메뉴 건너뛰기




Volumn 14, Issue 2, 2014, Pages 109-121

Innate immunity to Toxoplasma gondii infection

Author keywords

[No Author keywords available]

Indexed keywords

CD8 ANTIGEN; GAMMA INTERFERON; INDOLEAMINE 2,3 DIOXYGENASE; INFLAMMASOME; INTERLEUKIN 12; MYELOID DIFFERENTIATION FACTOR 88; NITROGEN OXIDE; REACTIVE OXYGEN METABOLITE; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 1; TOLL LIKE RECEPTOR 11; TOLL LIKE RECEPTOR 12; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 6; TOLL LIKE RECEPTOR 7; TOLL LIKE RECEPTOR 9; UNCLASSIFIED DRUG;

EID: 84893115383     PISSN: 14741733     EISSN: 14741741     Source Type: Journal    
DOI: 10.1038/nri3598     Document Type: Review
Times cited : (342)

References (156)
  • 1
    • 77956252678 scopus 로고    scopus 로고
    • Regulation of CD8+ T cell responses to infection with parasitic protozoa
    • Jordan, K. A. and Hunter, C. A. Regulation of CD8+ T cell responses to infection with parasitic protozoa. Exp. Parasitol. 126, 318-325 (2010).
    • (2010) Exp. Parasitol. , vol.126 , pp. 318-325
    • Jordan, K.A.1    Hunter, C.A.2
  • 2
    • 33947134461 scopus 로고    scopus 로고
    • Cytokine regulation of immunopathology in toxoplasmosis
    • Gaddi, P. J. and Yap, G. S. Cytokine regulation of immunopathology in toxoplasmosis. Immunol. Cell Biol. 85, 155-159 (2007).
    • (2007) Immunol. Cell Biol. , vol.85 , pp. 155-159
    • Gaddi, P.J.1    Yap, G.S.2
  • 3
    • 0032718790 scopus 로고    scopus 로고
    • T lymphocyte-dependent effector mechanisms of immunity to Toxoplasma gondii
    • Denkers, E. Y. T lymphocyte-dependent effector mechanisms of immunity to Toxoplasma gondii. Microbes Infect. 1, 699-708 (1999).
    • (1999) Microbes Infect. , vol.1 , pp. 699-708
    • Denkers, E.Y.1
  • 4
    • 84867751254 scopus 로고    scopus 로고
    • Modulation of innate immunity by Toxoplasma gondii virulence effectors
    • Hunter, C. A. and Sibley, L. D. Modulation of innate immunity by Toxoplasma gondii virulence effectors. Nature Rev. Microbiol. 10, 766-778 (2012).
    • (2012) Nature Rev. Microbiol. , vol.10 , pp. 766-778
    • Hunter, C.A.1    Sibley, L.D.2
  • 5
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi, O. and Akira, S. Pattern recognition receptors and inflammation. Cell 140, 805-820 (2010).
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 6
    • 20644433342 scopus 로고    scopus 로고
    • TLR11 activation of dendritic cells by a protozoan profilin-like protein
    • Yarovinsky, F. et al. TLR11 activation of dendritic cells by a protozoan profilin-like protein. Science 308, 1626-1629 (2005).
    • (2005) Science , vol.308 , pp. 1626-1629
    • Yarovinsky, F.1
  • 7
    • 38849095132 scopus 로고    scopus 로고
    • Toxoplasma profilin is essential for host cell invasion and TLR11-dependent induction of an interleukin-12 response
    • Plattner, F. et al. Toxoplasma profilin is essential for host cell invasion and TLR11-dependent induction of an interleukin-12 response. Cell Host Microbe 3, 77-87 (2008).
    • (2008) Cell Host Microbe , vol.3 , pp. 77-87
    • Plattner, F.1
  • 8
    • 0035399862 scopus 로고    scopus 로고
    • Activation of Toll-like receptor-2 by glycosylphosphatidylinositol anchors from a protozoan parasite
    • Campos, M. A. et al. Activation of Toll-like receptor-2 by glycosylphosphatidylinositol anchors from a protozoan parasite. J. Immunol. 167, 416-423 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 416-423
    • Campos, M.A.1
  • 9
    • 34548752958 scopus 로고    scopus 로고
    • Activation of TLR2 and TLR4 by glycosylphosphatidylinositols derived from Toxoplasma gondii
    • Debierre-Grockiego, F. et al. Activation of TLR2 and TLR4 by glycosylphosphatidylinositols derived from Toxoplasma gondii. J. Immunol. 179, 1129-1137 (2007).
    • (2007) J. Immunol. , vol.179 , pp. 1129-1137
    • Debierre-Grockiego, F.1
  • 10
    • 68349131303 scopus 로고    scopus 로고
    • Gut commensal bacteria direct a protective immune response against Toxoplasma gondii
