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Volumn 100, Issue 5, 2011, Pages 1335-1343

Induced conformational changes in the activation of the pseudomonas aeruginosa type III toxin, ExoU

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA; MAMMALIA; PHOS; PSEUDOMONAS AERUGINOSA;

EID: 79953903080     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.01.056     Document Type: Article
Times cited : (16)

References (47)
  • 2
    • 3943093972 scopus 로고    scopus 로고
    • Nosocomial bloodstream infections in US hospitals: Analysis of 24,179 cases from a prospective nationwide surveillance study
    • DOI 10.1086/421946
    • Wisplinghoff, H., T. Bischoff, M. B. Edmond. 2004. Nosocomial bloodstream infections in US hospitals: analysis of 24,179 cases from a prospective nationwide surveillance study. Clin. Infect. Dis. 39:309-317. (Pubitemid 39050477)
    • (2004) Clinical Infectious Diseases , vol.39 , Issue.3 , pp. 309-317
    • Wisplinghoff, H.1    Bischoff, T.2    Tallent, S.M.3    Seifert, H.4    Wenzel, R.P.5    Edmond, M.B.6
  • 3
    • 0036191393 scopus 로고    scopus 로고
    • Type III protein secretion is associated with poor clinical outcomes in patients with ventilator-associated pneumonia caused by Pseudomonas aeruginosa
    • Hauser, A. R., E. Cobb, J. Rello. 2002. Type III protein secretion is associated with poor clinical outcomes in patients with ventilator-associated pneumonia caused by Pseudomonas aeruginosa. Crit. Care Med. 30:521-528. (Pubitemid 34214611)
    • (2002) Critical Care Medicine , vol.30 , Issue.3 , pp. 521-528
    • Hauser, A.R.1    Cobb, E.2    Bodi, M.3    Mariscal, D.4    Valles, J.5    Engel, J.N.6    Rello, J.7
  • 4
    • 0036225688 scopus 로고    scopus 로고
    • Lung infections associated with cystic fibrosis
    • DOI 10.1128/CMR.15.2.194-222.2002
    • Lyczak, J. B., C. L. Cannon, and G. B. Pier. 2002. Lung infections associated with cystic fibrosis. Clin. Microbiol. Rev. 15:194-222. (Pubitemid 34303763)
    • (2002) Clinical Microbiology Reviews , vol.15 , Issue.2 , pp. 194-222
    • Lyczak, J.B.1    Cannon, C.L.2    Pier, G.B.3
  • 5
    • 0036160582 scopus 로고    scopus 로고
    • CFTR mutations and host susceptibility to Pseudomonas aeruginosa lung infection
    • DOI 10.1016/S1369-5274(02)00290-4
    • Pier, G. B. 2002. CFTR mutations and host susceptibility to Pseudomonas aeruginosa lung infection. Curr. Opin. Microbiol. 5:81-86. (Pubitemid 34118162)
    • (2002) Current Opinion in Microbiology , vol.5 , Issue.1 , pp. 81-86
    • Pier, G.B.1
  • 6
    • 0033591446 scopus 로고    scopus 로고
    • Type III secretion machines: Bacterial devices for protein delivery into host cells
    • DOI 10.1126/science.284.5418.1322
    • Galan, J. E., and A. Collmer. 1999. Type III secretion machines: bacterial devices for protein delivery into host cells. Science. 284:1322-1328. (Pubitemid 29289652)
    • (1999) Science , vol.284 , Issue.5418 , pp. 1322-1328
    • Galan, J.E.1    Collmer, A.2
  • 7
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • DOI 10.1038/nature05272, PII NATURE05272
