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Volumn 6, Issue 9, 2011, Pages

Requirement of the CXXC motif of novel Francisella infectivity potentiator protein B FipB, and fipA in virulence of f. tularensis subsp. tularensis

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; BACTERIAL PROTEIN; CYSTEINE; FRANCISELLA INFECTIVITY POTENTIATOR A PROTEIN; FRANCISELLA INFECTIVITY POTENTIATOR B PROTEIN; MACROPHAGE INFECTIVITY POTENTIATOR PROTEIN; UNCLASSIFIED DRUG; VIRULENCE FACTOR; ISOPROTEIN;

EID: 80052537034     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0024611     Document Type: Article
Times cited : (26)

References (46)
  • 1
    • 0004227306 scopus 로고    scopus 로고
    • New York, Random House
    • Alibek K, (1999) Biohazard New York Random House.
    • (1999) Biohazard
    • Alibek, K.1
  • 2
    • 0035816032 scopus 로고    scopus 로고
    • Tularemia as a biological weapon: medical and public health management
    • Dennis DT, Inglesby TV, Henderson DA, Bartlett JG, Ascher MS, et al. (2001) Tularemia as a biological weapon: medical and public health management. Jama 285: 2763-2773.
    • (2001) Jama , vol.285 , pp. 2763-2773
    • Dennis, D.T.1    Inglesby, T.V.2    Henderson, D.A.3    Bartlett, J.G.4    Ascher, M.S.5
  • 3
    • 78149353989 scopus 로고    scopus 로고
    • Francisella tularensis vaccines
    • Oyston PC, (2009) Francisella tularensis vaccines. Vaccine 27 (Suppl 4): D48-51.
    • (2009) Vaccine , vol.27 , Issue.SUPPL. 4 , pp. 48-51
    • Oyston, P.C.1
  • 4
    • 0041929305 scopus 로고    scopus 로고
    • Francisella tularensis selectively induces proinflammatory changes in endothelial cells
    • Forestal CA, Benach JL, Carbonara C, Italo JK, Lisinski TJ, et al. (2003) Francisella tularensis selectively induces proinflammatory changes in endothelial cells. J Immunol 171: 2563-2570.
    • (2003) J Immunol , vol.171 , pp. 2563-2570
    • Forestal, C.A.1    Benach, J.L.2    Carbonara, C.3    Italo, J.K.4    Lisinski, T.J.5
  • 5
    • 0026469140 scopus 로고
    • Early pathogenesis of infection in the liver with the facultative intracellular bacteria Listeria monocytogenes, Francisella tularensis, and Salmonella typhimurium involves lysis of infected hepatocytes by leukocytes
    • Conlan JW, North RJ, (1992) Early pathogenesis of infection in the liver with the facultative intracellular bacteria Listeria monocytogenes, Francisella tularensis, and Salmonella typhimurium involves lysis of infected hepatocytes by leukocytes. Infect Immun 60: 5164-5171.
    • (1992) Infect Immun , vol.60 , pp. 5164-5171
    • Conlan, J.W.1    North, R.J.2
  • 6
    • 0025834766 scopus 로고
    • Growth of Francisella spp. in rodent macrophages
    • Anthony LD, Burke RD, Nano FE, (1991) Growth of Francisella spp. in rodent macrophages. Infect Immun 59: 3291-3296.
    • (1991) Infect Immun , vol.59 , pp. 3291-3296
    • Anthony, L.D.1    Burke, R.D.2    Nano, F.E.3
  • 7
    • 46249110662 scopus 로고    scopus 로고
    • Acquisition of the vacuolar ATPase proton pump and phagosome acidification are essential for escape of Francisella tularensis into the macrophage cytosol
    • Santic M, Asare R, Skrobonja I, Jones S, Abu Kwaik Y, (2008) Acquisition of the vacuolar ATPase proton pump and phagosome acidification are essential for escape of Francisella tularensis into the macrophage cytosol. Infect Immun 76: 2671-2677.
