메뉴 건너뛰기




Volumn 21, Issue 1, 2005, Pages 35-41

Sabotage and exploitation in macrophages parasitized by intracellular protozoans

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; TOLL LIKE RECEPTOR;

EID: 11444261151     PISSN: 14714922     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pt.2004.10.004     Document Type: Review
Times cited : (69)

References (73)
  • 1
    • 0030937832 scopus 로고    scopus 로고
    • Nitric oxide and macrophage function
    • J. MacMicking Nitric oxide and macrophage function Annu. Rev. Immunol. 15 1997 323 350
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 323-350
    • MacMicking, J.1
  • 2
    • 0035019794 scopus 로고    scopus 로고
    • Oxygen-dependent anti-Salmonella activity of macrophages
    • A. Vazquez-Torres, and F.C. Fang Oxygen-dependent anti-Salmonella activity of macrophages Trends Microbiol. 9 2001 29 33
    • (2001) Trends Microbiol. , vol.9 , pp. 29-33
    • Vazquez-Torres, A.1    Fang, F.C.2
  • 3
    • 0036216769 scopus 로고    scopus 로고
    • Phagocytosis of microbes: Complexity in action
    • D.M. Underhill, and A. Ozinsky Phagocytosis of microbes: complexity in action Annu. Rev. Immunol. 20 2002 825 852
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 825-852
    • Underhill, D.M.1    Ozinsky, A.2
  • 5
    • 0033495303 scopus 로고    scopus 로고
    • Parasite persistence correlates with disease severity and localization in chronic Chagas' disease
    • L. Zhang, and R.L. Tarleton Parasite persistence correlates with disease severity and localization in chronic Chagas' disease J. Infect. Dis. 180 1999 480 486
    • (1999) J. Infect. Dis. , vol.180 , pp. 480-486
    • Zhang, L.1    Tarleton, R.L.2
  • 7
    • 0027493801 scopus 로고
    • Toxoplasmic encephalitis in patients with the acquired immunodeficiency syndrome
    • B.J. Luft Toxoplasmic encephalitis in patients with the acquired immunodeficiency syndrome N. Engl. J. Med. 329 1993 995 1000
    • (1993) N. Engl. J. Med. , vol.329 , pp. 995-1000
    • Luft, B.J.1
  • 8
    • 0034235989 scopus 로고    scopus 로고
    • Leishmania-host-cell interaction: Complexities and alternative views
    • M.G. Rittig, and C. Bogdan Leishmania-host-cell interaction: complexities and alternative views Parasitol. Today 16 2000 292 297
    • (2000) Parasitol. Today , vol.16 , pp. 292-297
    • Rittig, M.G.1    Bogdan, C.2
  • 9
    • 0022413168 scopus 로고
    • The mouse macrophage receptor for C3bi (CR3) is a major mechanism in the phagocytosis of Leishmania promastigotes
    • D.M. Mosser, and P.J. Edelson The mouse macrophage receptor for C3bi (CR3) is a major mechanism in the phagocytosis of Leishmania promastigotes J. Immunol. 135 1985 2785 2789
    • (1985) J. Immunol. , vol.135 , pp. 2785-2789
    • Mosser, D.M.1    Edelson, P.J.2
  • 10
    • 0031005660 scopus 로고    scopus 로고
    • Inhibition of phagolysosomal biogenesis by the Leishmania lipophosphoglycan
    • M. Desjardins, and A. Descoteaux Inhibition of phagolysosomal biogenesis by the Leishmania lipophosphoglycan J. Exp. Med. 185 1997 2061 2068
    • (1997) J. Exp. Med. , vol.185 , pp. 2061-2068
    • Desjardins, M.1    Descoteaux, A.2
  • 11
    • 0035895960 scopus 로고    scopus 로고
    • Phosphoglycan repeat-deficient Leishmania mexicana parasites remain infectious to macrophages and mice
    • T. Ilg Phosphoglycan repeat-deficient Leishmania mexicana parasites remain infectious to macrophages and mice J. Biol. Chem. 276 2001 4988 4997
    • (2001) J. Biol. Chem. , vol.276 , pp. 4988-4997
    • Ilg, T.1
  • 12
    • 0034085602 scopus 로고    scopus 로고
    • Leishmania promastigotes require lipophosphoglycan to actively modulate the fusion properties of phagosomes at an early stage in phagocytosis
    • J.F. Dermine Leishmania promastigotes require lipophosphoglycan to actively modulate the fusion properties of phagosomes at an early stage in phagocytosis Cell. Microbiol. 2 2000 115 126
    • (2000) Cell. Microbiol. , vol.2 , pp. 115-126
    • Dermine, J.F.1
  • 13
    • 0032991895 scopus 로고    scopus 로고
    • How do protozoan parasites survive inside macrophages?
