메뉴 건너뛰기




Volumn 11, Issue 1, 2008, Pages 15-20

A novel pathway for exotoxin delivery by an intracellular pathogen

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; EXOTOXIN;

EID: 40849102399     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2007.12.002     Document Type: Review
Times cited : (20)

References (44)
  • 1
    • 3042568878 scopus 로고    scopus 로고
    • Large clostridial cytotoxins: cellular biology of Rho/Ras-glucosylating toxins
    • Schirmer J., and Aktories K. Large clostridial cytotoxins: cellular biology of Rho/Ras-glucosylating toxins. Biochim Biophys Acta 1673 (2004) 66-74
    • (2004) Biochim Biophys Acta , vol.1673 , pp. 66-74
    • Schirmer, J.1    Aktories, K.2
  • 3
    • 33748598700 scopus 로고    scopus 로고
    • Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
    • Gurcel L., Abrami L., Girardin S., Tschopp J., and van der Goot F.G. Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival. Cell 126 (2006) 1135-1145
    • (2006) Cell , vol.126 , pp. 1135-1145
    • Gurcel, L.1    Abrami, L.2    Girardin, S.3    Tschopp, J.4    van der Goot, F.G.5
  • 6
    • 0036441135 scopus 로고    scopus 로고
    • Membrane traffic exploited by protein toxins
    • Sandvig K., and van Deurs B. Membrane traffic exploited by protein toxins. Annu Rev Cell Dev Biol 18 (2002) 1-24
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 1-24
    • Sandvig, K.1    van Deurs, B.2
  • 7
    • 34548288267 scopus 로고    scopus 로고
    • Toxin entry and trafficking in mammalian cells
    • Watson P., and Spooner R.A. Toxin entry and trafficking in mammalian cells. Adv Drug Deliv Rev 58 (2006) 1581-1596
    • (2006) Adv Drug Deliv Rev , vol.58 , pp. 1581-1596
    • Watson, P.1    Spooner, R.A.2
  • 8
    • 36048988438 scopus 로고    scopus 로고
    • Where and how do anthrax toxins exit endosomes to intoxicate host cells?
    • Puhar A., and Montecucco C. Where and how do anthrax toxins exit endosomes to intoxicate host cells?. Trends Microbiol 15 (2007) 477-482
    • (2007) Trends Microbiol , vol.15 , pp. 477-482
    • Puhar, A.1    Montecucco, C.2
  • 9
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • Galan J.E., and Wolf-Watz H. Protein delivery into eukaryotic cells by type III secretion machines. Nature 444 (2006) 567-573
    • (2006) Nature , vol.444 , pp. 567-573
    • Galan, J.E.1    Wolf-Watz, H.2
  • 10
    • 1642415666 scopus 로고    scopus 로고
    • Unveiling molecular scaffolds of the type IV secretion system
    • Yeo H.J., and Waksman G. Unveiling molecular scaffolds of the type IV secretion system. J Bacteriol 186 (2004) 1919-1926
    • (2004) J Bacteriol , vol.186 , pp. 1919-1926
    • Yeo, H.J.1    Waksman, G.2
  • 11
    • 33750110911 scopus 로고    scopus 로고
    • The type III secretion injectisome
    • Cornelis G.R. The type III secretion injectisome. Nat Rev Microbiol 4 (2006) 811-825
    • (2006) Nat Rev Microbiol , vol.4 , pp. 811-825
    • Cornelis, G.R.1
  • 12
    • 33645865541 scopus 로고    scopus 로고
    • Type IV secretion systems and their effectors in bacterial pathogenesis
    • Backert S., and Meyer T.F. Type IV secretion systems and their effectors in bacterial pathogenesis. Curr Opin Microbiol 9 (2006) 207-217
    • (2006) Curr Opin Microbiol , vol.9 , pp. 207-217
    • Backert, S.1    Meyer, T.F.2
  • 13
    • 38049046618 scopus 로고    scopus 로고
    • Spanò S, Ugalde JE, Galán JE: Delivery of a Salmonella Typhi exotoxin from a host intracellular compartment. Cell Host & Microbe 2008, 3:30-38.
    • Spanò S, Ugalde JE, Galán JE: Delivery of a Salmonella Typhi exotoxin from a host intracellular compartment. Cell Host & Microbe 2008, 3:30-38. This paper describes a novel S. Typhi toxin that is delivered from an intracellular location by an unusual autocrine and paracrine pathway.