    • (2008) Infect Immun , vol.76 , pp. 2671-2677
    • Santic, M.1    Asare, R.2    Skrobonja, I.3    Jones, S.4    Abu Kwaik, Y.5
  • 8
    • 65449134827 scopus 로고    scopus 로고
    • Francisella tularensis phagosomal escape does not require acidification of the phagosome
    • Clemens DL, Lee BY, Horwitz MA, (2009) Francisella tularensis phagosomal escape does not require acidification of the phagosome. Infect Immun 77: 1757-1773.
    • (2009) Infect Immun , vol.77 , pp. 1757-1773
    • Clemens, D.L.1    Lee, B.Y.2    Horwitz, M.A.3
  • 9
    • 57349126161 scopus 로고    scopus 로고
    • The early phagosomal stage of Francisella tularensis determines optimal phagosomal escape and Francisella pathogenicity island protein expression
    • Chong A, Wehrly TD, Nair V, Fischer ER, Barker JR, et al. (2008) The early phagosomal stage of Francisella tularensis determines optimal phagosomal escape and Francisella pathogenicity island protein expression. Infect Immun 76: 5488-5499.
    • (2008) Infect Immun , vol.76 , pp. 5488-5499
    • Chong, A.1    Wehrly, T.D.2    Nair, V.3    Fischer, E.R.4    Barker, J.R.5
  • 10
    • 33749264796 scopus 로고    scopus 로고
    • Autophagy-mediated reentry of Francisella tularensis into the endocytic compartment after cytoplasmic replication
    • Checroun C, Wehrly TD, Fischer ER, Hayes SF, Celli J, (2006) Autophagy-mediated reentry of Francisella tularensis into the endocytic compartment after cytoplasmic replication. Proc Natl Acad Sci U S A 103: 14578-14583.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 14578-14583
    • Checroun, C.1    Wehrly, T.D.2    Fischer, E.R.3    Hayes, S.F.4    Celli, J.5
  • 11
    • 34748882473 scopus 로고    scopus 로고
    • The Francisella pathogenicity island
    • Nano FE, Schmerk C, (2007) The Francisella pathogenicity island. Ann N Y Acad Sci 1105: 122-137.
    • (2007) Ann N Y Acad Sci , vol.1105 , pp. 122-137
    • Nano, F.E.1    Schmerk, C.2
  • 12
    • 34548411393 scopus 로고    scopus 로고
    • A Francisella tularensis pathogenicity island protein essential for bacterial proliferation within the host cell cytosol
    • Santic M, Molmeret M, Barker JR, Klose KE, Dekanic A, et al. (2007) A Francisella tularensis pathogenicity island protein essential for bacterial proliferation within the host cell cytosol. Cell Microbiol 9: 2391-2403.
    • (2007) Cell Microbiol , vol.9 , pp. 2391-2403
    • Santic, M.1    Molmeret, M.2    Barker, J.R.3    Klose, K.E.4    Dekanic, A.5
  • 13
    • 72049089849 scopus 로고    scopus 로고
    • The Francisella tularensis pathogenicity island encodes a secretion system that is required for phagosome escape and virulence
    • Barker JR, Chong A, Wehrly TD, Yu JJ, Rodriguez SA, et al. (2009) The Francisella tularensis pathogenicity island encodes a secretion system that is required for phagosome escape and virulence. Mol Microbiol 74: 1459-1470.
    • (2009) Mol Microbiol , vol.74 , pp. 1459-1470
    • Barker, J.R.1    Chong, A.2    Wehrly, T.D.3    Yu, J.J.4    Rodriguez, S.A.5
  • 14
    • 58449112802 scopus 로고    scopus 로고
    • Identification of an essential Francisella tularensis subsp. tularensis virulence factor
    • Qin A, Scott DW, Thompson JA, Mann BJ, (2009) Identification of an essential Francisella tularensis subsp. tularensis virulence factor. Infect Immun 77: 152-161.