    • C. Bogdan, and M. Rollinghoff How do protozoan parasites survive inside macrophages? Parasitol. Today 15 1999 22 28
    • (1999) Parasitol. Today , vol.15 , pp. 22-28
    • Bogdan, C.1    Rollinghoff, M.2
  • 14
    • 0041856096 scopus 로고    scopus 로고
    • Toxoplasma gondii: Perfecting an intracellular life style
    • L.D. Sibley Toxoplasma gondii: perfecting an intracellular life style Traffic 4 2003 581 586
    • (2003) Traffic , vol.4 , pp. 581-586
    • Sibley, L.D.1
  • 15
    • 0029869791 scopus 로고    scopus 로고
    • Toxoplasma invasion of mammalian cells is powered by the actin cytoskeleton of the parasite
    • J.M. Dobrowski, and L.D. Sibley Toxoplasma invasion of mammalian cells is powered by the actin cytoskeleton of the parasite Cell 84 1996 933 939
    • (1996) Cell , vol.84 , pp. 933-939
    • Dobrowski, J.M.1    Sibley, L.D.2
  • 16
    • 0033397899 scopus 로고    scopus 로고
    • Invasion by Toxoplasma gondii establishes a moving junction that selectively excludes host cell plasma membrane proteins on the basis of their membrane anchoring
    • D.G. Mordue Invasion by Toxoplasma gondii establishes a moving junction that selectively excludes host cell plasma membrane proteins on the basis of their membrane anchoring J. Exp. Med. 190 1999 1783 1792
    • (1999) J. Exp. Med. , vol.190 , pp. 1783-1792
    • Mordue, D.G.1
  • 17
    • 0031278412 scopus 로고    scopus 로고
    • Intracellular fate of vacuoles containing Toxoplasma gondii is determined at the time of formation and depends upon the mechanism of entry
    • D.G. Mordue, and L.D. Sibley Intracellular fate of vacuoles containing Toxoplasma gondii is determined at the time of formation and depends upon the mechanism of entry J. Immunol. 159 1997 4452 4459
    • (1997) J. Immunol. , vol.159 , pp. 4452-4459
    • Mordue, D.G.1    Sibley, L.D.2
  • 18
    • 0345151828 scopus 로고    scopus 로고
    • Toxoplasma gondii resides in a vacuole that avoids fusion with host cell endocytic and exocytic vesicular trafficking pathways
    • D.G. Mordue Toxoplasma gondii resides in a vacuole that avoids fusion with host cell endocytic and exocytic vesicular trafficking pathways Exp. Parasitol. 92 1999 87 99
    • (1999) Exp. Parasitol. , vol.92 , pp. 87-99
    • Mordue, D.G.1
  • 19
    • 0030956863 scopus 로고    scopus 로고
    • Sequential protein secretion from three distinct organelles of Toxoplasma gondii accompanies invasion of human fibroblasts
    • V.B. Carruthers, and L.D. Sibley Sequential protein secretion from three distinct organelles of Toxoplasma gondii accompanies invasion of human fibroblasts Eur. J. Cell Biol. 73 1997 114 123
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 114-123
    • Carruthers, V.B.1    Sibley, L.D.2
  • 20
    • 0038558167 scopus 로고    scopus 로고
    • Rapid invasion of host cells by Toxoplasma requires secretion of the MIC2-M2AP adhesive protein complex
    • M-H. Huynh Rapid invasion of host cells by Toxoplasma requires secretion of the MIC2-M2AP adhesive protein complex EMBO J. 22 2003 2082 2090
    • (2003) EMBO J. , vol.22 , pp. 2082-2090
    • Huynh, M.-H.1
  • 21
    • 0036855862 scopus 로고    scopus 로고
    • Cell signalling and Trypanosoma cruzi invasion
    • B.A. Burleigh, and A.M. Woolsey Cell signalling and Trypanosoma cruzi invasion Cell. Microbiol. 4 2002 701 711
    • (2002) Cell. Microbiol. , vol.4 , pp. 701-711
    • Burleigh, B.A.1    Woolsey, A.M.2
  • 22
    • 0033545999 scopus 로고    scopus 로고
    • 2+-dependent exocytosis of lysosomes and lysosome-mediated cell invasion by trypanosomes
    • 2+-dependent exocytosis of lysosomes and lysosome-mediated cell invasion by trypanosomes J. Biol. Chem. 274 1999 16754 16759
