메뉴 건너뛰기




Volumn 27, Issue 9, 2006, Pages 434-440

Anthrax toxins: a paradigm of bacterial immune suppression

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE CYCLASE TOXIN; ADENYLATE CYCLASE TOXIN A; ANTHRAX TOXIN; CHOLERA TOXIN; CYCLIC AMP; EDEMA TOXIN; EXOTOXIN; LETHAL TOXIN; MITOGEN ACTIVATED PROTEIN KINASE; PERTUSSIS TOXIN; UNCLASSIFIED DRUG;

EID: 33747066785     PISSN: 14714906     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.it.2006.07.002     Document Type: Review
Times cited : (139)

References (56)
  • 2
    • 24944453136 scopus 로고    scopus 로고
    • 100th anniversary of Robert Koch's Nobel Prize for the discovery of the tubercle bacillus
    • Kaufmann S.H., and Schaible U.E. 100th anniversary of Robert Koch's Nobel Prize for the discovery of the tubercle bacillus. Trends Microbiol. 10 (2005) 469-475
    • (2005) Trends Microbiol. , vol.10 , pp. 469-475
    • Kaufmann, S.H.1    Schaible, U.E.2
  • 3
    • 0345690145 scopus 로고    scopus 로고
    • Bioterrorism. Anthrax powder: state of the art?
    • Matsumoto G. Bioterrorism. Anthrax powder: state of the art?. Science 302 (2003) 1492-1497
    • (2003) Science , vol.302 , pp. 1492-1497
    • Matsumoto, G.1
  • 5
    • 0035829509 scopus 로고    scopus 로고
    • Identification of the cellular receptor for anthrax toxin
    • Bradley K.A., et al. Identification of the cellular receptor for anthrax toxin. Nature 414 (2001) 225-229
    • (2001) Nature , vol.414 , pp. 225-229
    • Bradley, K.A.1
  • 7
    • 0038303163 scopus 로고    scopus 로고
    • Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor
    • Scobie H.M., et al. Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 5170-5174
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5170-5174
    • Scobie, H.M.1
  • 8
    • 33646019842 scopus 로고    scopus 로고
    • The LDL receptor-related protein LRP6 mediates internalization and lethality of anthrax toxin
    • Wei W., et al. The LDL receptor-related protein LRP6 mediates internalization and lethality of anthrax toxin. Cell 124 (2006) 1141-1154
    • (2006) Cell , vol.124 , pp. 1141-1154
    • Wei, W.1
  • 9
    • 0026498189 scopus 로고
    • Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin
    • Klimpel K.R., et al. Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 10277-10281
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10277-10281
    • Klimpel, K.R.1
  • 10
    • 12944322216 scopus 로고    scopus 로고
    • Anthrax toxin: the long and winding road that leads to the kill
    • Abrami L., et al. Anthrax toxin: the long and winding road that leads to the kill. Trends Microbiol. 13 (2005) 72-78
    • (2005) Trends Microbiol. , vol.13 , pp. 72-78
    • Abrami, L.1
  • 11
    • 0000947082 scopus 로고
    • Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells
    • Leppla S.H. Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc. Natl. Acad. Sci. U. S. A. 79 (1982) 3162-3166
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 3162-3166
    • Leppla, S.H.1
  • 12
    • 0037165139 scopus 로고    scopus 로고
    • Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin
    • Drum C.L., et al. Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature 415 (2002) 396-402
    • (2002) Nature , vol.415 , pp. 396-402
    • Drum, C.L.1
  • 13
    • 0034672216 scopus 로고    scopus 로고
    • Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor
    • Vitale G., et al. Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor. Biochem. J. 352 (2000) 739-745
    • (2000) Biochem. J. , vol.352 , pp. 739-745
    • Vitale, G.1
  • 14
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signaling cascades