    • (2009) Infect Immun , vol.77 , pp. 152-161
    • Qin, A.1    Scott, D.W.2    Thompson, J.A.3    Mann, B.J.4
  • 16
    • 0027511108 scopus 로고
    • Cloning and sequencing of Coxiella burnetii outer membrane protein gene com1
    • Hendrix LR, Mallavia LP, Samuel JE, (1993) Cloning and sequencing of Coxiella burnetii outer membrane protein gene com1. Infect Immun 61: 470-477.
    • (1993) Infect Immun , vol.61 , pp. 470-477
    • Hendrix, L.R.1    Mallavia, L.P.2    Samuel, J.E.3
  • 17
    • 0028846924 scopus 로고
    • Influence of site specifically altered Mip proteins on intracellular survival of Legionella pneumophila in eukaryotic cells
    • Wintermeyer E, Ludwig B, Steinert M, Schmidt B, Fischer G, et al. (1995) Influence of site specifically altered Mip proteins on intracellular survival of Legionella pneumophila in eukaryotic cells. Infect Immun 63: 4576-4583.
    • (1995) Infect Immun , vol.63 , pp. 4576-4583
    • Wintermeyer, E.1    Ludwig, B.2    Steinert, M.3    Schmidt, B.4    Fischer, G.5
  • 18
    • 27444447753 scopus 로고    scopus 로고
    • Ng-MIP, a surface-exposed lipoprotein of Neisseria gonorrhoeae, has a peptidyl-prolyl cis/trans isomerase (PPIase) activity and is involved in persistence in macrophages
    • Leuzzi R, Serino L, Scarselli M, Savino S, Fontana MR, et al. (2005) Ng-MIP, a surface-exposed lipoprotein of Neisseria gonorrhoeae, has a peptidyl-prolyl cis/trans isomerase (PPIase) activity and is involved in persistence in macrophages. Mol Microbiol 58: 669-681.
    • (2005) Mol Microbiol , vol.58 , pp. 669-681
    • Leuzzi, R.1    Serino, L.2    Scarselli, M.3    Savino, S.4    Fontana, M.R.5
  • 19
    • 34347375108 scopus 로고    scopus 로고
    • Molecular characterization and subcellular localization of macrophage infectivity potentiator, a Chlamydia trachomatis lipoprotein
    • Neff L, Daher S, Muzzin P, Spenato U, Gulacar F, et al. (2007) Molecular characterization and subcellular localization of macrophage infectivity potentiator, a Chlamydia trachomatis lipoprotein. J Bacteriol 189: 4739-4748.
    • (2007) J Bacteriol , vol.189 , pp. 4739-4748
    • Neff, L.1    Daher, S.2    Muzzin, P.3    Spenato, U.4    Gulacar, F.5
  • 20
    • 70449347075 scopus 로고    scopus 로고
    • Proteome analysis of an attenuated Francisella tularensis dsbA mutant: identification of potential DsbA substrate proteins
    • Straskova A, Pavkova I, Link M, Forslund AL, Kuoppa K, et al. (2009) Proteome analysis of an attenuated Francisella tularensis dsbA mutant: identification of potential DsbA substrate proteins. J Proteome Res 8: 5336-5346.
    • (2009) J Proteome Res , vol.8 , pp. 5336-5346
    • Straskova, A.1    Pavkova, I.2    Link, M.3    Forslund, A.L.4    Kuoppa, K.5
  • 21
    • 0028971218 scopus 로고
    • Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA
    • Guilhot C, Jander G, Martin NL, Beckwith J, (1995) Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA. Proc Natl Acad Sci U S A 92: 9895-9899.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 9895-9899
    • Guilhot, C.1    Jander, G.2    Martin, N.L.3    Beckwith, J.4
  • 22
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin JL, Bardwell JC, Kuriyan J, (1993) Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 365: 464-468.
