메뉴 건너뛰기




Volumn 7, Issue 5, 2009, Pages 333-340

Life on the inside: The intracellular lifestyle of cytosolic bacteria

Author keywords

[No Author keywords available]

Indexed keywords

AUTOPHAGY; BACTERIAL GENETICS; BACTERIAL GROWTH; BACTERIAL SURVIVAL; BACTERIAL VIRULENCE; BACTERIOLYSIS; BURKHOLDERIA PSEUDOMALLEI; CELL DIVISION; CELL MIGRATION; CELL PROLIFERATION; CELL VACUOLE; CYTOSOL; CYTOSOLIC BACTERIA; FRANCISELLA TULARENSIS; GRAM NEGATIVE AEROBIC RODS AND COCCI; IMMUNE RESPONSE; NONHUMAN; ORGANISMS BY LIFE CYCLE STAGE; PRIORITY JOURNAL; REVIEW; RICKETTSIA; SHIGELLA FLEXNERI; ANIMAL; BACTERIAL PHENOMENA AND FUNCTIONS; BACTERIUM; HUMAN; IMMUNOLOGY; MICROBIOLOGY;

EID: 64749104915     PISSN: 17401526     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrmicro2112     Document Type: Review
Times cited : (337)

References (121)
  • 1
    • 1842430006 scopus 로고    scopus 로고
    • Cossart, P. & Sansonetti, P. J. Bacterial invasion: The paradigms of enteroinvasive pathogens. Science 304, 242-248 (2004).
    • Cossart, P. & Sansonetti, P. J. Bacterial invasion: The paradigms of enteroinvasive pathogens. Science 304, 242-248 (2004).
  • 2
    • 33947194392 scopus 로고    scopus 로고
    • The phagosome: Compartment with a license to kill
    • Haas, A. The phagosome: Compartment with a license to kill. Traffic 8, 311-330 (2007).
    • (2007) Traffic , vol.8 , pp. 311-330
    • Haas, A.1
  • 3
    • 0035172569 scopus 로고    scopus 로고
    • Rupture, invasion and inflammatory destruction of the intestinal barrier by Shigella, making sense of prokaryote-eukaryote cross-talks
    • Sansonetti, P. J. Rupture, invasion and inflammatory destruction of the intestinal barrier by Shigella, making sense of prokaryote-eukaryote cross-talks. FEMS Microbiol. Rev. 25, 3-14 (2001).
    • (2001) FEMS Microbiol. Rev , vol.25 , pp. 3-14
    • Sansonetti, P.J.1
  • 4
    • 38549126641 scopus 로고    scopus 로고
    • Molecular pathogenesis of Shigella spp.: Controlling host cell signaling, invasion, and death by type III secretion
    • Schroeder, G. N. & Hilbi, H. Molecular pathogenesis of Shigella spp.: Controlling host cell signaling, invasion, and death by type III secretion. Clin. Microbiol. Rev. 21, 134-156 (2008).
    • (2008) Clin. Microbiol. Rev , vol.21 , pp. 134-156
    • Schroeder, G.N.1    Hilbi, H.2
  • 5
    • 84920348196 scopus 로고    scopus 로고
    • pH-dependent perforation of macrophage phagosomes by listeriolysin O from Listeria monocytogenes
    • Beauregard, K. E., Lee, K. D., Collier, R. J. & Swanson, J. A. pH-dependent perforation of macrophage phagosomes by listeriolysin O from Listeria monocytogenes. Mol. Biol. Cell 8, 680 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , pp. 680
    • Beauregard, K.E.1    Lee, K.D.2    Collier, R.J.3    Swanson, J.A.4
  • 6
    • 0141446069 scopus 로고    scopus 로고
    • An attenuated strain of the facultative intracellular bacterium Francisella tularensis can escape the phagosome of monocytic cells
    • Golovliov, I., Baranov, V., Krocova, Z., Kovarova, H. & Sjostedt, A. An attenuated strain of the facultative intracellular bacterium Francisella tularensis can escape the phagosome of monocytic cells. Infect. Immun. 71, 5940-5950 (2003).
    • (2003) Infect. Immun , vol.71 , pp. 5940-5950
    • Golovliov, I.1    Baranov, V.2    Krocova, Z.3    Kovarova, H.4    Sjostedt, A.5
  • 7
    • 33644824480 scopus 로고    scopus 로고
    • Cytolysin-dependent delay of vacuole maturation in macrophages infected with Listeria monocytogenes
    • Henry, R. et al. Cytolysin-dependent delay of vacuole maturation in macrophages infected with Listeria monocytogenes. Cell. Microbiol. 8, 107-119 (2006).
    • (2006) Cell. Microbiol , vol.8 , pp. 107-119
    • Henry, R.1
  • 8
    • 0242494307 scopus 로고    scopus 로고
    • Localized reactive oxygen and nitrogen intermediates inhibit escape of Listeria monocytogenes from vacuoles in activated macrophages
    • Myers, J. T., Tsang, A. W. & Swanson, J. A. Localized reactive oxygen and nitrogen intermediates inhibit escape of Listeria monocytogenes from vacuoles in activated macrophages. J. Immunol. 171, 5447-5453 (2003).
    • (2003) J. Immunol , vol.171 , pp. 5447-5453
    • Myers, J.T.1    Tsang, A.W.2    Swanson, J.A.3
  • 9
    • 0022630209 scopus 로고
    • Multiplication of Shigella flexneri within HeLa cells: Lysis of the phagocytic vacuole and plasmid-mediated contact hemolysis
    • Sansonetti, P. J., Ryter, A., Clerc, P., Maurelli, A. T. & Mounier, J. Multiplication of Shigella flexneri within HeLa cells: Lysis of the phagocytic vacuole and plasmid-mediated contact hemolysis. Infect. Immun. 51, 461-469 (1986).
    • (1986) Infect. Immun , vol.51 , pp. 461-469
    • Sansonetti, P.J.1    Ryter, A.2    Clerc, P.3    Maurelli, A.T.4    Mounier, J.5
  • 10
    • 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. 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).
    • (2008) Infect. Immun , vol.76 , pp. 2671-2677
    • Santic, M.1    Asare, R.2    Skrobonja, I.3    Jones, S.4    Abu Kwaik, Y.5
  • 11
    • 33645553471 scopus 로고    scopus 로고
    • Membrane perforations inhibit lysosome fusion by altering pH and calcium in Listeria monocytogenes vacuoles
    • Shaughnessy, L. M., Hoppe, A. D., Christensen, J. A. & Swanson, J. A. Membrane perforations inhibit lysosome fusion by altering pH and calcium in Listeria monocytogenes vacuoles. Cell. Microbiol. 8 781-792 (2006).
    • (2006) Cell. Microbiol , vol.8 , pp. 781-792
    • Shaughnessy, L.M.1    Hoppe, A.D.2    Christensen, J.A.3    Swanson, J.A.4
  • 12
    • 0028819298 scopus 로고
    • Rickettsia conorii entry into Vero cells
    • Teysseire, N., Boudier, J. A. & Raoult, D. Rickettsia conorii entry into Vero cells. Infect. Immun. 63, 366-374 (1995).