    • (1999) J. Biol. Chem. , vol.274 , pp. 16754-16759
    • Rodriguez, A.1
  • 23
    • 0025277577 scopus 로고
    • T. cruzi secreted protein immunologically related to the complement component C9: Evidence for membrane pore-forming activity at low pH
    • N.W. Andrews T. cruzi secreted protein immunologically related to the complement component C9: evidence for membrane pore-forming activity at low pH Cell 61 1990 1277 1287
    • (1990) Cell , vol.61 , pp. 1277-1287
    • Andrews, N.W.1
  • 24
    • 0026637237 scopus 로고
    • Desialylation of lysosomal membrane glycoproteins by Trypanosoma cruzi: A role for the surface neuraminidase in facilitating parasite entry into the host cell cytoplasm
    • B.F. Hall Desialylation of lysosomal membrane glycoproteins by Trypanosoma cruzi: a role for the surface neuraminidase in facilitating parasite entry into the host cell cytoplasm J. Exp. Med. 176 1992 313 325
    • (1992) J. Exp. Med. , vol.176 , pp. 313-325
    • Hall, B.F.1
  • 25
    • 0029131548 scopus 로고
    • Trypanosome invasion of mammalian cells requires activation of TGF-β signaling pathways
    • M. Ming Trypanosome invasion of mammalian cells requires activation of TGF-β signaling pathways Cell 82 1995 287 296
    • (1995) Cell , vol.82 , pp. 287-296
    • Ming, M.1
  • 26
    • 0036853070 scopus 로고    scopus 로고
    • Evasion of innate immunity by parasitic protozoa
    • D. Sacks, and A. Sher Evasion of innate immunity by parasitic protozoa Nat. Immunol. 3 2002 1041 1047
    • (2002) Nat. Immunol. , vol.3 , pp. 1041-1047
    • Sacks, D.1    Sher, A.2
  • 27
    • 0028158318 scopus 로고
    • + T cells during initiation of infection
    • + T cells during initiation of infection J. Exp. Med. 179 1994 447 456
    • (1994) J. Exp. Med. , vol.179 , pp. 447-456
    • Reiner, S.L.1
  • 28
    • 0029769511 scopus 로고    scopus 로고
    • Regulation of the expression of nitric oxide synthase and leishmanicidal activity by glycoconjugates of Leishmania lipophosphoglycan in murine macrophages
    • L. Proudfoot Regulation of the expression of nitric oxide synthase and leishmanicidal activity by glycoconjugates of Leishmania lipophosphoglycan in murine macrophages Proc. Natl. Acad. Sci. U. S. A. 93 1996 10984 10989
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 10984-10989
    • Proudfoot, L.1
  • 29
    • 0023122832 scopus 로고
    • Susceptibilities of macrophage populations to infection in vitro by Leishmania donovani
    • M. Olivier, and C.E. Tanner Susceptibilities of macrophage populations to infection in vitro by Leishmania donovani Infect. Immun. 55 1987 467 471
    • (1987) Infect. Immun. , vol.55 , pp. 467-471
    • Olivier, M.1    Tanner, C.E.2
  • 30
    • 0028089711 scopus 로고
    • Deficient expression of costimulatory molecules on Leishmania-infected macrophages
    • P.M. Kaye Deficient expression of costimulatory molecules on Leishmania-infected macrophages Eur. J. Immunol. 24 1994 2850 2854
    • (1994) Eur. J. Immunol. , vol.24 , pp. 2850-2854
    • Kaye, P.M.1
  • 31
    • 0023151617 scopus 로고
    • Parasite-accessory cell interactions in murine leishmaniasis. II. Leishmania donovani suppresses macrophage expression of class I and class II major histocompatibility complex gene products
    • N.E. Reiner Parasite-accessory cell interactions in murine leishmaniasis. II. Leishmania donovani suppresses macrophage expression of class I and class II major histocompatibility complex gene products J. Immunol. 138 1987 1926 1932
    • (1987) J. Immunol. , vol.138 , pp. 1926-1932
    • Reiner, N.E.1
  • 32
    • 0030021084 scopus 로고    scopus 로고
    • Leishmania promastigotes selectively inhibit interleukin 12 induction in bone marrow-derived macrophages from susceptible and resistant mice