    • (1993) Nature , vol.365 , pp. 464-468
    • Martin, J.L.1    Bardwell, J.C.2    Kuriyan, J.3
  • 23
    • 80052523346 scopus 로고    scopus 로고
    • Glycosylation of DsbA in Francisella tularensis subspecies tularensis
    • (epub ahead of print)
    • Thomas RM, Twine SM, Fulton KM, Tessier L, Kilmury SL, et al. (2011) Glycosylation of DsbA in Francisella tularensis subspecies tularensis. J Bacteriol (epub ahead of print).
    • (2011) J Bacteriol
    • Thomas, R.M.1    Twine, S.M.2    Fulton, K.M.3    Tessier, L.4    Kilmury, S.L.5
  • 24
    • 77950672706 scopus 로고    scopus 로고
    • A multimethodological approach to identification of glycoproteins from the proteome of Francisella tularensis, an intracellular microorganism
    • Balonova L, Hernychova L, Mann BF, Link M, Bilkova Z, et al. (2010) A multimethodological approach to identification of glycoproteins from the proteome of Francisella tularensis, an intracellular microorganism. J Proteome Res 9: 1935-2005.
    • (2010) J Proteome Res , vol.9 , pp. 1935-2005
    • Balonova, L.1    Hernychova, L.2    Mann, B.F.3    Link, M.4    Bilkova, Z.5
  • 25
    • 10444282165 scopus 로고    scopus 로고
    • Construction and characterization of a highly efficient Francisella shuttle plasmid
    • Maier TM, Havig A, Casey M, Nano FE, Frank DW, et al. (2004) Construction and characterization of a highly efficient Francisella shuttle plasmid. Appl Environ Microbiol 70: 7511-7519.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 7511-7519
    • Maier, T.M.1    Havig, A.2    Casey, M.3    Nano, F.E.4    Frank, D.W.5
  • 28
    • 77956318615 scopus 로고    scopus 로고
    • Mechanisms of oxidative protein folding in the bacterial cell envelope
    • Kadokura H, Beckwith J, (2010) Mechanisms of oxidative protein folding in the bacterial cell envelope. Antioxid Redox Signal 13: 1231-1246.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1231-1246
    • Kadokura, H.1    Beckwith, J.2
  • 29
    • 4844227315 scopus 로고    scopus 로고
    • Functional diversity of three different DsbA proteins from Neisseria meningitidis
    • Sinha S, Langford PR, Kroll JS, (2004) Functional diversity of three different DsbA proteins from Neisseria meningitidis. Microbiology 150: 2993-3000.
    • (2004) Microbiology , vol.150 , pp. 2993-3000
    • Sinha, S.1    Langford, P.R.2    Kroll, J.S.3
  • 30
    • 77952691205 scopus 로고    scopus 로고
    • Francisella tularensis DeltapyrF mutants show that replication in nonmacrophages is sufficient for pathogenesis in vivo
    • Horzempa J, O'Dee DM, Shanks RM, Nau GJ, (2010) Francisella tularensis DeltapyrF mutants show that replication in nonmacrophages is sufficient for pathogenesis in vivo. Infect Immun 78: 2607-2619.
    • (2010) Infect Immun , vol.78 , pp. 2607-2619
    • Horzempa, J.1    O'Dee, D.M.2    Shanks, R.M.3    Nau, G.J.4
  • 31
    • 0028074989 scopus 로고
    • A homodimer represents an active species of the peptidyl-prolyl cis/trans isomerase FKBP25mem from Legionella pneumophila
    • Schmidt B, Rahfeld J, Schierhorn A, Ludwig B, Hacker J, et al. (1994) A homodimer represents an active species of the peptidyl-prolyl cis/trans isomerase FKBP25mem from Legionella pneumophila. FEBS Lett 352: 185-190.
    • (1994) FEBS Lett , vol.352 , pp. 185-190
    • Schmidt, B.1    Rahfeld, J.2    Schierhorn, A.3    Ludwig, B.4    Hacker, J.5
  • 32
    • 33846230030 scopus 로고    scopus 로고
    • Collagen binding protein Mip enables Legionella pneumophila to transmigrate through a barrier of NCI-H292 lung epithelial cells and extracellular matrix
    • Wagner C, Khan AS, Kamphausen T, Schmausser B, Unal C, et al. (2007) Collagen binding protein Mip enables Legionella pneumophila to transmigrate through a barrier of NCI-H292 lung epithelial cells and extracellular matrix. Cell Microbiol 9: 450-462.