    • Chang L., and Karin M. Mammalian MAP kinase signaling cascades. Nature 410 (2001) 37-40
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 15
    • 33644976705 scopus 로고    scopus 로고
    • MAP kinases in immune responses
    • Zhang Y.L., and Dong C. MAP kinases in immune responses. Cell. Mol. Immunol. 2 (2005) 20-27
    • (2005) Cell. Mol. Immunol. , vol.2 , pp. 20-27
    • Zhang, Y.L.1    Dong, C.2
  • 16
    • 3242804491 scopus 로고    scopus 로고
    • Stop the killer: how to inhibit the anthrax lethal factor metalloprotease
    • Montecucco C., et al. Stop the killer: how to inhibit the anthrax lethal factor metalloprotease. Trends Biochem. Sci. 29 (2004) 282-285
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 282-285
    • Montecucco, C.1
  • 17
    • 1642617628 scopus 로고    scopus 로고
    • The protein kinase PKR is required for macrophage apoptosis after activation of Toll-like receptor 4
    • Hsu L.C., et al. The protein kinase PKR is required for macrophage apoptosis after activation of Toll-like receptor 4. Nature 428 (2004) 341-345
    • (2004) Nature , vol.428 , pp. 341-345
    • Hsu, L.C.1
  • 18
    • 0033965158 scopus 로고    scopus 로고
    • The p38 signal transduction pathway: activation and function
    • Ono K., and Han J. The p38 signal transduction pathway: activation and function. Cell. Signal. 12 (2000) 1-13
    • (2000) Cell. Signal. , vol.12 , pp. 1-13
    • Ono, K.1    Han, J.2
  • 19
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • Kyriakis J.M., and Avruch J. Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol. Rev. 81 (2001) 807-869
    • (2001) Physiol. Rev. , vol.81 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 20
    • 7244231301 scopus 로고    scopus 로고
    • MAP kinases and cell migration
    • Huang C., et al. MAP kinases and cell migration. J. Cell Sci. 117 (2004) 4619-4628
    • (2004) J. Cell Sci. , vol.117 , pp. 4619-4628
    • Huang, C.1
  • 21
    • 0023938335 scopus 로고
    • The adenylate cyclase-cAMP-protein kinase A pathway and regulation of the immune response
    • Kammer G.M. The adenylate cyclase-cAMP-protein kinase A pathway and regulation of the immune response. Immunol. Today 9 (1988) 222-229
    • (1988) Immunol. Today , vol.9 , pp. 222-229
    • Kammer, G.M.1
  • 22
    • 0037144590 scopus 로고    scopus 로고
    • Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition
    • Park J.M., et al. Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition. Science 297 (2002) 2048-2051
    • (2002) Science , vol.297 , pp. 2048-2051
    • Park, J.M.1
  • 23
    • 0036295213 scopus 로고    scopus 로고
    • Lethal toxin of Bacillus anthracis causes apoptosis of macrophages
    • Popov S.G., et al. Lethal toxin of Bacillus anthracis causes apoptosis of macrophages. Biochem. Biophys. Res. Commun. 293 (2002) 349-355
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 349-355
    • Popov, S.G.1
  • 24
    • 2442701424 scopus 로고    scopus 로고
    • Anthrax lethal toxin rapidly activates caspase-1/ICE and induces extracellular release of interleukin (IL)-1β and IL-18
    • Cordoba-Rodriguez R., et al. Anthrax lethal toxin rapidly activates caspase-1/ICE and induces extracellular release of interleukin (IL)-1β and IL-18. J. Biol. Chem. 279 (2004) 20563-20566
    • (2004) J. Biol. Chem. , vol.279 , pp. 20563-20566
    • Cordoba-Rodriguez, R.1
  • 25
    • 0033056295 scopus 로고    scopus 로고
    • Proteasome activity is required for anthrax lethal toxin to kill macrophages
    • Tang G., and Leppla S.H. Proteasome activity is required for anthrax lethal toxin to kill macrophages. Infect. Immun. 67 (1999) 3055-3056