    • L. Carrera Leishmania promastigotes selectively inhibit interleukin 12 induction in bone marrow-derived macrophages from susceptible and resistant mice J. Exp. Med. 183 1996 515 526
    • (1996) J. Exp. Med. , vol.183 , pp. 515-526
    • Carrera, L.1
  • 33
    • 0032921744 scopus 로고    scopus 로고
    • Regulation of macrophage IL-12 synthesis by Leishmania phosphoglycans
    • D. Piedrafita Regulation of macrophage IL-12 synthesis by Leishmania phosphoglycans Eur. J. Immunol. 29 1999 235 244
    • (1999) Eur. J. Immunol. , vol.29 , pp. 235-244
    • Piedrafita, D.1
  • 34
    • 0027284773 scopus 로고
    • Alteration of Leishmania donovani infection levels by selective impairment of macrophage signal transduction
    • K.J. Moore Alteration of Leishmania donovani infection levels by selective impairment of macrophage signal transduction J. Immunol. 150 1993 4457 4465
    • (1993) J. Immunol. , vol.150 , pp. 4457-4465
    • Moore, K.J.1
  • 35
    • 0026693720 scopus 로고
    • Defective stimulus-response coupling in human monocytes infected with Leishmania donovani is associated with altered activation and translocation of protein kinase C
    • M. Olivier Defective stimulus-response coupling in human monocytes infected with Leishmania donovani is associated with altered activation and translocation of protein kinase C Proc. Natl. Acad. Sci. U. S. A. 89 1992 7481 7485
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 7481-7485
    • Olivier, M.1
  • 36
    • 0026673841 scopus 로고
    • Inhibition of macrophage protein kinase C-mediated protein phosphorylation by Leishmania donovani lipophosphoglycan
    • A. Descoteaux Inhibition of macrophage protein kinase C-mediated protein phosphorylation by Leishmania donovani lipophosphoglycan J. Immunol. 149 1992 3008 3015
    • (1992) J. Immunol. , vol.149 , pp. 3008-3015
    • Descoteaux, A.1
  • 37
    • 0028827229 scopus 로고
    • Attenuation of gamma interferon-induced tyrosine phoshporylation in mononuclear phagocytes infected with Leishmania donovani: Selective inhibition of signaling through Janus kinases and Stat1
    • D. Nandan, and S.L. Reiner Attenuation of gamma interferon-induced tyrosine phoshporylation in mononuclear phagocytes infected with Leishmania donovani: selective inhibition of signaling through Janus kinases and Stat1 Infect. Immun. 63 1995 4495 4500
    • (1995) Infect. Immun. , vol.63 , pp. 4495-4500
    • Nandan, D.1    Reiner, S.L.2
  • 38
    • 0032577457 scopus 로고    scopus 로고
    • Modulation of interferon-γ-induced macrophage activation by phosphotyrosine phosphatase inhibition
    • M. Olivier Modulation of interferon-γ-induced macrophage activation by phosphotyrosine phosphatase inhibition J. Biol. Chem. 273 1998 13944 13949
    • (1998) J. Biol. Chem. , vol.273 , pp. 13944-13949
    • Olivier, M.1
  • 39
    • 0032744175 scopus 로고    scopus 로고
    • Leishmania-induced increases in activation of macrophage SHP-1 tyrosine phosphatase are associated with impaired IFN-γ-triggered JAK2 activation
    • J. Blanchette Leishmania-induced increases in activation of macrophage SHP-1 tyrosine phosphatase are associated with impaired IFN-γ-triggered JAK2 activation Eur. J. Immunol. 29 1999 3737 3744
    • (1999) Eur. J. Immunol. , vol.29 , pp. 3737-3744
    • Blanchette, J.1
  • 40
    • 0037146607 scopus 로고    scopus 로고
    • Leishmania EF-1α activates the Src homology 2 domain containing tyrosine phosphatase SHP-1 leading to macrophage deactivation
    • D. Nandan Leishmania EF-1α activates the Src homology 2 domain containing tyrosine phosphatase SHP-1 leading to macrophage deactivation J. Biol. Chem. 277 2002 50190 50197
