Garcia-Monco, J.C.7    Benach, J.L.8
  • 28
    • 84878482841 scopus 로고    scopus 로고
    • Proving lipid rafts exist: Membrane domains in the prokaryote Borrelia burgdorferi have the same properties as eukaryotic lipid rafts
    • LaRocca TJ, Pathak P, Chiantia S, Toledo A, Silvius JR, Benach JL, London E. 2013. Proving lipid rafts exist: membrane domains in the prokaryote Borrelia burgdorferi have the same properties as eukaryotic lipid rafts. PLoS Pathog. 9:e1003353. http://dx.doi.org/10.1371/ journal.ppat.1003353.
    • (2013) PLoS Pathog. , vol.9
    • LaRocca, T.J.1    Pathak, P.2    Chiantia, S.3    Toledo, A.4    Silvius, J.R.5    Benach, J.L.6    London, E.7
  • 30
    • 0024421344 scopus 로고
    • Molecular analysis of linear plasmid-encoded major surface proteins, OspA and OspB, of the Lyme disease spirochaete Borrelia burgdorferi
    • Bergström S, Bundoc VG, Barbour AG. 1989. Molecular analysis of linear plasmid-encoded major surface proteins, OspA and OspB, of the Lyme disease spirochaete Borrelia burgdorferi. Mol. Microbiol. 3:479-486. http://dx.doi.org/10.1111/j.1365-2958.1989.tb00194.x.
    • (1989) Mol. Microbiol. , vol.3 , pp. 479-486
    • Bergström, S.1    Bundoc, V.G.2    Barbour, A.G.3
  • 31
    • 0023906178 scopus 로고
    • A murine IgM monoclonal antibody binds an antigenic determinant in outer surface protein A, an immunodominant basic protein of the Lyme disease spirochete
    • Benach JL, Coleman JL, Golightly MG. 1988. A murine IgM monoclonal antibody binds an antigenic determinant in outer surface protein A, an immunodominant basic protein of the Lyme disease spirochete. J. Immunol. 140:265-272.
    • (1988) J. Immunol. , vol.140 , pp. 265-272
    • Benach, J.L.1    Coleman, J.L.2    Golightly, M.G.3
  • 32
    • 0028926240 scopus 로고
    • Induction of an outer surface protein on Borrelia burgdorferi during tick feeding
    • Schwan TG, Piesman J, Golde WT, Dolan MC, Rosa PA. 1995. Induction of an outer surface protein on Borrelia burgdorferi during tick feeding. Proc. Natl. Acad. Sci. U. S. A. 92:2909-2913. http://dx.doi.org/ 10.1073/pnas.92.7.2909.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 2909-2913
    • Schwan, T.G.1    Piesman, J.2    Golde, W.T.3    Dolan, M.C.4    Rosa, P.A.5
  • 33
    • 0025202254 scopus 로고
    • Protection of mice against the Lyme disease agent by immunizing with recombinant OspA
    • Fikrig E, Barthold SW, Kantor FS, Flavell RA. 1990. Protection of mice against the Lyme disease agent by immunizing with recombinant OspA. Science 250:553-556. http://dx.doi.org/10.1126/science.2237407.
    • (1990) Science , vol.250 , pp. 553-556
    • Fikrig, E.1    Barthold, S.W.2    Kantor, F.S.3    Flavell, R.A.4
  • 36
    • 1542283705 scopus 로고    scopus 로고
    • Essential role for OspA/B in the life cycle of the Lyme disease spirochete
    • Yang XF, Pal U, Alani SM, Fikrig E, Norgard MV. 2004. Essential role for OspA/B in the life cycle of the Lyme disease spirochete. J. Exp. Med. 199:641-648. http://dx.doi.org/10.1084/jem.20031960.
    • (2004) J. Exp. Med. , vol.199 , pp. 641-648
    • Yang, X.F.1    Pal, U.2    Alani, S.M.3    Fikrig, E.4    Norgard, M.V.5
  • 37
    • 17844363213 scopus 로고    scopus 로고
    • The versatile roles of antibodies in Borrelia infections
    • Connolly SE, Benach JL. 2005. The versatile roles of antibodies in Borrelia infections. Nat. Rev. Microbiol. 3:411-420. http://dx.doi.org/10.1038/ nrmicro1149.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 411-420
    • Connolly, S.E.1    Benach, J.L.2
  • 38
    • 67649811039 scopus 로고    scopus 로고
    • The bactericidal effect of a complement-independent antibody is osmolytic and specific to Borrelia
    • LaRocca TJ, Holthausen DJ, Hsieh C, Renken C, Mannella CA, Benach JL. 2009. The bactericidal effect of a complement-independent antibody is osmolytic and specific to Borrelia. Proc. Natl. Acad. Sci. U. S. A. 106: 10752-10757. http://dx.doi.org/10.1073/pnas.0901858106.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 10752-10757
    • LaRocca, T.J.1    Holthausen, D.J.2    Hsieh, C.3    Renken, C.4    Mannella, C.A.5    Benach, J.L.6
  • 39
    • 0030901450 scopus 로고    scopus 로고
    • Characterization of the physiological requirements for the bactericidal effects of a monoclonal antibody to OspB of Borrelia burgdorferi by confocal microscopy
    • Escudero R, Halluska ML, Backenson PB, Coleman JL, Benach JL. 1997. Characterization of the physiological requirements for the bactericidal effects of a monoclonal antibody to OspB of Borrelia burgdorferi by confocal microscopy. Infect. Immun. 65:1908-1915.