  • 15
    • 4444349432 scopus 로고    scopus 로고
    • Persistent bacterial infections: the interface of the pathogen and the host immune system
    • Monack D.M., Mueller A., and Falkow S. Persistent bacterial infections: the interface of the pathogen and the host immune system. Nat Rev Microbiol 2 (2004) 747-765
    • (2004) Nat Rev Microbiol , vol.2 , pp. 747-765
    • Monack, D.M.1    Mueller, A.2    Falkow, S.3
  • 16
    • 3142544236 scopus 로고    scopus 로고
    • Frontal and stealth attack strategies in microbial pathogenesis
    • Merrell D.S., and Falkow S. Frontal and stealth attack strategies in microbial pathogenesis. Nature 430 (2004) 250-256
    • (2004) Nature , vol.430 , pp. 250-256
    • Merrell, D.S.1    Falkow, S.2
  • 17
    • 27144472742 scopus 로고    scopus 로고
    • The functional interface between Salmonella and its host cell: opportunities for therapeutic intervention
    • Patel J.C., Rossanese O.W., and Galan J.E. The functional interface between Salmonella and its host cell: opportunities for therapeutic intervention. Trends Pharmacol Sci 26 (2005) 564-570
    • (2005) Trends Pharmacol Sci , vol.26 , pp. 564-570
    • Patel, J.C.1    Rossanese, O.W.2    Galan, J.E.3
  • 18
    • 31844438569 scopus 로고    scopus 로고
    • Salmonella type III secretion effectors: pulling the host cell's strings
    • Schlumberger M.C., and Hardt W.D. Salmonella type III secretion effectors: pulling the host cell's strings. Curr Opin Microbiol 9 (2006) 46-54
    • (2006) Curr Opin Microbiol , vol.9 , pp. 46-54
    • Schlumberger, M.C.1    Hardt, W.D.2
  • 19
    • 0035188434 scopus 로고    scopus 로고
    • Salmonella interactions with host cells: type III secretion at work
    • Galan J.E. Salmonella interactions with host cells: type III secretion at work. Annu Rev Cell Dev Biol 17 (2001) 53-86
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 53-86
    • Galan, J.E.1
  • 20
    • 20344376677 scopus 로고    scopus 로고
    • Problem pathogens: extra-intestinal complications of Salmonella enterica serotype Typhi infection
    • Huang D.B., and DuPont H.L. Problem pathogens: extra-intestinal complications of Salmonella enterica serotype Typhi infection. Lancet Infect Dis 5 (2005) 341-348
    • (2005) Lancet Infect Dis , vol.5 , pp. 341-348
    • Huang, D.B.1    DuPont, H.L.2
  • 22
    • 0036468520 scopus 로고    scopus 로고
    • Comparative genomics of closely related salmonellae
    • Edwards R.A., Olsen G.J., and Maloy S.R. Comparative genomics of closely related salmonellae. Trends Microbiol 10 (2002) 94-99
    • (2002) Trends Microbiol , vol.10 , pp. 94-99
    • Edwards, R.A.1    Olsen, G.J.2    Maloy, S.R.3
  • 24
    • 0036498707 scopus 로고    scopus 로고
    • Cytolethal distending toxin: limited damage as a strategy to modulate cellular functions
    • Lara-Tejero M., and Galan J.E. Cytolethal distending toxin: limited damage as a strategy to modulate cellular functions. Trends Microbiol 10 (2002) 147-152
    • (2002) Trends Microbiol , vol.10 , pp. 147-152
    • Lara-Tejero, M.1    Galan, J.E.2
  • 25
    • 1842585488 scopus 로고    scopus 로고
    • Salmonella typhi encodes a functional cytolethal distending toxin that is delivered into host cells by a bacterial-internalization pathway
    • Haghjoo E., and Galan J.E. Salmonella typhi encodes a functional cytolethal distending toxin that is delivered into host cells by a bacterial-internalization pathway. Proc Natl Acad Sci U S A 101 (2004) 4614-4619
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 4614-4619
    • Haghjoo, E.1    Galan, J.E.2
  • 26
    • 14544272400 scopus 로고    scopus 로고
    • Cytolethal distending toxin: creating a gap in the cell cycle
    • Heywood W., Henderson B., and Nair S.P. Cytolethal distending toxin: creating a gap in the cell cycle. J Med Microbiol 54 (2005) 207-216
    • (2005) J Med Microbiol , vol.54 , pp. 207-216
    • Heywood, W.1    Henderson, B.2    Nair, S.P.3
  • 27
    • 0030775355 scopus 로고    scopus 로고