    • Benson, A., Pifer, R., Behrendt, C. L., Hooper, L. V. and Yarovinsky, F. Gut commensal bacteria direct a protective immune response against Toxoplasma gondii. Cell Host Microbe 6, 187-196 (2009).
    • (2009) Cell Host Microbe , vol.6 , pp. 187-196
    • Benson, A.1    Pifer, R.2    Behrendt, C.L.3    Hooper, L.V.4    Yarovinsky, F.5
  • 11
    • 0037097795 scopus 로고    scopus 로고
    • Cutting edge: MyD88 is required for resistance to Toxoplasma gondii infection and regulates parasite-induced IL-12 production by dendritic cells
    • Scanga, C. A. et al. Cutting edge: MyD88 is required for resistance to Toxoplasma gondii infection and regulates parasite-induced IL-12 production by dendritic cells. J. Immunol. 168, 5997-6001 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 5997-6001
    • Scanga, C.A.1
  • 12
    • 0036199625 scopus 로고    scopus 로고
    • In the absence of IL-12, CD4+ T cell responses to intracellular pathogens fail to default to a TH2 pattern and are host protective in an IL-10-/- setting
    • Jankovic, D. et al. In the absence of IL-12, CD4+ T cell responses to intracellular pathogens fail to default to a TH2 pattern and are host protective in an IL-10-/- setting. Immunity 16, 429-439 (2002).
    • (2002) Immunity , vol.16 , pp. 429-439
    • Jankovic, D.1
  • 13
    • 33748879305 scopus 로고    scopus 로고
    • Toll-like receptor recognition regulates immunodominance in an antimicrobial CD4+ T cell response
    • Yarovinsky, F., Kanzler, H., Hieny, S., Coffman, R. L. and Sher, A. Toll-like receptor recognition regulates immunodominance in an antimicrobial CD4+ T cell response. Immunity 25, 655-664 (2006).
    • (2006) Immunity , vol.25 , pp. 655-664
    • Yarovinsky, F.1    Kanzler, H.2    Hieny, S.3    Coffman, R.L.4    Sher, A.5
  • 14
    • 78651101742 scopus 로고    scopus 로고
    • Critical coordination of innate immune defense against Toxoplasma gondii by dendritic cells responding via their Toll-like receptors
    • Hou, B., Benson, A., Kuzmich, L., DeFranco, A. L. and Yarovinsky, F. Critical coordination of innate immune defense against Toxoplasma gondii by dendritic cells responding via their Toll-like receptors. Proc. Natl Acad. Sci. USA 108, 278-283 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 278-283
    • Hou, B.1    Benson, A.2    Kuzmich, L.3    Defranco, A.L.4    Yarovinsky, F.5
  • 15
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Spring Harb. Symp. Quant. Biol
    • Janeway, C. A. Jr. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb. Symp. Quant. Biol. 1, 1-13 (1989).
    • (1989) Cold , vol.1 , pp. 1-13
    • Janeway Jr., C.A.1
  • 16
    • 79952789527 scopus 로고    scopus 로고
    • UNC93B1 is essential for TLR11 activation and IL-12-dependent host resistance to Toxoplasma gondii
    • Pifer, R., Benson, A., Sturge, C. R. and Yarovinsky, F. UNC93B1 is essential for TLR11 activation and IL-12-dependent host resistance to Toxoplasma gondii. J. Biol. Chem. 286, 3307-3314 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 3307-3314
    • Pifer, R.1    Benson, A.2    Sturge, C.R.3    Yarovinsky, F.4
  • 17
    • 80051765668 scopus 로고    scopus 로고
    • Innate responses to Toxoplasma gondii in mice and humans
    • Pifer, R. and Yarovinsky, F. Innate responses to Toxoplasma gondii in mice and humans. Trends Parasitol. 27, 388-393 (2011).
    • (2011) Trends Parasitol , vol.27 , pp. 388-393
    • Pifer, R.1    Yarovinsky, F.2
  • 18
    • 84886041693 scopus 로고    scopus 로고
    • Cooperation of TLR12 and TLR11 in the IRF8-dependent IL-12 response to Toxoplasma gondii profilin
    • Raetz, M. et al. Cooperation of TLR12 and TLR11 in the IRF8-dependent IL-12 response to Toxoplasma gondii profilin. J. Immunol. 191, 4818-4827 (2013).
    • (2013) J. Immunol. , vol.191 , pp. 4818-4827
    • Raetz, M.1
  • 19
    • 84872761427 scopus 로고    scopus 로고
    • Recognition of profilin by Toll-like receptor 12 is critical for host resistance to Toxoplasma gondii