    • (2002) J. Biol. Chem. , vol.277 , pp. 50190-50197
    • Nandan, D.1
  • 41
    • 0035184717 scopus 로고    scopus 로고
    • Role of host phosphotyrosine phosphatase SHP-1 in the development of murine leishmaniasis
    • G. Forget Role of host phosphotyrosine phosphatase SHP-1 in the development of murine leishmaniasis Eur. J. Immunol. 31 2001 3185 3196
    • (2001) Eur. J. Immunol. , vol.31 , pp. 3185-3196
    • Forget, G.1
  • 42
    • 0032740614 scopus 로고    scopus 로고
    • Extracellular signal-related kinase (ERK) and p38 mitogen-activated protein (MAP) kinases differentially regulate the lipopolysaccharide-mediated induction of inducible nitric oxide synthase and IL-12 in macrophages: Leishmania phosphoglycans subvert macrophage IL-12 production by targeting ERK MAP kinase
    • G.J. Feng Extracellular signal-related kinase (ERK) and p38 mitogen-activated protein (MAP) kinases differentially regulate the lipopolysaccharide-mediated induction of inducible nitric oxide synthase and IL-12 in macrophages: Leishmania phosphoglycans subvert macrophage IL-12 production by targeting ERK MAP kinase J. Immunol. 163 1999 6403 6412
    • (1999) J. Immunol. , vol.163 , pp. 6403-6412
    • Feng, G.J.1
  • 43
    • 0033847256 scopus 로고    scopus 로고
    • Leishmania donovani promastigotes evade the activation of mitogen-activated protein kinases p38, c-Jun N-terminal kinase, and extracellular signal-regulated kinase-1/2 during infection of naive macrophages
    • C. Prive, and A. Descoteaux Leishmania donovani promastigotes evade the activation of mitogen-activated protein kinases p38, c-Jun N-terminal kinase, and extracellular signal-regulated kinase-1/2 during infection of naive macrophages Eur. J. Immunol. 30 2000 2235 2244
    • (2000) Eur. J. Immunol. , vol.30 , pp. 2235-2244
    • Prive, C.1    Descoteaux, A.2
  • 44
    • 0030980385 scopus 로고    scopus 로고
    • Regulation of interleukin-12 by complement receptor 3 signaling
    • T. Marth, and B.L. Kelsall Regulation of interleukin-12 by complement receptor 3 signaling J. Exp. Med. 185 1997 1987 1995
    • (1997) J. Exp. Med. , vol.185 , pp. 1987-1995
    • Marth, T.1    Kelsall, B.L.2
  • 45
    • 0035313284 scopus 로고    scopus 로고
    • Suppression of IL-12 transcription in macrophages following Fcγ receptor ligation
    • M.G. Cappiello Suppression of IL-12 transcription in macrophages following Fcγ receptor ligation J. Immunol. 166 2001 4498 4506
    • (2001) J. Immunol. , vol.166 , pp. 4498-4506
    • Cappiello, M.G.1
  • 46
    • 0031570514 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored mucin-like glycoproteins isolated from Trypanosoma cruzi trypomastigotes initiate the synthesis of proinflammatory cytokines by macrophages
    • M.M. Camargo Glycosylphosphatidylinositol-anchored mucin-like glycoproteins isolated from Trypanosoma cruzi trypomastigotes initiate the synthesis of proinflammatory cytokines by macrophages J. Immunol. 158 1997 5890 5901
    • (1997) J. Immunol. , vol.158 , pp. 5890-5901
    • Camargo, M.M.1
  • 47
    • 0033902040 scopus 로고    scopus 로고
    • Signaling of immune system cells by glycosylphosphatidylinositol (GPI) anchor and related structures derived from parasitic protozoa
    • C. Ropert, and R.T. Gazzinelli Signaling of immune system cells by glycosylphosphatidylinositol (GPI) anchor and related structures derived from parasitic protozoa Curr. Opin. Microbiol. 3 2000 395 403
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 395-403
    • Ropert, C.1    Gazzinelli, R.T.2
  • 48
    • 0035399862 scopus 로고    scopus 로고
    • Activation of Toll-like receptor-2 by glycosylphosphatidylinositol anchors from a protozoan parasite