    • Galan, J. E., and H. Wolf-Watz. 2006. Protein delivery into eukaryotic cells by type III secretion machines. Nature. 444:567-573. (Pubitemid 44864429)
    • (2006) Nature , vol.444 , Issue.7119 , pp. 567-573
    • Galan, J.E.1    Wolf-Watz, H.2
  • 10
    • 0035137564 scopus 로고    scopus 로고
    • Type III secretion/intoxication system important in virulence of Pseudomonas aeruginosa infections in burns
    • DOI 10.1016/S0305-4179(00)00142-X, PII S030541790000142X
    • Holder, I. A., A. N. Neely, and D. W. Frank. 2001. Type III secretion/intoxication system important in virulence of Pseudomonas aeruginosa infections in burns. Burns. 27:129-130. (Pubitemid 32156984)
    • (2001) Burns , vol.27 , Issue.2 , pp. 129-130
    • Holder, I.A.1    Neely, A.N.2    Frank, D.W.3
  • 11
    • 0034877753 scopus 로고    scopus 로고
    • PcrV immunization enhances survival of burned Pseudomonas aeruginosa-infected mice
    • DOI 10.1128/IAI.69.9.5908-5910.2001
    • Holder, I. A., A. N. Neely, and D. W. Frank. 2001. PcrV immunization enhances survival of burned Pseudomonas aeruginosa-infected mice. Infect. Immun. 69:5908-5910. (Pubitemid 32786533)
    • (2001) Infection and Immunity , vol.69 , Issue.9 , pp. 5908-5910
    • Holder, I.A.1    Neely, A.N.2    Frank, D.W.3
  • 12
    • 67349265146 scopus 로고    scopus 로고
    • Morbidity associated with Pseudomonas aeruginosa bloodstream infections
    • Scheetz, M. H., M. Hoffman, A. R. Hauser. 2009. Morbidity associated with Pseudomonas aeruginosa bloodstream infections. Diagn. Microbiol. Infect. Dis. 64:311-319.
    • (2009) Diagn. Microbiol. Infect. Dis. , vol.64 , pp. 311-319
    • Scheetz, M.H.1    Hoffman, M.2    Hauser, A.R.3
  • 14
    • 0142135037 scopus 로고    scopus 로고
    • 2 Inhibitors
    • DOI 10.1074/jbc.M302472200
    • Phillips, R. M., D. A. Six, P. Ghosh. 2003. In vivo phospholipase activity of the Pseudomonas aeruginosa cytotoxin ExoU and protection of mammalian cells with phospholipase A2 inhibitors. J. Biol. Chem. 278:41326-41332. (Pubitemid 37280961)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.42 , pp. 41326-41332
    • Phillips, R.M.1    Six, D.A.2    Dennis, E.A.3    Ghosh, P.4
  • 15
    • 13244295376 scopus 로고    scopus 로고
    • Characterization of phospholipase activity of the Pseudomonas aeruginosa type III cytotoxin, ExoU
    • DOI 10.1128/JB.187.3.1192-1195.2005
    • Sato, H., J. B. Feix, D. W. Frank. 2005. Characterization of phospholipase activity of the Pseudomonas aeruginosa type III cytotoxin, ExoU. J. Bacteriol. 187:1192-1195. (Pubitemid 40189790)
    • (2005) Journal of Bacteriology , vol.187 , Issue.3 , pp. 1192-1195
    • Sato, H.1    Feix, J.B.2    Hillard, C.J.3    Frank, D.W.4
  • 16
    • 69249157248 scopus 로고    scopus 로고
    • The type III secretion system of Pseudomonas aeruginosa: Infection by injection
    • Hauser, A. R. 2009. The type III secretion system of Pseudomonas aeruginosa: infection by injection. Nat. Rev. Microbiol. 7:654-665.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 654-665
    • Hauser, A.R.1
  • 17
    • 33748672064 scopus 로고    scopus 로고