    • (2007) Cell Microbiol , vol.9 , pp. 450-462
    • Wagner, C.1    Khan, A.S.2    Kamphausen, T.3    Schmausser, B.4    Unal, C.5
  • 33
    • 33748041655 scopus 로고    scopus 로고
    • Legionella pneumophila Mip, a surface-exposed peptidylproline cis-trans-isomerase, promotes the presence of phospholipase C-like activity in culture supernatants
    • Debroy S, Aragon V, Kurtz S, Cianciotto NP, (2006) Legionella pneumophila Mip, a surface-exposed peptidylproline cis-trans-isomerase, promotes the presence of phospholipase C-like activity in culture supernatants. Infect Immun 74: 5152-5160.
    • (2006) Infect Immun , vol.74 , pp. 5152-5160
    • Debroy, S.1    Aragon, V.2    Kurtz, S.3    Cianciotto, N.P.4
  • 34
    • 0042265192 scopus 로고    scopus 로고
    • Biochemical and functional analyses of the Mip protein: influence of the N-terminal half and of peptidylprolyl isomerase activity on the virulence of Legionella pneumophila
    • Kohler R, Fanghanel J, Konig B, Luneberg E, Frosch M, et al. (2003) Biochemical and functional analyses of the Mip protein: influence of the N-terminal half and of peptidylprolyl isomerase activity on the virulence of Legionella pneumophila. Infect Immun 71: 4389-4397.
    • (2003) Infect Immun , vol.71 , pp. 4389-4397
    • Kohler, R.1    Fanghanel, J.2    Konig, B.3    Luneberg, E.4    Frosch, M.5
  • 35
    • 0029161150 scopus 로고
    • DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA
    • Kishigami S, Kanaya E, Kikuchi M, Ito K, (1995) DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA. J Biol Chem 270: 17072-17074.
    • (1995) J Biol Chem , vol.270 , pp. 17072-17074
    • Kishigami, S.1    Kanaya, E.2    Kikuchi, M.3    Ito, K.4
  • 36
    • 0037372822 scopus 로고    scopus 로고
    • DsbA of Pseudomonas aeruginosa is essential for multiple virulence factors
    • Ha UH, Wang Y, Jin S, (2003) DsbA of Pseudomonas aeruginosa is essential for multiple virulence factors. Infect Immun 71: 1590-1595.
    • (2003) Infect Immun , vol.71 , pp. 1590-1595
    • Ha, U.H.1    Wang, Y.2    Jin, S.3
  • 37
    • 0031871879 scopus 로고    scopus 로고
    • Inactivation of DsbA, but not DsbC and DsbD, affects the intracellular survival and virulence of Shigella flexneri
    • Yu J, (1998) Inactivation of DsbA, but not DsbC and DsbD, affects the intracellular survival and virulence of Shigella flexneri. Infect Immun 66: 3909-3917.
    • (1998) Infect Immun , vol.66 , pp. 3909-3917
    • Yu, J.1
  • 38
    • 4544229875 scopus 로고    scopus 로고
    • Two periplasmic disulfide oxidoreductases, DsbA and SrgA, target outer membrane protein SpiA, a component of the Salmonella pathogenicity island 2 type III secretion system
    • Miki T, Okada N, Danbara H, (2004) Two periplasmic disulfide oxidoreductases, DsbA and SrgA, target outer membrane protein SpiA, a component of the Salmonella pathogenicity island 2 type III secretion system. J Biol Chem 279: 34631-34642.