    • M.A.S. Campos Activation of Toll-like receptor-2 by glycosylphosphatidylinositol anchors from a protozoan parasite J. Immunol. 167 2001 416 423
    • (2001) J. Immunol. , vol.167 , pp. 416-423
    • Campos, M.A.S.1
  • 49
    • 0242271833 scopus 로고    scopus 로고
    • MyD88 is essential for clearance of Leishmania major: Possible role for lipophosphoglycan and Toll-like receptor 2 signaling
    • M.J. de Veer MyD88 is essential for clearance of Leishmania major: possible role for lipophosphoglycan and Toll-like receptor 2 signaling Eur. J. Immunol. 33 2003 2822 2831
    • (2003) Eur. J. Immunol. , vol.33 , pp. 2822-2831
    • De Veer, M.J.1
  • 50
    • 2442666530 scopus 로고    scopus 로고
    • Toxoplasma gondii triggers MyD88-dependent and CCL2(MCP-1) responses using distinct parasite molecules and host receptors
    • L. Del Rio Toxoplasma gondii triggers MyD88-dependent and CCL2(MCP-1) responses using distinct parasite molecules and host receptors J. Immunol. 172 2004 6954 6960
    • (2004) J. Immunol. , vol.172 , pp. 6954-6960
    • Del Rio, L.1
  • 51
    • 0034043956 scopus 로고    scopus 로고
    • Inhibition of lipopolysaccharide-induced signal transduction in endotoxin-tolerized mouse macrophages: Dysregulation of cytokine, chemokine, and toll-like receptor 2 and 4 gene expression
    • A.E. Medvedev Inhibition of lipopolysaccharide-induced signal transduction in endotoxin-tolerized mouse macrophages: dysregulation of cytokine, chemokine, and toll-like receptor 2 and 4 gene expression J. Immunol. 164 2000 5564 5574
    • (2000) J. Immunol. , vol.164 , pp. 5564-5574
    • Medvedev, A.E.1
  • 52
    • 0042346123 scopus 로고    scopus 로고
    • Inhibition of a p38/stress-activated protein kinase-2-dependent phosphatase restores function of IL-1 receptor-associated kinase-1 and reverses Toll-like receptor 2- and 4-dependent tolerance in macrophages
    • C. Ropert Inhibition of a p38/stress-activated protein kinase-2-dependent phosphatase restores function of IL-1 receptor-associated kinase-1 and reverses Toll-like receptor 2- and 4-dependent tolerance in macrophages J. Immunol. 171 2003 1456 1465
    • (2003) J. Immunol. , vol.171 , pp. 1456-1465
    • Ropert, C.1
  • 53
    • 0035284834 scopus 로고    scopus 로고
    • Requirement of mitogen-activated protein kinases and IκB phosphorylation for induction of proinflammatory cytokine synthesis by macrophages indicates functional similarity of receptors triggered by glycosylphosphatidylinositol anchors from parasitic protozoa and bacterial lipopolysaccharide
    • C. Ropert Requirement of mitogen-activated protein kinases and IκB phosphorylation for induction of proinflammatory cytokine synthesis by macrophages indicates functional similarity of receptors triggered by glycosylphosphatidylinositol anchors from parasitic protozoa and bacterial lipopolysaccharide J. Immunol. 166 2001 3423 3431
    • (2001) J. Immunol. , vol.166 , pp. 3423-3431
    • Ropert, C.1
  • 54
    • 0042520922 scopus 로고    scopus 로고
    • Induction and regulation of IL-12-dependent host resistance to Toxoplasma gondii
    • A. Sher Induction and regulation of IL-12-dependent host resistance to Toxoplasma gondii Immunol. Res. 27 2003 521 528
    • (2003) Immunol. Res. , vol.27 , pp. 521-528
    • Sher, A.1
  • 55
    • 0031736936 scopus 로고    scopus 로고
    • Regulation and function of T cell-mediated immunity during Toxoplasma gondii infection
    • E.Y. Denkers, and R.T. Gazzinelli Regulation and function of T cell-mediated immunity during Toxoplasma gondii infection Clin. Microbiol. Rev. 11 1998 569 588
    • (1998) Clin. Microbiol. Rev. , vol.11 , pp. 569-588
    • Denkers, E.Y.1    Gazzinelli, R.T.2
  • 56