    • Identification of superoxide dismutase as a cofactor for the Pseudomonas type III toxin, ExoU
    • DOI 10.1021/bi060788j
    • Sato, H., J. B. Feix, and D. W. Frank. 2006. Identification of superoxide dismutase as a cofactor for the Pseudomonas type III toxin, ExoU. Biochemistry. 45:10368-10375. (Pubitemid 44384812)
    • (2006) Biochemistry , vol.45 , Issue.34 , pp. 10368-10375
    • Sato, H.1    Feix, J.B.2    Frank, D.W.3
  • 18
    • 0034977803 scopus 로고    scopus 로고
    • Multiple domains are required for the toxic activity of Pseudomonas aeruginosa ExoU
    • DOI 10.1128/JB.183.14.4330-4344.2001
    • Finck-Barbancon, V., and D. W. Frank. 2001. Multiple domains are required for the toxic activity of Pseudomonas aeruginosa ExoU. J. Bacteriol. 183:4330-4344. (Pubitemid 32568086)
    • (2001) Journal of Bacteriology , vol.183 , Issue.14 , pp. 4330-4344
    • Finck-Barbancon, V.1    Frank, D.W.2
  • 19
    • 33745621121 scopus 로고    scopus 로고
    • Eukaryotic localization, activation and ubiquitinylation of a bacterial type III secreted toxin
    • Stirling, F. R., A. Cuzick, T. J. Evans. 2006. Eukaryotic localization, activation and ubiquitinylation of a bacterial type III secreted toxin. Cell Microbiol. 8:1294-1309.
    • (2006) Cell Microbiol. , vol.8 , pp. 1294-1309
    • Stirling, F.R.1    Cuzick, A.2    Evans, T.J.3
  • 20
    • 11144265658 scopus 로고    scopus 로고
    • Functional regions of the Pseudomonas aeruginosa cytotoxin ExoU
    • DOI 10.1128/IAI.73.1.573-582.2005
    • Rabin, S. D., and A. R. Hauser. 2005. Functional regions of the Pseudomonas aeruginosa cytotoxin ExoU. Infect. Immun. 73: 573-582. (Pubitemid 40041152)
    • (2005) Infection and Immunity , vol.73 , Issue.1 , pp. 573-582
    • Rabin, S.D.P.1    Hauser, A.R.2
  • 21
    • 33646374906 scopus 로고    scopus 로고
    • A C-terminal domain targets the Pseudomonas aeruginosa cytotoxin ExoU to the plasma membrane of host cells
    • DOI 10.1128/IAI.74.5.2552-2561.2006
    • Rabin, S. D., J. L. Veesenmeyer, A. R. Hauser. 2006. A C-terminal domain targets the Pseudomonas aeruginosa cytotoxin ExoU to the plasma membrane of host cells. Infect. Immun. 74:2552-2561. (Pubitemid 43672962)
    • (2006) Infection and Immunity , vol.74 , Issue.5 , pp. 2552-2561
    • Rabin, S.D.P.1    Veesenmeyer, J.L.2    Bieging, K.T.3    Hauser, A.R.4
  • 22
    • 77955302592 scopus 로고    scopus 로고
    • Role of the membrane localization domain of the Pseudomonas aeruginosa effector protein ExoU in cytotoxicity
    • Veesenmeyer, J. L., H. Howel, A. R. Hauser. 2010. Role of the membrane localization domain of the Pseudomonas aeruginosa effector protein ExoU in cytotoxicity. Infect. Immun. 78:3346-3357.
    • (2010) Infect. Immun. , vol.78 , pp. 3346-3357
    • Veesenmeyer, J.L.1    Howel, H.2    Hauser, A.R.3
  • 23
    • 77949694407 scopus 로고    scopus 로고
    • Activation of ExoU phospholipase activity requires specific C-terminal regions
    • Schmalzer, K. M., M. A. Benson, and D. W. Frank. 2010. Activation of ExoU phospholipase activity requires specific C-terminal regions. J. Bacteriol. 192:1801-1812.