    • (1995) Infect. Immun , vol.63 , pp. 366-374
    • Teysseire, N.1    Boudier, J.A.2    Raoult, D.3
  • 13
    • 0024741693 scopus 로고
    • Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes
    • Tilney, L. G. & Portnoy, D. A. Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes. J. Cell Biol. 109, 1597-1608 (1989).
    • (1989) J. Cell Biol , vol.109 , pp. 1597-1608
    • Tilney, L.G.1    Portnoy, D.A.2
  • 14
    • 17444415369 scopus 로고    scopus 로고
    • The kinetics of phagosome maturation as a function of phagosome/lysosome fusion and acquisition of hydrolytic activity
    • Yates, R. M., Hermetter, A. & Russell, D. G. The kinetics of phagosome maturation as a function of phagosome/lysosome fusion and acquisition of hydrolytic activity. Traffic 6, 413-420 (2005).
    • (2005) Traffic , vol.6 , pp. 413-420
    • Yates, R.M.1    Hermetter, A.2    Russell, D.G.3
  • 15
    • 0024464468 scopus 로고
    • Listeriolysin O is essential for virulence of Listeria monocytogenes: Direct evidence obtained by gene complementation
    • Cossart, P. et al. Listeriolysin O is essential for virulence of Listeria monocytogenes: Direct evidence obtained by gene complementation. Infect. Immun. 57, 3629-3636 (1989).
    • (1989) Infect. Immun , vol.57 , pp. 3629-3636
    • Cossart, P.1
  • 16
    • 0033977538 scopus 로고    scopus 로고
    • Role of listeriolysin O in cell-to-cell spread of Listeria monocytogenes
    • Gedde, M. M., Higgins, D. E., Tilney, L. G. & Portnoy, D. A. Role of listeriolysin O in cell-to-cell spread of Listeria monocytogenes. Infect. Immun. 68, 999-1003 (2000).
    • (2000) Infect. Immun , vol.68 , pp. 999-1003
    • Gedde, M.M.1    Higgins, D.E.2    Tilney, L.G.3    Portnoy, D.A.4
  • 17
    • 0023898917 scopus 로고
    • Role of hemolysin for the intracellular growth of Listeria monocytogenes
    • Portnoy, D. A., Jacks, P. S. & Hinrichs, D. J. Role of hemolysin for the intracellular growth of Listeria monocytogenes. J. Exp. Med. 167, 1459-1471 (1988).
    • (1988) J. Exp. Med , vol.167 , pp. 1459-1471
    • Portnoy, D.A.1    Jacks, P.S.2    Hinrichs, D.J.3
  • 18
    • 0028828198 scopus 로고
    • The two distinct phospholipases C of Listeria monocytogenes have overlapping roles in escape from a vacuole and cell-to-cell spread
    • Smith, G. A. et al. The two distinct phospholipases C of Listeria monocytogenes have overlapping roles in escape from a vacuole and cell-to-cell spread. Infect. Immun. 63, 4231-4237 (1995).
    • (1995) Infect. Immun , vol.63 , pp. 4231-4237
    • Smith, G.A.1
  • 19
    • 0025329666 scopus 로고
    • Bacillus subtilis expressing a hemolysin gene from Listeria monocytogenes can grow in mammalian cells
    • Bielecki, J., Youngman, P., Connelly, P. & Portnoy, D. A. Bacillus subtilis expressing a hemolysin gene from Listeria monocytogenes can grow in mammalian cells. Nature 345, 175-176 (1990).
    • (1990) Nature , vol.345 , pp. 175-176
    • Bielecki, J.1    Youngman, P.2    Connelly, P.3    Portnoy, D.A.4
  • 20
    • 0026710550 scopus 로고
    • Capacity of listeriolysin O, streptolysin O, and perfringolysin O to mediate growth of Bacillus subtilis within mammalian cells
    • Portnoy, D. A., Tweten, R. K., Kehoe, M. & Bielecki, J. Capacity of listeriolysin O, streptolysin O, and perfringolysin O to mediate growth of Bacillus subtilis within mammalian cells. Infect. Immun. 60, 2710-2717 (1992).
    • (1992) Infect. Immun , vol.60 , pp. 2710-2717
    • Portnoy, D.A.1    Tweten, R.K.2    Kehoe, M.3    Bielecki, J.4
  • 21
    • 0027476804 scopus 로고
    • Dual roles of plcA in Listeria monocytogenes pathogenesis
    • Camilli, A., Tilney, L. G. & Portnoy, D. A. Dual roles of plcA in Listeria monocytogenes pathogenesis. Mol. Microbiol. 8 143-157 (1993).
    • (1993) Mol. Microbiol , vol.8 , pp. 143-157
    • Camilli, A.1    Tilney, L.G.2    Portnoy, D.A.3
  • 22
    • 0033955871 scopus 로고    scopus 로고
    • pH-regulated activation and release of a bacteria-associated phospholipase C during intracellular infection by Listeria monocytogenes
    • Marquis, H. & Hager, E. J. pH-regulated activation and release of a bacteria-associated phospholipase C during intracellular infection by Listeria monocytogenes. Mol. Microbiol. 35, 289-298 (2000).
    • (2000) Mol. Microbiol , vol.35 , pp. 289-298
    • Marquis, H.1    Hager, E.J.2
  • 23
    • 33746529256 scopus 로고    scopus 로고
    • Regulated translation of listeriolysin O controls virulence of Listeria monocytogenes
    • Schnupf, P. et al. Regulated translation of listeriolysin O controls virulence of Listeria monocytogenes. Mol. Microbiol. 61, 999-1012 (2006).
    • (2006) Mol. Microbiol , vol.61 , pp. 999-1012
    • Schnupf, P.1
  • 24
    • 0344851711 scopus 로고    scopus 로고
    • Listeria monocytogenes mutants that fail to compartmentalize listerolysin O activity are cytotoxic, avirulent, and unable to evade host extracellular defenses
    • Glomski, I. J., Decatur, A. L. & Portnoy, D. A. Listeria monocytogenes mutants that fail to compartmentalize listerolysin O activity are cytotoxic, avirulent, and unable to evade host extracellular defenses. Infect. Immun. 71, 6754-6765 (2003).
    • (2003) Infect. Immun , vol.71 , pp. 6754-6765
    • Glomski, I.J.1    Decatur, A.L.2    Portnoy, D.A.3
  • 25
    • 0037128936 scopus 로고    scopus 로고
    • The Listeria monocytogenes hemolysin has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells
    • Glomski, I. J., Gedde, M. M., Tsang, A. W., Swanson, J. A. & Portnoy, D. A. The Listeria monocytogenes hemolysin has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells. J. Cell Biol. 156, 1029-1038 (2002).
    • (2002) J. Cell Biol , vol.156 , pp. 1029-1038
    • Glomski, I.J.1    Gedde, M.M.2    Tsang, A.W.3    Swanson, J.A.4    Portnoy, D.A.5
  • 26
    • 55249111793 scopus 로고    scopus 로고
    • GILT is a critical host factor for Listeria monocytogenes infection
    • Singh, R., Jamieson, A. & Cresswell, P. GILT is a critical host factor for Listeria monocytogenes infection. Nature 455, 1244-1247 (2008).