    • (1997) Infect. Immun. , vol.65 , pp. 1908-1915
    • Escudero, R.1    Halluska, M.L.2    Backenson, P.B.3    Coleman, J.L.4    Benach, J.L.5
  • 42
    • 0027537039 scopus 로고
    • Transcriptional analyses and mapping of the ospC gene in Lyme disease spirochetes
    • Marconi RT, Samuels DS, Garon CF. 1993. Transcriptional analyses and mapping of the ospC gene in Lyme disease spirochetes. J. Bacteriol. 175: 926-932.
    • (1993) J. Bacteriol. , vol.175 , pp. 926-932
    • Marconi, R.T.1    Samuels, D.S.2    Garon, C.F.3
  • 43
    • 28044444737 scopus 로고    scopus 로고
    • Demonstration of OspC type diversity in invasive human Lyme disease isolates and identification of previously uncharacterized epitopes that define the specificity of the OspC murine antibody response
    • Earnhart CG, Buckles EL, Dumler JS, Marconi RT. 2005. Demonstration of OspC type diversity in invasive human Lyme disease isolates and identification of previously uncharacterized epitopes that define the specificity of the OspC murine antibody response. Infect. Immun. 73: 7869-7877. http://dx.doi.org/10.1128/IAI.73.12.7869-7877.2005.
    • (2005) Infect. Immun. , vol.73 , pp. 7869-7877
    • Earnhart, C.G.1    Buckles, E.L.2    Dumler, J.S.3    Marconi, R.T.4
  • 45
    • 84884221809 scopus 로고    scopus 로고
    • Multilocus sequence typing of Borrelia burgdorferi suggests existence of lineages with differential pathogenic properties in humans
    • Hanincova K, Mukherjee P, Ogden NH, Margos G, Wormser GP, Reed KD, Meece JK, Vandermause MF, Schwartz I. 2013. Multilocus sequence typing of Borrelia burgdorferi suggests existence of lineages with differential pathogenic properties in humans. PLoS One 8:e73066. http:// dx.doi.org/10.1371/journal.pone.0073066.
    • (2013) PLoS One , vol.8
    • Hanincova, K.1    Mukherjee, P.2    Ogden, N.H.3    Margos, G.4    Wormser, G.P.5    Reed, K.D.6    Meece, J.K.7    Vandermause, M.F.8    Schwartz, I.9
  • 47
    • 33646045625 scopus 로고    scopus 로고
    • Borrelia burgdorferi sensu stricto invasiveness is correlated with OspCplasminogen affinity
    • Lagal V, Portnoï D, Faure G, Postic D, Baranton G. 2006. Borrelia burgdorferi sensu stricto invasiveness is correlated with OspCplasminogen affinity. Microbes Infect. 8:645-652. http://dx.doi.org/ 10.1016/j.micinf.2005.08.017.
    • (2006) Microbes Infect. , vol.8 , pp. 645-652
    • Lagal, V.1    Portnoï, D.2    Faure, G.3    Postic, D.4    Baranton, G.5
  • 48
    • 0029039462 scopus 로고
    • Borrelia burgdorferi binds plasminogen, resulting in enhanced penetration of endothelial monolayers
    • Coleman JL, Sellati TJ, Testa JE, Kew RR, Furie MB, Benach JL. 1995. Borrelia burgdorferi binds plasminogen, resulting in enhanced penetration of endothelial monolayers. Infect. Immun. 63:2478-2484.
    • (1995) Infect. Immun. , vol.63 , pp. 2478-2484
    • Coleman, J.L.1    Sellati, T.J.2    Testa, J.E.3    Kew, R.R.4    Furie, M.B.5    Benach, J.L.6
  • 50
    • 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, Kariu T, Wang Y, Pal U. 2011. Characterization of multiprotein complexes of the Borrelia burgdorferi outer membrane vesicles. J. Proteome Res. 10:4556-4566. http:// dx.doi.org/10.1021/pr200395b.