    • (2010) J. Bacteriol. , vol.192 , pp. 1801-1812
    • Schmalzer, K.M.1    Benson, M.A.2    Frank, W.D.3
  • 24
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell, W. L., D. S. Cafiso, and C. Altenbach. 2000. Identifying conformational changes with site-directed spin labeling. Nat. Struct. Biol. 7:735-739.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 25
    • 0036606899 scopus 로고    scopus 로고
    • A new spin on protein dynamics
    • DOI 10.1016/S0968-0004(02)02095-9, PII S0968000402020959
    • Columbus, L., and W. L. Hubbell. 2002. A new spin on protein dynamics. Trends Biochem. Sci. 27:288-295. (Pubitemid 34628668)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.6 , pp. 288-295
    • Columbus, L.1    Hubbell, W.L.2
  • 26
    • 33749041288 scopus 로고    scopus 로고
    • Recent advances and applications of site-directed spin labeling
    • DOI 10.1016/j.sbi.2006.08.008, PII S0959440X06001436, Carbohydrates and Glycoconjugates / Biophysical Methods
    • Fanucci, G. E., and D. S. Cafiso. 2006. Recent advances and applications of site-directed spin labeling. Curr. Opin. Struct. Biol. 16: 644-653. (Pubitemid 44466409)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.5 , pp. 644-653
    • Fanucci, G.E.1    Cafiso, D.S.2
  • 27
    • 35448961949 scopus 로고    scopus 로고
    • Methods and applications of sitedirected spin labeling EPR spectroscopy
    • Klug, C. S., and J. B. Feix. 2008. Methods and applications of sitedirected spin labeling EPR spectroscopy. Methods Cell Biol. 84: 617-658.
    • (2008) Methods Cell Biol. , vol.84 , pp. 617-658
    • Klug, C.S.1    Feix, J.B.2
  • 28
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • Pannier, M., S. Veit, H. W. Spiess. 2000. Dead-time free measurement of dipole-dipole interactions between electron spins. J. Magn. Reson. 142:331-340.
    • (2000) J. Magn. Reson. , vol.142 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Spiess, H.W.3
  • 29
    • 34250841296 scopus 로고    scopus 로고
    • Measuring Distances by Pulsed Dipolar ESR Spectroscopy: Spin-Labeled Histidine Kinases
    • DOI 10.1016/S0076-6879(07)23003-4, PII S0076687907230034, Two Component Signaling Systems, Part B
    • Borbat, P. P., and J. H. Freed. 2007. Measuring distances by pulsed dipolar ESR spectroscopy: spin-labeled histidine kinases. Methods Enzymol. 423:52-116. (Pubitemid 46991091)
    • (2007) Methods in Enzymology , vol.423 , pp. 52-116
    • Borbat, P.P.1    Freed, J.H.2
  • 30
    • 33748509727 scopus 로고    scopus 로고
    • Substrate-dependent unfolding of the energy coupling motif of a membrane transport protein determined by double electron-electron resonance
    • DOI 10.1021/bi061051x
    • Xu, Q., J. F. Ellena, D. S. Cafiso. 2006. Substrate-dependent unfolding of the energy coupling motif of a membrane transport protein determined by double electron-electron resonance. Biochemistry. 45:10847-10854. (Pubitemid 44360154)
    • (2006) Biochemistry , vol.45 , Issue.36 , pp. 10847-10854
    • Xu, Q.1    Ellena, J.F.2    Kim, M.3    Cafiso, D.S.4
  • 31
    • 35148883146 scopus 로고    scopus 로고
    • Structure of the cytoplasmic domain of erythrocyte band 3 hereditary spherocytosis variant P327R: Band 3 Tuscaloosa
    • DOI 10.1021/bi700948p
    • Zhou, Z., S. C. DeSensi, A. H. Beth. 2007. Structure of the cytoplasmic domain of erythrocyte band 3 hereditary spherocytosis variant P327R: band 3 Tuscaloosa. Biochemistry. 46:10248-10257. (Pubitemid 350067618)
    • (2007) Biochemistry , vol.46 , Issue.36 , pp. 10248-10257
    • Zhou, Z.1    DeSensi, S.C.2    Stein, R.A.3    Brandon, S.4    Song, L.5    Cobb, C.E.6    Hustedt, E.J.7    Beth, A.H.8
  • 33
    • 70349785109 scopus 로고    scopus 로고
    • Conformational cycle of the ABC transporter MsbA in liposomes: Detailed analysis using double electron-electron resonance spectroscopy
    • Zou, P., M. Bortolus, and H. S. Mchaourab. 2009. Conformational cycle of the ABC transporter MsbA in liposomes: detailed analysis using double electron-electron resonance spectroscopy. J. Mol. Biol. 393:586-597.