    • (2008) Nature , vol.455 , pp. 1244-1247
    • Singh, R.1    Jamieson, A.2    Cresswell, P.3
  • 27
    • 0023189876 scopus 로고
    • Purification, characterization, and toxicity of the sulfhydryl-activated hemolysin listeriolysin O from Listeria monocytogenes
    • Geoffroy, C., Gaillard, J. L., Alouf, J. E. & Berche, P. Purification, characterization, and toxicity of the sulfhydryl-activated hemolysin listeriolysin O from Listeria monocytogenes. Infect. Immun. 55 1641-1646 (1987).
    • (1987) Infect. Immun , vol.55 , pp. 1641-1646
    • Geoffroy, C.1    Gaillard, J.L.2    Alouf, J.E.3    Berche, P.4
  • 28
    • 0026534213 scopus 로고
    • IpaB of Shigella flexneri causes entry into epithelial cells and escape from the phagocytic vacuole
    • High, N., Mounier, J., Prevost, M. C. & Sansonetti, P. J. IpaB of Shigella flexneri causes entry into epithelial cells and escape from the phagocytic vacuole. EMBO J. 11, 1991-1999 (1992).
    • (1992) EMBO J , vol.11 , pp. 1991-1999
    • High, N.1    Mounier, J.2    Prevost, M.C.3    Sansonetti, P.J.4
  • 29
    • 17644366419 scopus 로고    scopus 로고
    • Cholesterol binding by the bacterial type III translocon is essential for virulence effector delivery into mammalian cells
    • Hayward, R. D. et al. Cholesterol binding by the bacterial type III translocon is essential for virulence effector delivery into mammalian cells. Mol. Microbiol. 56, 590-603 (2005).
    • (2005) Mol. Microbiol , vol.56 , pp. 590-603
    • Hayward, R.D.1
  • 30
    • 15544376398 scopus 로고    scopus 로고
    • IpaD of Shigella flexneri is independently required for regulation of Ipa protein secretion and efficient insertion of IpaB and IpaC into host membranes
    • Picking, W. L. et al. IpaD of Shigella flexneri is independently required for regulation of Ipa protein secretion and efficient insertion of IpaB and IpaC into host membranes. Infect. Immun. 73, 1432-1440 (2005).
    • (2005) Infect. Immun , vol.73 , pp. 1432-1440
    • Picking, W.L.1
  • 31
    • 0021854510 scopus 로고
    • Cloning of plasmid DNA sequences involved in invasion of HeLa cells by Shigella flexneri
    • Maurelli, A. T., Baudry, B., Dhauteville, H., Hale, T. L. & Sansonetti, P. J. Cloning of plasmid DNA sequences involved in invasion of HeLa cells by Shigella flexneri. Infect. Immun. 49, 164-171 (1985).
    • (1985) Infect. Immun , vol.49 , pp. 164-171
    • Maurelli, A.T.1    Baudry, B.2    Dhauteville, H.3    Hale, T.L.4    Sansonetti, P.J.5
  • 32
    • 0020003681 scopus 로고
    • Involvement of a plasmid in the invasive ability of Shigella flexneri
    • Sansonetti, P. J., Kopecko, D. J. & Formal, S. B. Involvement of a plasmid in the invasive ability of Shigella flexneri. Infect. Immun. 35, 852-860 (1982).
    • (1982) Infect. Immun , vol.35 , pp. 852-860
    • Sansonetti, P.J.1    Kopecko, D.J.2    Formal, S.B.3
  • 33
    • 0034110502 scopus 로고    scopus 로고
    • 7.8 facilitates escape of virulent bacteria from the endocytic vacuoles of mouse and human macrophages
    • 7.8 facilitates escape of virulent bacteria from the endocytic vacuoles of mouse and human macrophages. Infect. Immun. 68, 3608-3619 (2000).
    • (2000) Infect. Immun , vol.68 , pp. 3608-3619
    • Fernandez-Prada, C.M.1
  • 34
    • 34848886359 scopus 로고    scopus 로고
    • Shigella flexneri phagosomal escape is independent of invasion
    • Paetzold, S., Lourido, S., Raupach, B. & Zychlinsky, A. Shigella flexneri phagosomal escape is independent of invasion. Infect. Immun. 75, 4826-4830 (2007).
    • (2007) Infect. Immun , vol.75 , pp. 4826-4830
    • Paetzold, S.1    Lourido, S.2    Raupach, B.3    Zychlinsky, A.4
  • 35
    • 33646897295 scopus 로고    scopus 로고
    • Identification of Burkholderia pseudomallei genes required for the intracellular life cycle and in vivo virulence
    • Pilatz, S. et al. Identification of Burkholderia pseudomallei genes required for the intracellular life cycle and in vivo virulence. Infect. Immun. 74, 3576-3586 (2006).
    • (2006) Infect. Immun , vol.74 , pp. 3576-3586
    • Pilatz, S.1
  • 36
    • 25444490939 scopus 로고    scopus 로고
    • Expression of the Rickettsia prowazekii pld or tlyC gene in Salmonella enterica serovar typhimurium mediates phagosomal escape
    • Whitworth, T., Popov, V. L., Yu, X. J., Walker, D. H. & Bouyer, D. H. Expression of the Rickettsia prowazekii pld or tlyC gene in Salmonella enterica serovar typhimurium mediates phagosomal escape. Infect. Immun. 73, 6668-6673 (2005).
    • (2005) Infect. Immun , vol.73 , pp. 6668-6673
    • Whitworth, T.1    Popov, V.L.2    Yu, X.J.3    Walker, D.H.4    Bouyer, D.H.5
  • 37
    • 0242468462 scopus 로고    scopus 로고
    • Identification and characterization of a phospholipase D-superfamily gene in rickettsiae
    • Renesto, P. et al. Identification and characterization of a phospholipase D-superfamily gene in rickettsiae. J. Infect. Dis. 188, 1276-1283 (2003).
    • (2003) J. Infect. Dis , vol.188 , pp. 1276-1283
    • Renesto, P.1
  • 38
    • 0026664107 scopus 로고
    • Penetration of host cells by Rickettsia rickettsii appears to be mediated by a phospholipase of rickettsial origin
    • Silverman, D. J., Santucci, L. A., Meyers, N. & Sekeyova, Z. Penetration of host cells by Rickettsia rickettsii appears to be mediated by a phospholipase of rickettsial origin. Infect. Immun. 60, 2733-2740 (1992).
    • (1992) Infect. Immun , vol.60 , pp. 2733-2740
    • Silverman, D.J.1    Santucci, L.A.2    Meyers, N.3    Sekeyova, Z.4
  • 39
    • 0019942799 scopus 로고
    • Phospholipase A and the interaction of Rickettsia prowazekii and mouse fibroblasts (L-929 cells)
    • Winkler, H. H. & Miller, E. T. Phospholipase A and the interaction of Rickettsia prowazekii and mouse fibroblasts (L-929 cells). Infect. Immun. 38, 109-113 (1982).