    • Escherichia coli cytolethal distending toxin blocks the HeLa cell cycle at the G2/M transition by preventing cdc2 protein kinase dephosphorylation and activation
    • Comayras C., Tasca C., Peres S.Y., Ducommun B., Oswald E., and De Rycke J. Escherichia coli cytolethal distending toxin blocks the HeLa cell cycle at the G2/M transition by preventing cdc2 protein kinase dephosphorylation and activation. Infect Immun 65 (1997) 5088-5095
    • (1997) Infect Immun , vol.65 , pp. 5088-5095
    • Comayras, C.1    Tasca, C.2    Peres, S.Y.3    Ducommun, B.4    Oswald, E.5    De Rycke, J.6
  • 29
    • 0023891492 scopus 로고
    • A new heat-labile cytolethal distending toxin (CLDT) produced by Escherichia coli isolates from clinical material
    • Johnson W.M., and Lior H. A new heat-labile cytolethal distending toxin (CLDT) produced by Escherichia coli isolates from clinical material. Microb Pathog 4 (1988) 103-113
    • (1988) Microb Pathog , vol.4 , pp. 103-113
    • Johnson, W.M.1    Lior, H.2
  • 30
    • 0032722556 scopus 로고    scopus 로고
    • Cytolethal distending toxin of Haemophilus ducreyi induces apoptotic death of Jurkat T cells
    • Gelfanova V., Hansen E.J., and Spinola S.M. Cytolethal distending toxin of Haemophilus ducreyi induces apoptotic death of Jurkat T cells. Infect Immun 67 (1999) 6394-6402
    • (1999) Infect Immun , vol.67 , pp. 6394-6402
    • Gelfanova, V.1    Hansen, E.J.2    Spinola, S.M.3
  • 31
    • 0034987923 scopus 로고    scopus 로고
    • The impact of Haemophilus ducreyi cytolethal distending toxin on cells involved in immune response
    • Svensson L.A., Tarkowski A., Thelestam M., and Lagergard T. The impact of Haemophilus ducreyi cytolethal distending toxin on cells involved in immune response. Microb Pathog 30 (2001) 157-166
    • (2001) Microb Pathog , vol.30 , pp. 157-166
    • Svensson, L.A.1    Tarkowski, A.2    Thelestam, M.3    Lagergard, T.4
  • 32
    • 0035399760 scopus 로고    scopus 로고
    • Induction of apoptosis in human T cells by Actinobacillus actinomycetemcomitans cytolethal distending toxin is a consequence of G2 arrest of the cell cycle
    • Shenker B.J., Hoffmaster R.H., Zekavat A., Yamaguchi N., Lally E.T., and Demuth D.R. Induction of apoptosis in human T cells by Actinobacillus actinomycetemcomitans cytolethal distending toxin is a consequence of G2 arrest of the cell cycle. J Immunol 167 (2001) 435-441
    • (2001) J Immunol , vol.167 , pp. 435-441
    • Shenker, B.J.1    Hoffmaster, R.H.2    Zekavat, A.3    Yamaguchi, N.4    Lally, E.T.5    Demuth, D.R.6
  • 33
    • 23344435789 scopus 로고    scopus 로고
    • Intracellular survival of Campylobacter jejuni in human monocytic cells and induction of apoptotic death by cytholethal distending toxin
    • Hickey T.E., Majam G., and Guerry P. Intracellular survival of Campylobacter jejuni in human monocytic cells and induction of apoptotic death by cytholethal distending toxin. Infect Immun 73 (2005) 5194-5197
    • (2005) Infect Immun , vol.73 , pp. 5194-5197
    • Hickey, T.E.1    Majam, G.2    Guerry, P.3
  • 34
    • 33645515720 scopus 로고    scopus 로고
    • Exposure of lymphocytes to high doses of Actinobacillus actinomycetemcomitans cytolethal distending toxin induces rapid onset of apoptosis-mediated DNA fragmentation
    • Shenker B.J., Demuth D.R., and Zekavat A. Exposure of lymphocytes to high doses of Actinobacillus actinomycetemcomitans cytolethal distending toxin induces rapid onset of apoptosis-mediated DNA fragmentation. Infect Immun 74 (2006) 2080-2092
    • (2006) Infect Immun , vol.74 , pp. 2080-2092
    • Shenker, B.J.1    Demuth, D.R.2    Zekavat, A.3
  • 35
    • 0035895984 scopus 로고    scopus 로고
    • The Haemophilus ducreyi cytolethal distending toxin induces cell cycle arrest and apoptosis via the DNA damage checkpoint pathways
    • Cortes-Bratti X., Karlsson C., Lagergard T., Thelestam M., and Frisan T. The Haemophilus ducreyi cytolethal distending toxin induces cell cycle arrest and apoptosis via the DNA damage checkpoint pathways. J Biol Chem 276 (2001) 5296-5302