    • (1999) Infect. Immun. , vol.67 , pp. 3055-3056
    • Tang, G.1    Leppla, S.H.2
  • 26
    • 31744441475 scopus 로고    scopus 로고
    • Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin
    • Boyden E.D., and Dietrich W.F. Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat. Genet. 38 (2006) 240-244
    • (2006) Nat. Genet. , vol.38 , pp. 240-244
    • Boyden, E.D.1    Dietrich, W.F.2
  • 27
    • 33644701849 scopus 로고    scopus 로고
    • The inflammasome
    • 10.1016/j.cub.2005.07.049
    • Petrilli V., et al. The inflammasome. Curr. Biol. 15 (2005) R581. http://www.sciencedirect.com 10.1016/j.cub.2005.07.049
    • (2005) Curr. Biol. , vol.15
    • Petrilli, V.1
  • 28
    • 85047692288 scopus 로고    scopus 로고
    • Bacillus anthracis lethal toxin induces TNF-α-independent hypoxia-mediated toxicity in mice
    • Moayeri M., et al. Bacillus anthracis lethal toxin induces TNF-α-independent hypoxia-mediated toxicity in mice. J. Clin. Invest. 112 (2003) 670-682
    • (2003) J. Clin. Invest. , vol.112 , pp. 670-682
    • Moayeri, M.1
  • 29
    • 24944554790 scopus 로고    scopus 로고
    • Signalling pathways and genes that inhibit pathogen-induced macrophage apoptosis - CREB and NF-κB as key regulators
    • Park J.M., et al. Signalling pathways and genes that inhibit pathogen-induced macrophage apoptosis - CREB and NF-κB as key regulators. Immunity 23 (2005) 319-329
    • (2005) Immunity , vol.23 , pp. 319-329
    • Park, J.M.1
  • 30
    • 0041695260 scopus 로고    scopus 로고
    • Decreased glycogen synthase kinase 3-β levels and related physiological changes in Bacillus anthracis lethal toxin-treated macrophages
    • Tucker A.E., et al. Decreased glycogen synthase kinase 3-β levels and related physiological changes in Bacillus anthracis lethal toxin-treated macrophages. Cell. Microbiol. 5 (2003) 523-532
    • (2003) Cell. Microbiol. , vol.5 , pp. 523-532
    • Tucker, A.E.1
  • 31
    • 15044363028 scopus 로고    scopus 로고
    • Recent advances in the protein kinase B signalling pathway
    • Woodgett J.R. Recent advances in the protein kinase B signalling pathway. Curr. Opin. Cell Biol. 17 (2005) 150-157
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 150-157
    • Woodgett, J.R.1
  • 32
    • 27744496768 scopus 로고    scopus 로고
    • The biology of p38 kinase: a central role in inflammation
    • Schieven G.L. The biology of p38 kinase: a central role in inflammation. Curr. Top. Med. Chem. 5 (2005) 921-928
    • (2005) Curr. Top. Med. Chem. , vol.5 , pp. 921-928
    • Schieven, G.L.1
  • 33
    • 21344474327 scopus 로고    scopus 로고
    • From JNK to pay dirt: jun kinases, their biochemistry, physiology and clinical importance
    • Karin M., and Gallagher E. From JNK to pay dirt: jun kinases, their biochemistry, physiology and clinical importance. IUBMB Life 57 (2005) 283-295
    • (2005) IUBMB Life , vol.57 , pp. 283-295
    • Karin, M.1    Gallagher, E.2
  • 34
    • 0032755353 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFNγ-induced release of NO and TNFα
    • Pellizzari R., et al. Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFNγ-induced release of NO and TNFα. FEBS Lett. 462 (1999) 199-204
    • (1999) FEBS Lett. , vol.462 , pp. 199-204
    • Pellizzari, R.1
  • 35
    • 12844271628 scopus 로고    scopus 로고
    • Murine macrophage transcriptional responses to Bacillus anthracis infection and intoxication
    • Bergman N.H., et al. Murine macrophage transcriptional responses to Bacillus anthracis infection and intoxication. Infect. Immun. 73 (2005) 1069-1080
    • (2005) Infect. Immun. , vol.73 , pp. 1069-1080
    • Bergman, N.H.1