    • (1982) Infect. Immun , vol.38 , pp. 109-113
    • Winkler, H.H.1    Miller, E.T.2
  • 40
    • 33749264796 scopus 로고    scopus 로고
    • Autophagy-mediated reentry of Francisella tularensis into the endocytic compartment after cytoplasmic replication
    • Checroun, C., Wehrly, T. D., Fischer, E. R., Hayes, S. F. & Celli, J. Autophagy-mediated reentry of Francisella tularensis into the endocytic compartment after cytoplasmic replication. Proc. Natl Acad. Sci. USA 103, 14578-14583 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 14578-14583
    • Checroun, C.1    Wehrly, T.D.2    Fischer, E.R.3    Hayes, S.F.4    Celli, J.5
  • 41
    • 2542552050 scopus 로고    scopus 로고
    • Virulent and avirulent strains of Francisella tularensis prevent acidification and maturation of their phagosomes and escape into the cytoplasm in human macrophages
    • Clemens, D. L., Lee, B. Y. & Horwitz, M. A. Virulent and avirulent strains of Francisella tularensis prevent acidification and maturation of their phagosomes and escape into the cytoplasm in human macrophages. Infect. Immun. 72, 3204-3217 (2004).
    • (2004) Infect. Immun , vol.72 , pp. 3204-3217
    • Clemens, D.L.1    Lee, B.Y.2    Horwitz, M.A.3
  • 42
    • 21344468870 scopus 로고    scopus 로고
    • The Francisella tularensis pathogenicity island protein IglC and its regulator MglA are essential for modulating phagosome biogenesis and subsequent bacterial escape into the cytoplasm
    • Santic, M., Molmeret, M., Klose, K. E., Jones, S. & Kwaik, Y. A. The Francisella tularensis pathogenicity island protein IglC and its regulator MglA are essential for modulating phagosome biogenesis and subsequent bacterial escape into the cytoplasm. Cell. Microbiol. 7, 969-979 (2005).
    • (2005) Cell. Microbiol , vol.7 , pp. 969-979
    • Santic, M.1    Molmeret, M.2    Klose, K.E.3    Jones, S.4    Kwaik, Y.A.5
  • 43
    • 58449112802 scopus 로고    scopus 로고
    • Identification of an essential Francisella tularensis subsp. tularensis virulence factor
    • Qin, A., Scott, D. W., Thompson, J. A. & Mann, B. J. Identification of an essential Francisella tularensis subsp. tularensis virulence factor. Infect. Immun. 77, 152-161 (2009).
    • (2009) Infect. Immun , vol.77 , pp. 152-161
    • Qin, A.1    Scott, D.W.2    Thompson, J.A.3    Mann, B.J.4
  • 44
    • 0031871879 scopus 로고    scopus 로고
    • Inactivation of dsbA, but not dsbC and dsbD, affects the intracellular survival and virulence of Shigella flexneri
    • Yu, J. Inactivation of dsbA, but not dsbC and dsbD, affects the intracellular survival and virulence of Shigella flexneri. Infect. Immun. 66, 3909-3917 (1998).
    • (1998) Infect. Immun , vol.66 , pp. 3909-3917
    • Yu, J.1
  • 45
    • 0033792965 scopus 로고    scopus 로고
    • Key role for DsbA in cell-to-cell spread of Shigella flexneri, permitting secretion of Ipa proteins into interepithelial protrusions
    • Yu, J., Edwards-Jones, B., Neyrolles, O. & Kroll, J. S. Key role for DsbA in cell-to-cell spread of Shigella flexneri, permitting secretion of Ipa proteins into interepithelial protrusions. Infect. Immun. 68, 6449-6456 (2000).
    • (2000) Infect. Immun , vol.68 , pp. 6449-6456
    • Yu, J.1    Edwards-Jones, B.2    Neyrolles, O.3    Kroll, J.S.4
  • 46
    • 0029025060 scopus 로고
    • Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells
    • Watarai, M., Tobe, T., Yoshikawa, M. & Sasakawa, C. Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells. Proc. Natl Acad. Sci. USA 92, 4927-4931 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 4927-4931
    • Watarai, M.1    Tobe, T.2    Yoshikawa, M.3    Sasakawa, C.4
  • 48
    • 33845424970 scopus 로고    scopus 로고
    • Differential function of Listeria monocytogenes listeriolysin O and phospholipases C in vacuolar dissolution following cell-to-cell spread
    • Alberti-Segui, C., Goeden, K. R. & Higgins, D. E. Differential function of Listeria monocytogenes listeriolysin O and phospholipases C in vacuolar dissolution following cell-to-cell spread. Cell. Microbiol. 9, 179-195 (2007).
    • (2007) Cell. Microbiol , vol.9 , pp. 179-195
    • Alberti-Segui, C.1    Goeden, K.R.2    Higgins, D.E.3
  • 49
    • 33846024757 scopus 로고    scopus 로고
    • Compartmentalization of the broad-range phospholipase C activity to the spreading vacuole is critical for Listeria monocytogenes virulence
    • Yeung, P. S., Na, Y., Kreuder, A. J. & Marquis, H. Compartmentalization of the broad-range phospholipase C activity to the spreading vacuole is critical for Listeria monocytogenes virulence. Infect. Immun. 75, 44-51 (2007).
    • (2007) Infect. Immun , vol.75 , pp. 44-51
    • Yeung, P.S.1    Na, Y.2    Kreuder, A.J.3    Marquis, H.4
  • 50
    • 0032746658 scopus 로고    scopus 로고
    • A system for identifying post-invasion functions of invasion genes: Requirements for the Mxi-Spa type III secretion pathway of Shigella flexneri in intercellular dissemination
    • Schuch, R., Sandlin, R. C. & Maurelli, A. T. A system for identifying post-invasion functions of invasion genes: Requirements for the Mxi-Spa type III secretion pathway of Shigella flexneri in intercellular dissemination. Mol. Microbiol. 34, 675-689 (1999).
    • (1999) Mol. Microbiol , vol.34 , pp. 675-689
    • Schuch, R.1    Sandlin, R.C.2    Maurelli, A.T.3
  • 51
    • 0033188152 scopus 로고    scopus 로고
    • The secreted IpaB and IpaC invasins and their cytoplasmic chaperone IpgC are required for intercellular dissemination of Shigella flexneri
    • Page, A. L., Ohayon, H., Sansonetti, P. J. & Parsot, C. The secreted IpaB and IpaC invasins and their cytoplasmic chaperone IpgC are required for intercellular dissemination of Shigella flexneri. Cell. Microbiol. 1, 183-193 (1999).
    • (1999) Cell. Microbiol , vol.1 , pp. 183-193
    • Page, A.L.1    Ohayon, H.2    Sansonetti, P.J.3    Parsot, C.4
  • 52
    • 0034843552 scopus 로고    scopus 로고
    • Actin-based motility is sufficient for bacterial membrane protrusion formation and host cell uptake
    • Monack, D. M. & Theriot, J. A. Actin-based motility is sufficient for bacterial membrane protrusion formation and host cell uptake. Cell. Microbiol. 3, 633-647 (2001).
    • (2001) Cell. Microbiol , vol.3 , pp. 633-647
    • Monack, D.M.1    Theriot, J.A.2
  • 53
    • 0035833989 scopus 로고    scopus 로고
    • Microinjection and growth of bacteria in the cytosol of mammalian host cells
    • Goetz, M. et al. Microinjection and growth of bacteria in the cytosol of mammalian host cells. Proc. Natl Acad. Sci. USA 98 12221-12226 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 12221-12226
    • Goetz, M.1
  • 54
    • 0033973827 scopus 로고    scopus 로고
    • Bacterial replication in the host cell cytosol
    • Goebel, W. & Kuhn, M. Bacterial replication in the host cell cytosol. Curr. Opin. Microbiol. 3, 49-53 (2000).