    • 0035881856 scopus 로고    scopus 로고
    • Toxoplasma gondii tachyzoites inhibit proinflammatory cytokine induction in infected macrophages by preventing nuclear translocation of the transcription factor NFκB
    • B.A. Butcher Toxoplasma gondii tachyzoites inhibit proinflammatory cytokine induction in infected macrophages by preventing nuclear translocation of the transcription factor NFκB J. Immunol. 167 2001 2193 2201
    • (2001) J. Immunol. , vol.167 , pp. 2193-2201
    • Butcher, B.A.1
  • 57
    • 0036716776 scopus 로고    scopus 로고
    • Mechanism of entry determines ability of Toxoplasma gondii to inhibit macrophage proinflammatory cytokine production
    • B.A. Butcher, and E.Y. Denkers Mechanism of entry determines ability of Toxoplasma gondii to inhibit macrophage proinflammatory cytokine production Infect. Immun. 70 2002 5216 5224
    • (2002) Infect. Immun. , vol.70 , pp. 5216-5224
    • Butcher, B.A.1    Denkers, E.Y.2
  • 58
    • 0038643779 scopus 로고    scopus 로고
    • Reduced expression of the inducible nitric oxide synthase after infection with Toxoplasma gondii facilitates parasite replication in activated murine macrophages
    • C.G.K. Luder Reduced expression of the inducible nitric oxide synthase after infection with Toxoplasma gondii facilitates parasite replication in activated murine macrophages Int. J. Parasitol. 33 2003 833 844
    • (2003) Int. J. Parasitol. , vol.33 , pp. 833-844
    • Luder, C.G.K.1
  • 59
    • 0031782098 scopus 로고    scopus 로고
    • Down-regulation of MHC class II molecules and inability to up-regulate class I molecules in murine macrophages after infection with Toxoplasma gondii
    • C.G.K. Luder Down-regulation of MHC class II molecules and inability to up-regulate class I molecules in murine macrophages after infection with Toxoplasma gondii Clin. Exp. Immunol. 112 1998 308 316
    • (1998) Clin. Exp. Immunol. , vol.112 , pp. 308-316
    • Luder, C.G.K.1
  • 60
    • 0026529405 scopus 로고
    • IL-10 inhibits parasite killing and nitrogen oxide production by IFN-γ-activated macrophages
    • R.T. Gazzinelli IL-10 inhibits parasite killing and nitrogen oxide production by IFN-γ-activated macrophages J. Immunol. 148 1992 1792 1796
    • (1992) J. Immunol. , vol.148 , pp. 1792-1796
    • Gazzinelli, R.T.1
  • 61
    • 0026091204 scopus 로고
    • Tumor necrosis factor-α triggers antitoxoplasmal activity in IFN-γ primed macrophages
    • L.D. Sibley Tumor necrosis factor-α triggers antitoxoplasmal activity in IFN-γ primed macrophages J. Immunol. 147 1991 2340 2345
    • (1991) J. Immunol. , vol.147 , pp. 2340-2345
    • Sibley, L.D.1
  • 62
    • 0037083252 scopus 로고    scopus 로고
    • Suppression of NF-κB activation by infection with Toxoplasma gondii
    • S.S. Shapira Suppression of NF-κB activation by infection with Toxoplasma gondii J. Infect. Dis. 185 2002 S66 S72
    • (2002) J. Infect. Dis. , vol.185
    • Shapira, S.S.1
  • 63
    • 1342324679 scopus 로고    scopus 로고
    • Toxoplasma gondii interferes with lipopolysaccharide-induced mitogen-activated protein kinase activation by mechanisms distinct from endotoxin tolerance
    • L. Kim Toxoplasma gondii interferes with lipopolysaccharide-induced mitogen-activated protein kinase activation by mechanisms distinct from endotoxin tolerance J. Immunol. 172 2004 3003 3010
    • (2004) J. Immunol. , vol.172 , pp. 3003-3010
    • Kim, L.1
  • 64
    • 0343867201 scopus 로고    scopus 로고
    • Toxoplasma gondii down-regulates MHC class II gene expression and antigen presentation by murine macrophages via interference with nuclear translocation of STAT1α