    • (2009) J. Mol. Biol. , vol.393 , pp. 586-597
    • Zou, P.1    Bortolus, M.2    McHaourab, H.S.3
  • 34
    • 70349153078 scopus 로고    scopus 로고
    • Monitoring inhibitor-induced conformational population shifts in HIV-1 protease by pulsed EPR spectroscopy
    • Blackburn, M. E., A. M. Veloro, and G. E. Fanucci. 2009. Monitoring inhibitor-induced conformational population shifts in HIV-1 protease by pulsed EPR spectroscopy. Biochemistry. 48:8765-8767.
    • (2009) Biochemistry , vol.48 , pp. 8765-8767
    • Blackburn, M.E.1    Veloro, A.M.2    Fanucci, G.E.3
  • 36
    • 0000326938 scopus 로고    scopus 로고
    • Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified levenberg-marquardt algorithm
    • Budil, D. E., S. Lee, J. H. Freed. 1996. Nonlinear-least-squares analysis of slow motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt algorithm. J. Magn. Res. A. 120: 155-189. (Pubitemid 126751752)
    • (1996) Journal of Magnetic Resonance - Series A , vol.120 , Issue.2 , pp. 155-189
    • Budil, D.E.1    Sanghyuk, L.2    Saxena, S.3    Freed, J.H.4
  • 37
    • 0035799354 scopus 로고    scopus 로고
    • Molecular motion of spin labeled side chains in α-helices: Analysis by variation of side chain structure
    • DOI 10.1021/bi002645h
    • Columbus, L., T. Kálai, W. L. Hubbell. 2001. Molecular motion of spin labeled side chains in α-helices: analysis by variation of side chain structure. Biochemistry. 40:3828-3846. (Pubitemid 32280420)
    • (2001) Biochemistry , vol.40 , Issue.13 , pp. 3828-3846
    • Columbus, L.1    Kalai, T.2    Jeko, J.3    Hideg, K.4    Hubbell, W.L.5
  • 38
    • 33646382407 scopus 로고    scopus 로고
    • Conformational states and dynamics of rhodopsin in micelles and bilayers
    • DOI 10.1021/bi060101v
    • Kusnetzow, A. K., C. Altenbach, and W. L. Hubbell. 2006. Conformational states and dynamics of rhodopsin in micelles and bilayers. Biochemistry. 45:5538-5550. (Pubitemid 43673184)
    • (2006) Biochemistry , vol.45 , Issue.17 , pp. 5538-5550
    • Kusnetzow, A.K.1    Altenbach, C.2    Hubbell, W.L.3
  • 39
    • 33846344623 scopus 로고    scopus 로고
    • DEER Analysis 2006 - A comprehensive software package for analyzing pulsed ELDOR data
    • Jeschke, G., V. Chechik, H. Jung. 2006. DEER Analysis 2006 - a comprehensive software package for analyzing pulsed ELDOR data. Appl. Magn. Res. 30:473-498.
    • (2006) Appl. Magn. Res. , vol.30 , pp. 473-498
    • Jeschke, G.1    Chechik, V.2    Jung, H.3
  • 40
    • 0024974071 scopus 로고
    • Structural studies on transmembrane proteins. 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines
    • Altenbach, C., S. L. Flitsch, W. L. Hubbell. 1989. Structural studies on transmembrane proteins. 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines. Biochemistry. 28:7806-7812.