    • (2000) Curr. Opin. Microbiol , vol.3 , pp. 49-53
    • Goebel, W.1    Kuhn, M.2
  • 55
    • 0036685429 scopus 로고    scopus 로고
    • The host cytosol: Frontline or home front?
    • O'Riordan, M. & Portnoy, D. A. The host cytosol: Frontline or home front? Trends Microbiol. 10, 361-364 (2002).
    • (2002) Trends Microbiol , vol.10 , pp. 361-364
    • O'Riordan, M.1    Portnoy, D.A.2
  • 56
    • 0343517154 scopus 로고    scopus 로고
    • Salmonella maintains the integrity of its intracellular vacuole through the action of SifA
    • Beuzon, C. R. et al. Salmonella maintains the integrity of its intracellular vacuole through the action of SifA. EMBO J. 19 3235-3249 (2000).
    • (2000) EMBO J , vol.19 , pp. 3235-3249
    • Beuzon, C.R.1
  • 57
    • 0036259995 scopus 로고    scopus 로고
    • Disruption of the Salmonella-containing vacuole leads to increased replication of Salmonella enterica serovar Typhimurium in the cytosol of epithelial cells
    • Brumell, J. H., Tang, P., Zaharik, M. L. & Finlay, B. B. Disruption of the Salmonella-containing vacuole leads to increased replication of Salmonella enterica serovar Typhimurium in the cytosol of epithelial cells. Infect. Immun. 70, 3264-3270 (2002).
    • (2002) Infect. Immun , vol.70 , pp. 3264-3270
    • Brumell, J.H.1    Tang, P.2    Zaharik, M.L.3    Finlay, B.B.4
  • 58
    • 0036736564 scopus 로고    scopus 로고
    • Growth and killing of a Salmonella enterica serovar Typhimurium sifA mutant strain in the cytosol of different host cell lines
    • Beuzon, C. R., Salcedo, S. P. & Holden, D. W. Growth and killing of a Salmonella enterica serovar Typhimurium sifA mutant strain in the cytosol of different host cell lines. Microbiology 148, 2705-2715 (2002).
    • (2002) Microbiology , vol.148 , pp. 2705-2715
    • Beuzon, C.R.1    Salcedo, S.P.2    Holden, D.W.3
  • 59
    • 0035134947 scopus 로고    scopus 로고
    • SifA permits survival and replication of Salmonella typhimurium in murine macrophages
    • Brumell, J. H., Rosenberger, C. M., Gotto, G. T., Marcus, S. L. & Finlay, B. B. SifA permits survival and replication of Salmonella typhimurium in murine macrophages. Cell. Microbiol. 3, 75-84 (2001).
    • (2001) Cell. Microbiol , vol.3 , pp. 75-84
    • Brumell, J.H.1    Rosenberger, C.M.2    Gotto, G.T.3    Marcus, S.L.4    Finlay, B.B.5
  • 60
    • 50249151489 scopus 로고    scopus 로고
    • Francisella tularensis: Unravelling the secrets of an intracellular pathogen
    • Oyston, P. C. F. Francisella tularensis: Unravelling the secrets of an intracellular pathogen. J. Med. Microbiol. 57, 921-930 (2008).
    • (2008) J. Med. Microbiol , vol.57 , pp. 921-930
    • Oyston, P.C.F.1
  • 61
    • 30344481715 scopus 로고    scopus 로고
    • Francisella tularensis travels a novel, twisted road within macrophages
    • Santic, M., Molmeret, M., Klose, K. E. & Abu Kwaik, Y. Francisella tularensis travels a novel, twisted road within macrophages. Trends Microbiol. 14, 37-44 (2006).
    • (2006) Trends Microbiol , vol.14 , pp. 37-44
    • Santic, M.1    Molmeret, M.2    Klose, K.E.3    Abu Kwaik, Y.4
  • 62
    • 34447137410 scopus 로고    scopus 로고
    • Rickettsiae and rickettsial infections: The current state of knowledge
    • Walker, D. H. Rickettsiae and rickettsial infections: The current state of knowledge. Clin. Infect. Dis. 45, S39-S44 (2007).
    • (2007) Clin. Infect. Dis , vol.45
    • Walker, D.H.1
  • 63
    • 53449094756 scopus 로고    scopus 로고
    • Listeria monocytogenes, a unique model in infection biology: An overview
    • Cossart, P. & Toledo-Arana, A. Listeria monocytogenes, a unique model in infection biology: An overview. Microbes Infect. 10, 1041-1050 (2008).
    • (2008) Microbes Infect , vol.10 , pp. 1041-1050
    • Cossart, P.1    Toledo-Arana, A.2
  • 66
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic-reticulum
    • Hwang, C., Sinskey, A. J. & Lodish, H. F. Oxidized redox state of glutathione in the endoplasmic-reticulum. Science 257, 1496-1502 (1992).
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 67
    • 45849123222 scopus 로고    scopus 로고
    • A cytosolic iron chaperone that delivers iron to ferritin
    • Shi, H., Bencze, K. Z., Stemmler, T. L. & Philpott, C. C. A cytosolic iron chaperone that delivers iron to ferritin. Science 320, 1207-1210 (2008).
    • (2008) Science , vol.320 , pp. 1207-1210
    • Shi, H.1    Bencze, K.Z.2    Stemmler, T.L.3    Philpott, C.C.4
  • 68
    • 0027214122 scopus 로고
    • Intracytoplasmic growth and virulence of Listeria monocytogenes auxotrophic mutants
    • Marquis, H., Bouwer, H. G. A., Hinrichs, D. J. & Portnoy, D. A. Intracytoplasmic growth and virulence of Listeria monocytogenes auxotrophic mutants. Infect. Immun. 61, 3756-3760 (1993).
    • (1993) Infect. Immun , vol.61 , pp. 3756-3760
    • Marquis, H.1    Bouwer, H.G.A.2    Hinrichs, D.J.3    Portnoy, D.A.4
  • 69
    • 4644240236 scopus 로고    scopus 로고
    • Growth, virulence, and immunogenicity of Listeria monocytogenes aro mutants
    • Stritzker, J. et al. Growth, virulence, and immunogenicity of Listeria monocytogenes aro mutants. Infect. Immun. 72, 5622-5629 (2004).
    • (2004) Infect. Immun , vol.72 , pp. 5622-5629
    • Stritzker, J.1
  • 70
    • 0037039397 scopus 로고    scopus 로고
    • Hpt, a bacterial homolog of the microsomal glucose-6-phosphate translocase, mediates rapid intracellular proliferation in Listeria
    • Chico-Calero, I. et al. Hpt, a bacterial homolog of the microsomal glucose-6-phosphate translocase, mediates rapid intracellular proliferation in Listeria. Proc. Natl Acad. Sci. USA 99, 431-436 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 431-436
    • Chico-Calero, I.1
  • 71
    • 47749134181 scopus 로고    scopus 로고
    • Carbon metabolism of Listeria monocytogenes growing inside macrophages
    • Eylert, E. et al. Carbon metabolism of Listeria monocytogenes growing inside macrophages. Mol. Microbiol. 69, 1008-1017 (2008).