    • (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    Kariu, T.6    Wang, Y.7    Pal, U.8
  • 53
    • 84876702079 scopus 로고    scopus 로고
    • The HtrA protease of Borrelia burgdorferi degrades outer membrane protein BmpD and chemotaxis phosphatase CheX
    • Coleman JL, Crowley JT, Toledo AM, Benach JL. 2013. The HtrA protease of Borrelia burgdorferi degrades outer membrane protein BmpD and chemotaxis phosphatase CheX. Mol. Microbiol. 88:619-633. http:// dx.doi.org/10.1111/mmi.12213.
    • (2013) Mol. Microbiol. , vol.88 , pp. 619-633
    • Coleman, J.L.1    Crowley, J.T.2    Toledo, A.M.3    Benach, J.L.4
  • 54
    • 0042845804 scopus 로고    scopus 로고
    • Fluorescence energy transfer reveals microdomain formation at physiological temperatures in lipid mixtures modeling the outer leaflet of the plasma membrane
    • Silvius JR. 2003. Fluorescence energy transfer reveals microdomain formation at physiological temperatures in lipid mixtures modeling the outer leaflet of the plasma membrane. Biophys. J. 85:1034-1045. http:// dx.doi.org/10.1016/S0006-3495(03)74542-1.
    • (2003) Biophys. J. , vol.85 , pp. 1034-1045
    • Silvius, J.R.1
  • 55
    • 0027158861 scopus 로고
    • The cryptic ospC gene of Borrelia burgdorferi B31 is located on a circular plasmid
    • Sadziene A, Wilske B, Ferdows MS, Barbour AG. 1993. The cryptic ospC gene of Borrelia burgdorferi B31 is located on a circular plasmid. Infect. Immun. 61:2192-2195.
    • (1993) Infect. Immun. , vol.61 , pp. 2192-2195
    • Sadziene, A.1    Wilske, B.2    Ferdows, M.S.3    Barbour, A.G.4
  • 56
    • 0035971089 scopus 로고    scopus 로고
    • Crystal structure of Lyme disease antigen outer surface protein C from Borrelia burgdorferi
    • Eicken C, Sharma V, Klabunde T, Owens RT, Pikas DS, Höök M, Sacchettini JC. 2001. Crystal structure of Lyme disease antigen outer surface protein C from Borrelia burgdorferi. J. Biol. Chem. 276: 10010-10015. http://dx.doi.org/10.1074/jbc.M010062200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10010-10015
    • Eicken, C.1    Sharma, V.2    Klabunde, T.3    Owens, R.T.4    Pikas, D.S.5    Höök, M.6    Sacchettini, J.C.7
  • 57
    • 0035283085 scopus 로고    scopus 로고
    • Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi
    • Kumaran D, Eswaramoorthy S, Luft BJ, Koide S, Dunn JJ, Lawson CL, Swaminathan S. 2001. Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi. EMBO J. 20: 971-978. http://dx.doi.org/10.1093/emboj/20.5.971.
    • (2001) EMBO J. , vol.20 , pp. 971-978
    • Kumaran, D.1    Eswaramoorthy, S.2    Luft, B.J.3    Koide, S.4    Dunn, J.J.5    Lawson, C.L.6    Swaminathan, S.7
  • 58
    • 75149192610 scopus 로고    scopus 로고
    • Borrelia burgdorferi locus BB0795 encodes a BamA orthologue required for growth and efficient localization of outer membrane proteins
    • Lenhart TR, Akins DR. 2010. Borrelia burgdorferi locus BB0795 encodes a BamA orthologue required for growth and efficient localization of outer membrane proteins. Mol. Microbiol. 75:692-709. http://dx.doi.org/ 10.1111/j.1365-2958.2009.07015.x.
    • (2010) Mol. Microbiol. , vol.75 , pp. 692-709
    • Lenhart, T.R.1    Akins, D.R.2
  • 59
    • 80655125434 scopus 로고    scopus 로고
    • Determination of borrelia surface lipoprotein anchor topology by surface proteolysis
    • Chen S, Kumru OS, Zückert WR. 2011. Determination of borrelia surface lipoprotein anchor topology by surface proteolysis. J. Bacteriol. 193: 6379-6383. http://dx.doi.org/10.1128/JB.05849-11.
    • (2011) J. Bacteriol. , vol.193 , pp. 6379-6383
    • Chen, S.1    Kumru, O.S.2    Zückert, W.R.3
  • 61
    • 0037128163 scopus 로고    scopus 로고
    • An immune evasion mechanism for spirochetal persistence in Lyme borreliosis
    • Liang FT, Jacobs MB, Bowers LC, Philipp MT. 2002. An immune evasion mechanism for spirochetal persistence in Lyme borreliosis. J. Exp. Med. 195:415-422. http://dx.doi.org/10.1084/jem.20011870.