    • (2004) J Biol Chem , vol.279 , pp. 34631-34642
    • Miki, T.1    Okada, N.2    Danbara, H.3
  • 39
    • 0347622755 scopus 로고    scopus 로고
    • RtsA coordinately regulates DsbA and the Salmonella pathogenicity island 1 type III secretion system
    • Ellermeier CD, Slauch JM, (2004) RtsA coordinately regulates DsbA and the Salmonella pathogenicity island 1 type III secretion system. J Bacteriol 186: 68-79.
    • (2004) J Bacteriol , vol.186 , pp. 68-79
    • Ellermeier, C.D.1    Slauch, J.M.2
  • 40
    • 0032786363 scopus 로고    scopus 로고
    • DsbA: a protein-folding catalyst contributing to bacterial virulence
    • Yu J, Kroll JS, (1999) DsbA: a protein-folding catalyst contributing to bacterial virulence. Microbes Infect 1: 1221-1228.
    • (1999) Microbes Infect , vol.1 , pp. 1221-1228
    • Yu, J.1    Kroll, J.S.2
  • 41
    • 79955000469 scopus 로고    scopus 로고
    • DsbA2 (27 kDa Com1-like protein) of Legionella pneumophila catalyses extracytoplasmic disulphide-bond formation in proteins including the Dot/Icm type IV secretion system
    • Jameson-Lee M, Garduno RA, Hoffman PS, (2011) DsbA2 (27 kDa Com1-like protein) of Legionella pneumophila catalyses extracytoplasmic disulphide-bond formation in proteins including the Dot/Icm type IV secretion system. Mol Microbiol 80: 835-852.
    • (2011) Mol Microbiol , vol.80 , pp. 835-852
    • Jameson-Lee, M.1    Garduno, R.A.2    Hoffman, P.S.3
  • 43
    • 0037309117 scopus 로고    scopus 로고
    • Characterization of SrgA, a Salmonella enterica serovar typhimurium virulence plasmid-encoded paralogue of the disulfide oxidoreductase DsbA, essential for biogenesis of plasmid-encoded fimbriae
    • Bouwman CW, Kohli M, Killoran A, Touchie GA, Kadner RJ, et al. (2003) Characterization of SrgA, a Salmonella enterica serovar typhimurium virulence plasmid-encoded paralogue of the disulfide oxidoreductase DsbA, essential for biogenesis of plasmid-encoded fimbriae. J Bacteriol 185: 991-1000.
    • (2003) J Bacteriol , vol.185 , pp. 991-1000
    • Bouwman, C.W.1    Kohli, M.2    Killoran, A.3    Touchie, G.A.4    Kadner, R.J.5
  • 44
    • 33748148231 scopus 로고    scopus 로고
    • Identification of transposon insertion mutants of Francisella tularensis tularensis strain Schu S4 deficient in intracellular replication in the hepatic cell line HepG2
    • Qin A, Mann BJ, (2006) Identification of transposon insertion mutants of Francisella tularensis tularensis strain Schu S4 deficient in intracellular replication in the hepatic cell line HepG2. BMC Microbiol 6: 69.
    • (2006) BMC Microbiol , vol.6 , pp. 69
    • Qin, A.1    Mann, B.J.2
  • 45
    • 33744734682 scopus 로고    scopus 로고
    • Characterization of the siderophore of Francisella tularensis and role of fslA in siderophore production
    • Sullivan JT, Jeffery EF, Shannon JD, Ramakrishnan G, (2006) Characterization of the siderophore of Francisella tularensis and role of fslA in siderophore production. J Bacteriol 188: 3785-3795.
    • (2006) J Bacteriol , vol.188 , pp. 3785-3795
    • Sullivan, J.T.1    Jeffery, E.F.2    Shannon, J.D.3    Ramakrishnan, G.4
  • 46
    • 0033082686 scopus 로고    scopus 로고
    • Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors
    • Sheffield P, Garrard S, Derewenda Z, (1999) Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors. Protein Expr Purif 15: 34-39.
    • (1999) Protein Expr Purif , vol.15 , pp. 34-39
    • Sheffield, P.1    Garrard, S.2    Derewenda, Z.3


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