    • (2001) J Biol Chem , vol.276 , pp. 5296-5302
    • Cortes-Bratti, X.1    Karlsson, C.2    Lagergard, T.3    Thelestam, M.4    Frisan, T.5
  • 36
    • 0036123023 scopus 로고    scopus 로고
    • The Haemophilus ducreyi cytolethal distending toxin activates sensors of DNA damage and repair complexes in proliferating and non-proliferating cells
    • Li L., Sharipo A., Chaves-Olarte E., Masucci M.G., Levitsky V., Thelestam M., and Frisan T. The Haemophilus ducreyi cytolethal distending toxin activates sensors of DNA damage and repair complexes in proliferating and non-proliferating cells. Cell Microbiol 4 (2002) 87-99
    • (2002) Cell Microbiol , vol.4 , pp. 87-99
    • Li, L.1    Sharipo, A.2    Chaves-Olarte, E.3    Masucci, M.G.4    Levitsky, V.5    Thelestam, M.6    Frisan, T.7
  • 37
    • 0034644631 scopus 로고    scopus 로고
    • A bacterial toxin that controls cell cycle progression as a deoxyribonuclease I-like protein
    • Lara-Tejero M., and Galan J.E. A bacterial toxin that controls cell cycle progression as a deoxyribonuclease I-like protein. Science 290 (2000) 354-357
    • (2000) Science , vol.290 , pp. 354-357
    • Lara-Tejero, M.1    Galan, J.E.2
  • 38
    • 0033854239 scopus 로고    scopus 로고
    • DNase I homologous residues in CdtB are critical for cytolethal distending toxin-mediated cell cycle arrest
    • Elwell C.A., and Dreyfus L.A. DNase I homologous residues in CdtB are critical for cytolethal distending toxin-mediated cell cycle arrest. Mol Microbiol 37 (2000) 952-963
    • (2000) Mol Microbiol , vol.37 , pp. 952-963
    • Elwell, C.A.1    Dreyfus, L.A.2
  • 39
    • 0034967972 scopus 로고    scopus 로고
    • CdtA, CdtB, and CdtC form a tripartite complex that is required for cytolethal distending toxin activity
    • Lara-Tejero M., and Galan J.E. CdtA, CdtB, and CdtC form a tripartite complex that is required for cytolethal distending toxin activity. Infect Immun 69 (2001) 4358-4365
    • (2001) Infect Immun , vol.69 , pp. 4358-4365
    • Lara-Tejero, M.1    Galan, J.E.2
  • 40
    • 2642550772 scopus 로고    scopus 로고
    • Assembly and function of a bacterial genotoxin
    • Nesic D., Hsu Y., and Stebbins C.E. Assembly and function of a bacterial genotoxin. Nature 429 (2004) 429-433
    • (2004) Nature , vol.429 , pp. 429-433
    • Nesic, D.1    Hsu, Y.2    Stebbins, C.E.3
  • 42
    • 0034157346 scopus 로고    scopus 로고
    • Trafficking and release of mycobacterial lipids from infected macrophages
    • This paper describes that trafficking of mycobacterial lipids from the bacterial phagosome revealing a striking dynamic nature of the bacterial-containing vacuole.
    • Beatty W.L., Rhoades E.R., Ullrich H.J., Chatterjee D., Heuser J.E., and Russell D.G. Trafficking and release of mycobacterial lipids from infected macrophages. Traffic 1 (2000) 235-247. This paper describes that trafficking of mycobacterial lipids from the bacterial phagosome revealing a striking dynamic nature of the bacterial-containing vacuole.
    • (2000) Traffic , vol.1 , pp. 235-247
    • Beatty, W.L.1    Rhoades, E.R.2    Ullrich, H.J.3    Chatterjee, D.4    Heuser, J.E.5    Russell, D.G.6
  • 43
    • 0026634286 scopus 로고
    • Pertussis toxin and target eukaryotic cells: binding, entry, and activation
    • Kaslow H.R., and Burns D.L. Pertussis toxin and target eukaryotic cells: binding, entry, and activation. FASEB J 6 (1992) 2684-2690
    • (1992) FASEB J , vol.6 , pp. 2684-2690
    • Kaslow, H.R.1    Burns, D.L.2
  • 44
    • 0035077298 scopus 로고    scopus 로고
    • Campylobacter upsaliensis exerts a cytolethal distending toxin effect on HeLa cells and T lymphocytes
    • Mooney A., Clyne M., Curran T., Doherty D., Kilmartin B., and Bourke B. Campylobacter upsaliensis exerts a cytolethal distending toxin effect on HeLa cells and T lymphocytes. Microbiology 147 (2001) 735-743
    • (2001) Microbiology , vol.147 , pp. 735-743
    • Mooney, A.1    Clyne, M.2    Curran, T.3    Doherty, D.4    Kilmartin, B.5    Bourke, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.