    • C.G.K. Luder Toxoplasma gondii down-regulates MHC class II gene expression and antigen presentation by murine macrophages via interference with nuclear translocation of STAT1α Eur. J. Immunol. 31 2001 1475 1484
    • (2001) Eur. J. Immunol. , vol.31 , pp. 1475-1484
    • Luder, C.G.K.1
  • 65
    • 0034824828 scopus 로고    scopus 로고
    • Toxoplasma gondii and MHC-restricted antigen presentation: On degradation, transport and modulation
    • C.G.K. Luder, and F. Seeber Toxoplasma gondii and MHC-restricted antigen presentation: on degradation, transport and modulation Int. J. Parasitol. 31 2001 1355 1369
    • (2001) Int. J. Parasitol. , vol.31 , pp. 1355-1369
    • Luder, C.G.K.1    Seeber, F.2
  • 66
    • 17144447300 scopus 로고    scopus 로고
    • Activation of the cellular mitogen-activated protein kinase pathways ERK, p38 and JNK during Toxoplasma gondii invasion
    • A. Valere Activation of the cellular mitogen-activated protein kinase pathways ERK, p38 and JNK during Toxoplasma gondii invasion Parasite 10 2003 59 64
    • (2003) Parasite , vol.10 , pp. 59-64
    • Valere, A.1
  • 67
    • 0034766428 scopus 로고    scopus 로고
    • Inhibition of host cell apoptosis by Toxoplasma gondii is accompanied by reduced activation of the caspase cascade and alterations of poly(ADP-ribose) polymerase activation
    • S.G. Goebel Inhibition of host cell apoptosis by Toxoplasma gondii is accompanied by reduced activation of the caspase cascade and alterations of poly(ADP-ribose) polymerase activation J. Cell Sci. 114 2001 3495 3505
    • (2001) J. Cell Sci. , vol.114 , pp. 3495-3505
    • Goebel, S.G.1
  • 68
    • 0032519416 scopus 로고    scopus 로고
    • Toxoplasma gondii-infected cells are resistant to multiple inducers of apoptosis
    • P.B. Nash Toxoplasma gondii-infected cells are resistant to multiple inducers of apoptosis J. Immunol. 160 1998 1824 1830
    • (1998) J. Immunol. , vol.160 , pp. 1824-1830
    • Nash, P.B.1
  • 69
    • 2442560408 scopus 로고    scopus 로고
    • Manipulation of apoptosis in the host-parasite interaction
    • E.R. James, and D.R. Green Manipulation of apoptosis in the host-parasite interaction Trends Parasitol. 20 2004 280 287
    • (2004) Trends Parasitol. , vol.20 , pp. 280-287
    • James, E.R.1    Green, D.R.2
  • 70
    • 0028294578 scopus 로고
    • Intracellular infection by Leishmania donovani inhibits macrophage apoptosis
    • K.J. Moore, and G. Matlashewski Intracellular infection by Leishmania donovani inhibits macrophage apoptosis J. Immunol. 152 1994 2930 2937
    • (1994) J. Immunol. , vol.152 , pp. 2930-2937
    • Moore, K.J.1    Matlashewski, G.2
  • 71
    • 0034601110 scopus 로고    scopus 로고
    • Inhibition of Fas-mediated apoptosis by Trypanosoma cruzi infection
    • J. Nakajima-Shimada Inhibition of Fas-mediated apoptosis by Trypanosoma cruzi infection Biochim. Biophys. Acta 1475 2000 175 183
    • (2000) Biochim. Biophys. Acta , vol.1475 , pp. 175-183
    • Nakajima-Shimada, J.1
  • 72
    • 0242407708 scopus 로고    scopus 로고
    • Activation of NF-κB by Toxoplasma gondii correlates with increased expression of antiapoptotic genes and localization of phosphorylated IκB to the parasitophorous vacuole membrane
    • R.E. Molestina Activation of NF-κB by Toxoplasma gondii correlates with increased expression of antiapoptotic genes and localization of phosphorylated IκB to the parasitophorous vacuole membrane J. Cell Sci. 116 2003 4359 4371
    • (2003) J. Cell Sci. , vol.116 , pp. 4359-4371
    • Molestina, R.E.1
  • 73
    • 0141532262 scopus 로고    scopus 로고
    • Toll-like receptor signaling
    • S. Akira Toll-like receptor signaling J. Biol. Chem. 278 2003 38105 38108
    • (2003) J. Biol. Chem. , vol.278 , pp. 38105-38108
    • Akira, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.