    • (2002) J. Exp. Med. , vol.195 , pp. 415-422
    • Liang, F.T.1    Jacobs, M.B.2    Bowers, L.C.3    Philipp, M.T.4
  • 62
    • 67650080598 scopus 로고    scopus 로고
    • OspC-independent infection and dissemination by host-adapted Borrelia burgdorferi
    • Tilly K, Bestor A, Dulebohn DP, Rosa PA. 2009. OspC-independent infection and dissemination by host-adapted Borrelia burgdorferi. Infect. Immun. 77:2672-2682. http://dx.doi.org/10.1128/IAI.01193-08.
    • (2009) Infect. Immun. , vol.77 , pp. 2672-2682
    • Tilly, K.1    Bestor, A.2    Dulebohn, D.P.3    Rosa, P.A.4
  • 63
    • 84880135672 scopus 로고    scopus 로고
    • Lipoprotein succession in Borrelia burgdorferi: Similar but distinct roles for OspC and VlsE at different stages of mammalian infection
    • Tilly K, Bestor A, Rosa PA. 2013. Lipoprotein succession in Borrelia burgdorferi: similar but distinct roles for OspC and VlsE at different stages of mammalian infection. Mol. Microbiol. 89:216-227. http://dx.doi.org/ 10.1111/mmi.12271.
    • (2013) Mol. Microbiol. , vol.89 , pp. 216-227
    • Tilly, K.1    Bestor, A.2    Rosa, P.A.3
  • 64
    • 55849126646 scopus 로고    scopus 로고
    • Outer surface protein A protects Lyme disease spirochetes from acquired host immunity in the tick vector
    • Battisti JM, Bono JL, Rosa PA, Schrumpf ME, Schwan TG, Policastro PF. 2008. Outer surface protein A protects Lyme disease spirochetes from acquired host immunity in the tick vector. Infect. Immun. 76:5228-5237. http://dx.doi.org/10.1128/IAI.00410-08.
    • (2008) Infect. Immun. , vol.76 , pp. 5228-5237
    • Battisti, J.M.1    Bono, J.L.2    Rosa, P.A.3    Schrumpf, M.E.4    Schwan, T.G.5    Policastro, P.F.6
  • 65
    • 0026695713 scopus 로고
    • Characterization of antigenic determinants of Borrelia burgdorferi shared by other bacteria
    • Coleman JL, Benach JL. 1992. Characterization of antigenic determinants of Borrelia burgdorferi shared by other bacteria. J. Infect. Dis. 165: 658-666. http://dx.doi.org/10.1093/infdis/165.4.658.
    • (1992) J. Infect. Dis. , vol.165 , pp. 658-666
    • Coleman, J.L.1    Benach, J.L.2
  • 66
    • 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
  • 67
    • 77951151121 scopus 로고    scopus 로고
    • Identification of residues within ligand-binding domain 1 (LBD1) of the Borrelia burgdorferi OspC protein required for function in the mammalian environment
    • Earnhart CG, Leblanc DV, Alix KE, Desrosiers DC, Radolf JD, Marconi RT. 2010. Identification of residues within ligand-binding domain 1 (LBD1) of the Borrelia burgdorferi OspC protein required for function in the mammalian environment. Mol. Microbiol. 76:393-408. http:// dx.doi.org/10.1111/j.1365-2958.2010.07103.x.
    • (2010) Mol. Microbiol. , vol.76 , pp. 393-408
    • Earnhart, C.G.1    Leblanc, D.V.2    Alix, K.E.3    Desrosiers, D.C.4    Radolf, J.D.5    Marconi, R.T.6
  • 68
    • 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. http://dx.doi.org/ 10.1128/IAI.05836-11.
    • (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
  • 69
    • 0242407459 scopus 로고    scopus 로고
    • AadA confers streptomycin resistance in Borrelia burgdorferi
    • Frank KL, Bundle SF, Kresge ME, Eggers CH, Samuels DS. 2003. aadA confers streptomycin resistance in Borrelia burgdorferi. J. Bacteriol. 185: 6723-6727. http://dx.doi.org/10.1128/JB.185.22.6723-6727.2003.
    • (2003) J. Bacteriol. , vol.185 , pp. 6723-6727
    • Frank, K.L.1    Bundle, S.F.2    Kresge, M.E.3    Eggers, C.H.4    Samuels, D.S.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. http://dx.doi.org/ 10.1139/o59-099.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 71
    • 69449102231 scopus 로고    scopus 로고
    • On the use of Ripley's K-function and its derivatives to analyze domain size
    • Kiskowski MA, Hancock JF, Kenworthy AK. 2009. On the use of Ripley's K-function and its derivatives to analyze domain size. Biophys. J. 97: 1095-1103. http://dx.doi.org/10.1016/j.bpj.2009.05.039.
    • (2009) Biophys. J. , vol.97 , pp. 1095-1103
    • Kiskowski, M.A.1    Hancock, J.F.2    Kenworthy, A.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.