    • (1989) Biochemistry , vol.28 , pp. 7806-7812
    • Altenbach, C.1    Flitsch, S.L.2    Hubbell, W.L.3
  • 41
    • 0037022173 scopus 로고    scopus 로고
    • Structure and dynamics of a helical hairpin and loop region in annexin 12: A site-directed spin labeling study
    • DOI 10.1021/bi011856z
    • Isas, J. M., R. Langen, W. L. Hubbell. 2002. Structure and dynamics of a helical hairpin and loop region in annexin 12: a site-directed spin labeling study. Biochemistry. 41:1464-1473. (Pubitemid 34112735)
    • (2002) Biochemistry , vol.41 , Issue.5 , pp. 1464-1473
    • Isas, J.M.1    Langen, R.2    Haigler, H.T.3    Hubbell, W.L.4
  • 42
    • 5644258235 scopus 로고    scopus 로고
    • + channel in a lipid bilayer
    • DOI 10.1126/science.1101373
    • + channel in a lipid bilayer. Science. 306:491-495. (Pubitemid 39372450)
    • (2004) Science , vol.306 , Issue.5695 , pp. 491-495
    • Cuello, L.G.1    Cortes, D.M.2    Perozo, E.3
  • 43
    • 58149380718 scopus 로고    scopus 로고
    • Structure of membrane-bound α-synuclein from site-directed spin labeling and computational refinement
    • Jao, C. C., B. G. Hegde, R. Langen. 2008. Structure of membrane-bound α-synuclein from site-directed spin labeling and computational refinement. Proc. Natl. Acad. Sci. USA. 105:19666-19671.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19666-19671
    • Jao, C.C.1    Hegde, B.G.2    Langen, R.3
  • 44
    • 58849132410 scopus 로고    scopus 로고
    • Functionally important ATP binding and hydrolysis sites in Escherichia coli MsbA
    • Westfahl, K. M., J. A. Merten, C. S. Klug. 2008. Functionally important ATP binding and hydrolysis sites in Escherichia coli MsbA. Biochemistry. 47:13878-13886.
    • (2008) Biochemistry , vol.47 , pp. 13878-13886
    • Westfahl, K.M.1    Merten, J.A.2    Klug, C.S.3
  • 45
    • 0242569215 scopus 로고    scopus 로고
    • Spectroscopic Evidence that Osmolytes Used in Crystallization Buffers Inhibit a Conformation Change in a Membrane Protein
    • DOI 10.1021/bi035439t
    • Fanucci, G. E., J. Y. Lee, and D. S. Cafiso. 2003. Spectroscopic evidence that osmolytes used in crystallization buffers inhibit a conformation change in a membrane protein. Biochemistry. 42:13106-13112. (Pubitemid 37420662)
    • (2003) Biochemistry , vol.42 , Issue.45 , pp. 13106-13112
    • Fanucci, G.E.1    Lee, J.Y.2    Cafiso, D.S.3
  • 46
    • 33646202285 scopus 로고    scopus 로고
    • Solutes modify a conformational transition in a membrane transport protein
    • Kim, M., Q. Xu, D. S. Cafiso. 2006. Solutes modify a conformational transition in a membrane transport protein. Biophys. J. 90:2922-2929.
    • (2006) Biophys. J. , vol.90 , pp. 2922-2929
    • Kim, M.1    Xu, Q.2    Cafiso, D.S.3
  • 47
    • 67749124074 scopus 로고    scopus 로고
    • Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins
    • Lopez, C. J., M. R. Fleissner, W. L. Hubbell. 2009. Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins. Protein Sci. 18:1637-1652.
    • (2009) Protein Sci. , vol.18 , pp. 1637-1652
    • Lopez, C.J.1    Fleissner, M.R.2    Hubbell, W.L.3


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