    • (2008) Mol. Microbiol , vol.69 , pp. 1008-1017
    • Eylert, E.1
  • 72
    • 0030778201 scopus 로고    scopus 로고
    • Glucose-1-phosphate utilization by Listeria monocytogenes is PrfA dependent and coordinately expressed with virulence factors
    • Ripio, M. T., Brehm, K., Lara, M., Suarez, M. & VazquezBoland, J. A. Glucose-1-phosphate utilization by Listeria monocytogenes is PrfA dependent and coordinately expressed with virulence factors. J. Bacteriol. 179, 7174-7180 (1997).
    • (1997) J. Bacteriol , vol.179 , pp. 7174-7180
    • Ripio, M.T.1    Brehm, K.2    Lara, M.3    Suarez, M.4    VazquezBoland, J.A.5
  • 73
    • 0035955375 scopus 로고    scopus 로고
    • Comparative genomics of Listeria species
    • Glaser, P. et al. Comparative genomics of Listeria species. Science 294, 849-852 (2001).
    • (2001) Science , vol.294 , pp. 849-852
    • Glaser, P.1
  • 74
    • 0030747906 scopus 로고    scopus 로고
    • A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria
    • Jordan, S. W. & Cronan, J. E. A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. J. Biol. Chem. 272, 17903-17906 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 17903-17906
    • Jordan, S.W.1    Cronan, J.E.2
  • 75
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: Catalytic machines for multistep reactions
    • Perham, R. N. Swinging arms and swinging domains in multifunctional enzymes: Catalytic machines for multistep reactions. Annu. Rev. Biochem. 69, 961-1004 (2000).
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 961-1004
    • Perham, R.N.1
  • 76
    • 35448931669 scopus 로고    scopus 로고
    • LpIA1-dependent utilization of host lipoyl peptides enables Listeria cytosolic growth and virulence
    • Keeney, K. M., Stuckey, J. A. & O'Riordan, M. X. D. LpIA1-dependent utilization of host lipoyl peptides enables Listeria cytosolic growth and virulence. Mol. Microbiol. 66, 758-770 (2007).
    • (2007) Mol. Microbiol , vol.66 , pp. 758-770
    • Keeney, K.M.1    Stuckey, J.A.2    O'Riordan, M.X.D.3
  • 77
    • 0142116232 scopus 로고    scopus 로고
    • Listeria intracellular growth and virulence require host-derived lipoic acid
    • O'Riordan, M., Moors, M. A. & Portnoy, D. A. Listeria intracellular growth and virulence require host-derived lipoic acid. Science 302, 462-464 (2003).
    • (2003) Science , vol.302 , pp. 462-464
    • O'Riordan, M.1    Moors, M.A.2    Portnoy, D.A.3
  • 78
    • 0029665144 scopus 로고    scopus 로고
    • Engineered ΔguaB-A ΔvirG Shigella flexneri 2a strain CVD 1205: Construction, safety, immunogenicity, and potential efficacy as a mucosal vaccine
    • Noriega, F. R. et al. Engineered ΔguaB-A ΔvirG Shigella flexneri 2a strain CVD 1205: Construction, safety, immunogenicity, and potential efficacy as a mucosal vaccine. Infect. Immun. 64 3055-3061 (1996).
    • (1996) Infect. Immun , vol.64 , pp. 3055-3061
    • Noriega, F.R.1
  • 79
    • 0345714728 scopus 로고    scopus 로고
    • Analysis of virulence and inflammatory potential of Shigella flexneri purine biosynthesis mutants
    • Cersini, A., Martino, M. C., Martini, I., Rossi, G. & Bernardini, M. L. Analysis of virulence and inflammatory potential of Shigella flexneri purine biosynthesis mutants. Infect. Immun. 71, 7002-7013 (2003).
    • (2003) Infect. Immun , vol.71 , pp. 7002-7013
    • Cersini, A.1    Martino, M.C.2    Martini, I.3    Rossi, G.4    Bernardini, M.L.5
  • 80
    • 0031932645 scopus 로고    scopus 로고
    • Intracellular multiplication and virulence of Shigella flexneri auxotrophic mutants
    • Cersini, A., Salvia, A. M. & Bernardini, M. L. Intracellular multiplication and virulence of Shigella flexneri auxotrophic mutants. Infect. Immun. 66, 549-557 (1998).
    • (1998) Infect. Immun , vol.66 , pp. 549-557
    • Cersini, A.1    Salvia, A.M.2    Bernardini, M.L.3
  • 81
    • 0036739240 scopus 로고    scopus 로고
    • Selection of Shigella flexneri candidate virulence genes specifically induced in bacteria resident in host cell cytoplasm
    • Bartoleschi, C. et al. Selection of Shigella flexneri candidate virulence genes specifically induced in bacteria resident in host cell cytoplasm. Cell. Microbiol. 4, 613-626 (2002).
    • (2002) Cell. Microbiol , vol.4 , pp. 613-626
    • Bartoleschi, C.1
  • 82
    • 11144252281 scopus 로고    scopus 로고
    • Transcriptional adaptation of Shigella flexneri during infection of macrophages and epithelial cells: Insights into the strategies of a cytosolic bacterial pathogen
    • Lucchini, S., Liu, H., Jin, Q., Hinton, J. C. D. & Yu, J. Transcriptional adaptation of Shigella flexneri during infection of macrophages and epithelial cells: Insights into the strategies of a cytosolic bacterial pathogen. Infect. Immun. 73, 88-102 (2005).
    • (2005) Infect. Immun , vol.73 , pp. 88-102
    • Lucchini, S.1    Liu, H.2    Jin, Q.3    Hinton, J.C.D.4    Yu, J.5
  • 83
    • 0036073970 scopus 로고    scopus 로고
    • Identification of chromosomal Shigella flexneri genes induced by the eukaryotic intracellular environment
    • Runyen-Janecky, L. J. & Payne, S. M. Identification of chromosomal Shigella flexneri genes induced by the eukaryotic intracellular environment. Infect. Immun. 70, 4379-4388 (2002).
    • (2002) Infect. Immun , vol.70 , pp. 4379-4388
    • Runyen-Janecky, L.J.1    Payne, S.M.2
  • 84
    • 0023709265 scopus 로고
    • Proline incorporation into protein by Rickettsia prowazekii during growth in chinese hamster ovary (Cho-K1) cells
    • Austin, F. E. & Winkler, H. H. Proline incorporation into protein by Rickettsia prowazekii during growth in chinese hamster ovary (Cho-K1) cells. Infect. Immun. 56, 3167-3172 (1988).
    • (1988) Infect. Immun , vol.56 , pp. 3167-3172
    • Austin, F.E.1    Winkler, H.H.2
  • 85
    • 0023073674 scopus 로고
    • Rickettsia prowazekii requires host cell serine and glycine for growth
    • Austin, F. E., Turco, J. & Winkler, H. H. Rickettsia prowazekii requires host cell serine and glycine for growth. Infect. Immun. 55, 240-244 (1987).