  • 36
    • 33644880791 scopus 로고    scopus 로고
    • Sublethal doses of Bacillus anthracis lethal toxin inhibit inflammation with lipopolysaccharide and Escherichia coli challenge but have opposite effects on survival
    • Cui X., et al. Sublethal doses of Bacillus anthracis lethal toxin inhibit inflammation with lipopolysaccharide and Escherichia coli challenge but have opposite effects on survival. J. Infect. Dis. 193 (2006) 829-840
    • (2006) J. Infect. Dis. , vol.193 , pp. 829-840
    • Cui, X.1
  • 37
    • 1642577137 scopus 로고    scopus 로고
    • Anthrax lethal toxin inhibits activation of IFN-regulatory factor 3 by lipopolysaccharide
    • Dang O., et al. Anthrax lethal toxin inhibits activation of IFN-regulatory factor 3 by lipopolysaccharide. J. Immunol. 172 (2004) 747-751
    • (2004) J. Immunol. , vol.172 , pp. 747-751
    • Dang, O.1
  • 38
    • 0022973265 scopus 로고
    • Anthrax toxin blocks priming of neutrophils by lipopolysaccharide and by muramyl dipeptide
    • Wright G.G., and Mandell G.L. Anthrax toxin blocks priming of neutrophils by lipopolysaccharide and by muramyl dipeptide. J. Exp. Med. 164 (1986) 1700-1709
    • (1986) J. Exp. Med. , vol.164 , pp. 1700-1709
    • Wright, G.G.1    Mandell, G.L.2
  • 39
    • 0021930758 scopus 로고
    • Effects of anthrax toxin components on human neutrophils
    • O'Brien J., et al. Effects of anthrax toxin components on human neutrophils. Infect. Immun. 47 (1985) 306-310
    • (1985) Infect. Immun. , vol.47 , pp. 306-310
    • O'Brien, J.1
  • 40
    • 23944507581 scopus 로고    scopus 로고
    • Anthrax lethal toxin paralyzes neutrophil actin-based motility
    • During R.L., et al. Anthrax lethal toxin paralyzes neutrophil actin-based motility. J. Infect. Dis. 192 (2005) 837-845
    • (2005) J. Infect. Dis. , vol.192 , pp. 837-845
    • During, R.L.1
  • 41
    • 17844389894 scopus 로고    scopus 로고
    • Dendritic cells endocytose Bacillus anthracis spores: implications for anthrax pathogenesis
    • Brittingham K.C., et al. Dendritic cells endocytose Bacillus anthracis spores: implications for anthrax pathogenesis. J. Immunol. 174 (2005) 5545-5552
    • (2005) J. Immunol. , vol.174 , pp. 5545-5552
    • Brittingham, K.C.1
  • 42
    • 36749009663 scopus 로고    scopus 로고
    • Anthrax lethal toxin-mediated killing of human and murine dendritic cells impairs the adaptive immune response
    • 10.1371/journal. ppat. 0010019
    • Alileche A., et al. Anthrax lethal toxin-mediated killing of human and murine dendritic cells impairs the adaptive immune response. PLoS Pathogens (2005) e19. http://pathogens.plosjournals.org 10.1371/journal. ppat. 0010019
    • (2005) PLoS Pathogens
    • Alileche, A.1
  • 43
    • 0042964832 scopus 로고    scopus 로고
    • Impairment of dendritic cells and adaptive immunity by anthrax lethal toxin
    • Agrawal A., et al. Impairment of dendritic cells and adaptive immunity by anthrax lethal toxin. Nature 424 (2003) 329-334
    • (2003) Nature , vol.424 , pp. 329-334
    • Agrawal, A.1
  • 44
    • 17044400220 scopus 로고    scopus 로고
    • Anthrax edema toxin cooperates with lethal toxin to impair cytokine secretion during infection of dendritic cells
    • Tournier J.N., et al. Anthrax edema toxin cooperates with lethal toxin to impair cytokine secretion during infection of dendritic cells. J. Immunol. 174 (2005) 4934-4941
    • (2005) J. Immunol. , vol.174 , pp. 4934-4941
    • Tournier, J.N.1
  • 45
    • 15744404676 scopus 로고    scopus 로고
    • Role of superoxide in the germination of Bacillus anthracis endospores
    • Baillie L., et al. Role of superoxide in the germination of Bacillus anthracis endospores. FEMS Microbiol. Lett. 245 (2005) 33-38
    • (2005) FEMS Microbiol. Lett. , vol.245 , pp. 33-38
    • Baillie, L.1
  • 46
    • 2142659332 scopus 로고    scopus 로고
    • Macrophages release tumor necrosis factor alpha and interleukin-12 in response to intracellular Bacillus anthracis spores
    • Pickering A.K., and Merkel T.J. Macrophages release tumor necrosis factor alpha and interleukin-12 in response to intracellular Bacillus anthracis spores. Infect. Immun. 72 (2004) 3069-3072
    • (2004) Infect. Immun. , vol.72 , pp. 3069-3072
    • Pickering, A.K.1    Merkel, T.J.2
  • 47
    • 7044227860 scopus 로고    scopus 로고
    • Cytokine response to infection with Bacillus anthracis spores
    • Pickering A.K., et al. Cytokine response to infection with Bacillus anthracis spores. Infect. Immun. 72 (2004) 6382-6389
    • (2004) Infect. Immun. , vol.72 , pp. 6382-6389
    • Pickering, A.K.1
  • 48
    • 33645504807 scopus 로고    scopus 로고
    • Importance of nitric oxide synthase in the control of infection by Bacillus anthracis
    • Raines K.W., et al. Importance of nitric oxide synthase in the control of infection by Bacillus anthracis. Infect. Immun. 74 (2006) 2268-2276
    • (2006) Infect. Immun. , vol.74 , pp. 2268-2276
    • Raines, K.W.1
  • 49
    • 0036221384 scopus 로고    scopus 로고
    • MAP kinases in the immune response
    • Dong C., et al. MAP kinases in the immune response. Annu. Rev. Immunol. 20 (2002) 55-72
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 55-72
    • Dong, C.1
  • 50
    • 28444498350 scopus 로고    scopus 로고
    • Direct inhibition of T-lymphocyte activation by anthrax toxins in vivo
    • Comer J.E., et al. Direct inhibition of T-lymphocyte activation by anthrax toxins in vivo. Infect. Immun. 73 (2005) 8275-8281
    • (2005) Infect. Immun. , vol.73 , pp. 8275-8281
    • Comer, J.E.1
  • 51
    • 17044378194 scopus 로고    scopus 로고
    • + T cells
    • + T cells. J. Immunol. 174 (2005) 4966-4971
    • (2005) J. Immunol. , vol.174 , pp. 4966-4971
    • Fang, H.1
  • 52
    • 13644268542 scopus 로고    scopus 로고
    • Anthrax toxins suppress T lymphocyte activation by disrupting antigen receptor signalling
    • Rossi Paccani S., et al. Anthrax toxins suppress T lymphocyte activation by disrupting antigen receptor signalling. J. Exp. Med. 201 (2005) 325-331
    • (2005) J. Exp. Med. , vol.201 , pp. 325-331
    • Rossi Paccani, S.1
  • 53
    • 33646484203 scopus 로고    scopus 로고
    • Anthrax lethal toxin has direct and potent inhibitory effects on B cell proliferation and immunoglobulin production
    • Fang H., et al. Anthrax lethal toxin has direct and potent inhibitory effects on B cell proliferation and immunoglobulin production. J. Immunol. 176 (2006) 6155-6161
    • (2006) J. Immunol. , vol.176 , pp. 6155-6161
    • Fang, H.1
  • 54
    • 4644263749 scopus 로고    scopus 로고
    • Immune responses to Bacillus anthracis protective antigen in patients with bioterrorism-related cutaneous or inhalation anthrax
    • Quinn C.P., et al. Immune responses to Bacillus anthracis protective antigen in patients with bioterrorism-related cutaneous or inhalation anthrax. J. Infect. Dis. 190 (2004) 1228-1236
    • (2004) J. Infect. Dis. , vol.190 , pp. 1228-1236
    • Quinn, C.P.1
  • 56
    • 0035969533 scopus 로고    scopus 로고
    • Recognition and management of anthrax - an update
    • Swartz M.N. Recognition and management of anthrax - an update. New Engl. J. Med. 345 (2001) 1621-1626
    • (2001) New Engl. J. Med. , vol.345 , pp. 1621-1626
    • Swartz, M.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.