    • (1987) Infect. Immun , vol.55 , pp. 240-244
    • Austin, F.E.1    Turco, J.2    Winkler, H.H.3
  • 87
    • 55849122258 scopus 로고    scopus 로고
    • RipA, a cytoplasmic membrane protein conserved among Francisella species, is required for intracellular survival
    • Fuller, J. R. et al. RipA, a cytoplasmic membrane protein conserved among Francisella species, is required for intracellular survival. Infect. Immun. 76, 4934-4943 (2008).
    • (2008) Infect. Immun , vol.76 , pp. 4934-4943
    • Fuller, J.R.1
  • 88
    • 34548411393 scopus 로고    scopus 로고
    • A Francisella tularensis pathogenicity island protein essential for bacterial proliferation within the host cell cytosol
    • Santic, M. et al. A Francisella tularensis pathogenicity island protein essential for bacterial proliferation within the host cell cytosol. Cell. Microbiol. 9, 2391-2403 (2007).
    • (2007) Cell. Microbiol , vol.9 , pp. 2391-2403
    • Santic, M.1
  • 89
    • 48849105040 scopus 로고    scopus 로고
    • MglA and Igl proteins contribute to the modulation of Francisella tularensis live vaccine strain-containing phagosomes in murine macrophages
    • Bonquist, L., Lindgren, H., Golovliov, I., Guina, T. & Sjostedt, A. MglA and Igl proteins contribute to the modulation of Francisella tularensis live vaccine strain-containing phagosomes in murine macrophages. Infect. Immun. 76, 3502-3510 (2008).
    • (2008) Infect. Immun , vol.76 , pp. 3502-3510
    • Bonquist, L.1    Lindgren, H.2    Golovliov, I.3    Guina, T.4    Sjostedt, A.5
  • 90
    • 0032843865 scopus 로고    scopus 로고
    • Ubiquicidin, a novel murine microbicidal protein present in the cytosolic fraction of macrophages
    • Hiemstra, P. S., van den Barselaar, M. T., Roest, M., Nibbering, P. H. & van Furth, R. Ubiquicidin, a novel murine microbicidal protein present in the cytosolic fraction of macrophages. J. Leukoc. Biol. 66 423-428 (1999).
    • (1999) J. Leukoc. Biol , vol.66 , pp. 423-428
    • Hiemstra, P.S.1    van den Barselaar, M.T.2    Roest, M.3    Nibbering, P.H.4    van Furth, R.5
  • 91
    • 33846136089 scopus 로고    scopus 로고
    • Innate recognition of intracellular bacteria
    • Delbridge, L. M. & O'Riordan, M. X. Innate recognition of intracellular bacteria. Curr. Opin. Immunol. 19, 10-16 (2007).
    • (2007) Curr. Opin. Immunol , vol.19 , pp. 10-16
    • Delbridge, L.M.1    O'Riordan, M.X.2
  • 93
    • 57649166494 scopus 로고    scopus 로고
    • Eating the enemy within: Autophagy in infectious diseases
    • Orvedahl, A. & Levine, B. Eating the enemy within: Autophagy in infectious diseases. Cell Death Differ. 16, 57-69 (2008).
    • (2008) Cell Death Differ , vol.16 , pp. 57-69
    • Orvedahl, A.1    Levine, B.2
  • 94
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: Core machinery and adaptations
    • Xie, Z. & Klionsky, D. J. Autophagosome formation: Core machinery and adaptations. Nature Cell Biol. 9, 1102-1109 (2007).
    • (2007) Nature Cell Biol , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 95
    • 55249109400 scopus 로고    scopus 로고
    • Autophagosome-independent essential function for the autophagy protein Atg5 in cellular immunity to intracellular pathogens
    • Zhao, Z. et al. Autophagosome-independent essential function for the autophagy protein Atg5 in cellular immunity to intracellular pathogens. Cell Host Microbe 4, 458-469 (2008).
    • (2008) Cell Host Microbe , vol.4 , pp. 458-469
    • Zhao, Z.1
  • 96
    • 0037711625 scopus 로고    scopus 로고
    • Cytoplasmic bacteria can be targets for autophagy
    • Rich, K. A., Burkett, C. & Webster, P. Cytoplasmic bacteria can be targets for autophagy. Cell. Microbiol. 5, 455-468 (2003).
    • (2003) Cell. Microbiol , vol.5 , pp. 455-468
    • Rich, K.A.1    Burkett, C.2    Webster, P.3
  • 97
    • 47849094901 scopus 로고    scopus 로고
    • Autophagic control of listeria through intracellular innate immune recognition in drosophila
    • Yano, T. et al. Autophagic control of listeria through intracellular innate immune recognition in drosophila. Nature Immunol. 9, 908-916 (2008).
    • (2008) Nature Immunol , vol.9 , pp. 908-916
    • Yano, T.1
  • 98
    • 33947416152 scopus 로고    scopus 로고
    • Autophagy limits Listeria monocytogenes intracellular growth in the early phase of primary infection
    • Py, B. F., Lipinski, M. M. & Yuan, J. Y. Autophagy limits Listeria monocytogenes intracellular growth in the early phase of primary infection. Autophagy 3, 117-125 (2007).
    • (2007) Autophagy , vol.3 , pp. 117-125
    • Py, B.F.1    Lipinski, M.M.2    Yuan, J.Y.3
  • 99
    • 34548067415 scopus 로고    scopus 로고
    • Listeria monocytogenes evades killing by autophagy during colonization of host cells
    • Birmingham, C. L. et al. Listeria monocytogenes evades killing by autophagy during colonization of host cells. Autophagy 3, 442-451 (2007).
    • (2007) Autophagy , vol.3 , pp. 442-451
    • Birmingham, C.L.1
  • 100
    • 38349110486 scopus 로고    scopus 로고
    • Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles
    • Birmingham, C. L. et al. Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles. Nature 451 350-354 (2008).
    • (2008) Nature , vol.451 , pp. 350-354
    • Birmingham, C.L.1
  • 101
    • 13244256806 scopus 로고    scopus 로고
    • Escape of intracellular Shigella from autophagy
    • Ogawa, M. et al. Escape of intracellular Shigella from autophagy. Science 307, 727-731 (2005).
    • (2005) Science , vol.307 , pp. 727-731
    • Ogawa, M.1
  • 102
    • 50249111985 scopus 로고    scopus 로고
    • Stimulation of autophagy suppresses the intracellular survival of Burkholderia pseudomallei in mammalian cell lines
    • Cullinane, M. et al. Stimulation of autophagy suppresses the intracellular survival of Burkholderia pseudomallei in mammalian cell lines. Autophagy 4, 744-753 (2008).
    • (2008) Autophagy , vol.4 , pp. 744-753
    • Cullinane, M.1
  • 103
    • 4444223808 scopus 로고    scopus 로고
    • Attenuated virulence and protective efficacy of a Burkholderia pseudomallei bsa type III secretion mutant in murine models of melioidosis
    • Stevens, M. P. et al. Attenuated virulence and protective efficacy of a Burkholderia pseudomallei bsa type III secretion mutant in murine models of melioidosis. Microbiology 150, 2669-2676 (2004).
    • (2004) Microbiology , vol.150 , pp. 2669-2676
    • Stevens, M.P.1
  • 104
    • 51449099913 scopus 로고    scopus 로고
    • Microarray analysis of human monocytes infected with Francisella tularensis identifies new targets of host response subversion
    • Butchar, J. P. et al. Microarray analysis of human monocytes infected with Francisella tularensis identifies new targets of host response subversion. PLoS ONE 3, e2924 (2008).
    • (2008) PLoS ONE , vol.3
    • Butchar, J.P.1
  • 105
    • 0242611003 scopus 로고    scopus 로고
    • Mycobacterium marinum escapes from phagosomes and is propelled by actin-based motility
    • Stamm, L. M. et al. Mycobacterium marinum escapes from phagosomes and is propelled by actin-based motility. J. Exp. Med. 198, 1361-1368 (2003).
    • (2003) J. Exp. Med , vol.198 , pp. 1361-1368
    • Stamm, L.M.1
  • 106
    • 34250716965 scopus 로고    scopus 로고
    • van der Wel, N. et al. M. tuberculosis and M. leprae translocate from the phagolysosome to the cytosol in myeloid cells. Cell 129, 1287-1298 (2007).
    • van der Wel, N. et al. M. tuberculosis and M. leprae translocate from the phagolysosome to the cytosol in myeloid cells. Cell 129, 1287-1298 (2007).
  • 107
    • 55749090842 scopus 로고    scopus 로고
    • The HrpB-HrpA two-partnet secretion system is-essential for intracellular survival of Neisseria meningitidis
    • Tala. A. et al. The HrpB-HrpA two-partnet secretion system is-essential for intracellular survival of Neisseria meningitidis. Cell. Microbiol. 10, 2461-2482(2008).
    • (2008) Cell. Microbiol , vol.10 , pp. 2461-2482
    • Tala, A.1
  • 108
    • 13444301168 scopus 로고    scopus 로고
    • Actin-based motility of intracellular pathogens
    • Gouin, E., Welch, M. D. & Cossart, P. Actin-based motility of intracellular pathogens. Curr. Opin. Microbiol. 8, 35-45 (2005).
    • (2005) Curr. Opin. Microbiol , vol.8 , pp. 35-45
    • Gouin, E.1    Welch, M.D.2    Cossart, P.3
  • 109
    • 3042710591 scopus 로고    scopus 로고
    • Regulation of cytoskeletal dynamics by actin-monomer-binding proteins
    • Paavilainen, V. O., Bertling, E., Falck, S. & Lappalainen, P. Regulation of cytoskeletal dynamics by actin-monomer-binding proteins. Trends Cell Biol. 14, 386-394 (2004).
    • (2004) Trends Cell Biol , vol.14 , pp. 386-394
    • Paavilainen, V.O.1    Bertling, E.2    Falck, S.3    Lappalainen, P.4
  • 111
    • 0026515440 scopus 로고    scopus 로고
    • Kocks, C. et al. L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 68, 521-531 (1992).
    • Kocks, C. et al. L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 68, 521-531 (1992).
  • 112
    • 16244364769 scopus 로고    scopus 로고
    • Identification of a bacterial factor required for actin-based motility of Burkholderia pseudomallei
    • Stevens, M. P. et al. Identification of a bacterial factor required for actin-based motility of Burkholderia pseudomallei. Mol. Microbiol. 56, 40-53 (2005).
    • (2005) Mol. Microbiol , vol.56 , pp. 40-53
    • Stevens, M.P.1
  • 113
    • 0842263990 scopus 로고    scopus 로고
    • The RickA protein of Rickettsia conorii activates the Arp2/3 complex
    • Gouin, E. et al. The RickA protein of Rickettsia conorii activates the Arp2/3 complex. Nature 427, 457-461 (2004).
    • (2004) Nature , vol.427 , pp. 457-461
    • Gouin, E.1
  • 114
    • 4043176919 scopus 로고    scopus 로고
    • A Rickettsia WASP-like protein activates the Arp2/3 complex and mediates actin-based motility
    • Jeng, R. L. et al. A Rickettsia WASP-like protein activates the Arp2/3 complex and mediates actin-based motility. Cell. Microbiol. 6, 761-769 (2004).
    • (2004) Cell. Microbiol , vol.6 , pp. 761-769
    • Jeng, R.L.1
  • 115
    • 0035949529 scopus 로고    scopus 로고
    • Listeria protein ActA mimics WASP family proteins: It activates filament barbed end branching by Arp2/3 complex
    • Boujemaa-Paterski, R. et al. Listeria protein ActA mimics WASP family proteins: It activates filament barbed end branching by Arp2/3 complex. Biochemistry 40, 11390-11404 (2001).
    • (2001) Biochemistry , vol.40 , pp. 11390-11404
    • Boujemaa-Paterski, R.1
  • 116
    • 0032479578 scopus 로고    scopus 로고
    • Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
    • Welch, M. D., Rosenblatt, J., Skoble, J., Portnoy, D. A. & Mitchison, T. J. Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 281, 105-108 (1998).
    • (1998) Science , vol.281 , pp. 105-108
    • Welch, M.D.1    Rosenblatt, J.2    Skoble, J.3    Portnoy, D.A.4    Mitchison, T.J.5
  • 117
    • 0038677954 scopus 로고    scopus 로고
    • Actin-based motility of Burkholderia pseudomallei involves the Arp 2/3 complex, but not N-WASP and Ena/ VASP proteins
    • Breitbach, K. et al. Actin-based motility of Burkholderia pseudomallei involves the Arp 2/3 complex, but not N-WASP and Ena/ VASP proteins. Cell. Microbiol. 5, 385-393 (2003).
    • (2003) Cell. Microbiol , vol.5 , pp. 385-393
    • Breitbach, K.1
  • 118
    • 0024362336 scopus 로고
    • Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin
    • Bernardini, M. L., Mounier, J., Dhauteville, H., Coquisrondon, M. & Sansonetti, P. J. Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin. Proc. Natl Acad. Sci. USA 86, 3867-3871 (1989).
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 3867-3871
    • Bernardini, M.L.1    Mounier, J.2    Dhauteville, H.3    Coquisrondon, M.4    Sansonetti, P.J.5
  • 119
    • 0033588990 scopus 로고    scopus 로고
    • Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility
    • Egile, C. et al. Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell Biol. 146 1319-1332 (1999).
    • (1999) J. Cell Biol , vol.146 , pp. 1319-1332
    • Egile, C.1
  • 120
    • 0033914895 scopus 로고    scopus 로고
    • Ultrastructure of Rickettsia rickettsii actin tails and localization of cytoskeletal proteins
    • Van Kirk, L. S., Hayes, S. F. & Heinzen, R. A. Ultrastructure of Rickettsia rickettsii actin tails and localization of cytoskeletal proteins. Infect. Immun. 68, 4706-4713 (2000).
    • (2000) Infect. Immun , vol.68 , pp. 4706-4713
    • Van Kirk, L.S.1    Hayes, S.F.2    Heinzen, R.A.3
  • 121
    • 0036441427 scopus 로고    scopus 로고
    • An Inv/Mxi-Spa-like type III protein secretion system in Burkholderia pseudomallei modulates intracellular behaviour of the pathogen
    • Stevens, M. P. et al. An Inv/Mxi-Spa-like type III protein secretion system in Burkholderia pseudomallei modulates intracellular behaviour of the pathogen. Mol. Microbiol. 46, 649-659 (2002).
    • (2002) Mol. Microbiol , vol.46 , pp. 649-659
    • Stevens, M.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.