    • Koblansky, A. A. et al. Recognition of profilin by Toll-like receptor 12 is critical for host resistance to Toxoplasma gondii. Immunity 38, 119-130 (2013).
    • (2013) Immunity , vol.38 , pp. 119-130
    • Koblansky, A.A.1
  • 20
    • 84872596639 scopus 로고    scopus 로고
    • Combined action of nucleic acid-sensing Toll-like receptors and TLR11/TLR12 heterodimers imparts resistance to Toxoplasma gondii in mice
    • Andrade, W. A. et al. Combined action of nucleic acid-sensing Toll-like receptors and TLR11/TLR12 heterodimers imparts resistance to Toxoplasma gondii in mice. Cell Host Microbe 13, 42-53 (2013).
    • (2013) Cell Host Microbe , vol.13 , pp. 42-53
    • Andrade, W.A.1
  • 21
    • 44449151187 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells are activated by Toxoplasma gondii to present antigen and produce cytokines
    • Pepper, M. et al. Plasmacytoid dendritic cells are activated by Toxoplasma gondii to present antigen and produce cytokines. J. Immunol. 180, 6229-6236 (2008).
    • (2008) J. Immunol. , vol.180 , pp. 6229-6236
    • Pepper, M.1
  • 22
    • 77958144527 scopus 로고    scopus 로고
    • UNC93B1 mediates host resistance to infection with Toxoplasma gondii
    • Melo, M. B. et al. UNC93B1 mediates host resistance to infection with Toxoplasma gondii. PLoS Pathog. 6, 1001071 (2010).
    • (2010) PLoS Pathog , vol.6 , pp. 1001071
    • Melo, M.B.1
  • 23
    • 1542317550 scopus 로고    scopus 로고
    • Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA
    • Diebold, S. S., Kaisho, T., Hemmi, H., Akira, S. and Reis e Sousa, C. Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA. Science 303, 1529-1531 (2004).
    • (2004) Science , vol.303 , pp. 1529-1531
    • Diebold, S.S.1    Kaisho, T.2    Hemmi, H.3    Akira, S.4    Reis E Sousa, C.5
  • 24
    • 1542317578 scopus 로고    scopus 로고
    • Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8
    • Heil, F. et al. Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8. Science 303, 1526-1529 (2004).
    • (2004) Science , vol.303 , pp. 1526-1529
    • Heil, F.1
  • 25
    • 67349187318 scopus 로고    scopus 로고
    • Bacterial recognition by TLR7 in the lysosomes of conventional dendritic cells
    • Mancuso, G. et al. Bacterial recognition by TLR7 in the lysosomes of conventional dendritic cells. Nature Immunol. 10, 587-594 (2009).
    • (2009) Nature Immunol , vol.10 , pp. 587-594
    • Mancuso, G.1
  • 26
    • 33845579097 scopus 로고    scopus 로고
    • Nucleic acid agonists for Toll-like receptor 7 are defined by the presence of uridine ribonucleotides
    • Diebold, S. S. et al. Nucleic acid agonists for Toll-like receptor 7 are defined by the presence of uridine ribonucleotides. Eur. J. Immunol. 36, 3256-3267 (2006).
    • (2006) Eur. J. Immunol. , vol.36 , pp. 3256-3267
    • Diebold, S.S.1
  • 27
    • 33745168605 scopus 로고    scopus 로고
    • Autoreactive B cell responses to RNA-related antigens due to TLR7 gene duplication
    • Pisitkun, P. et al. Autoreactive B cell responses to RNA-related antigens due to TLR7 gene duplication. Science 312, 1669-1672 (2006).
    • (2006) Science , vol.312 , pp. 1669-1672
    • Pisitkun, P.1
  • 28
    • 0037738569 scopus 로고    scopus 로고
    • Toll-like receptor expression in murine DC subsets: Lack of TLR7 expression by CD8α+ DC correlates with unresponsiveness to imidazoquinolines
    • Edwards, A. D. et al. Toll-like receptor expression in murine DC subsets: lack of TLR7 expression by CD8α+ DC correlates with unresponsiveness to imidazoquinolines. Eur. J. Immunol. 33, 827-833 (2003).
    • (2003) Eur. J. Immunol. , vol.33 , pp. 827-833
    • Edwards, A.D.1
  • 29
    • 0000060327 scopus 로고    scopus 로고
    • In vivo microbial stimulation induces rapid CD40 ligand-independent production of interleukin 12 by dendritic cells and their redistribution to T cell areas
    • Reis e Sousa, C. et al. In vivo microbial stimulation induces rapid CD40 ligand-independent production of interleukin 12 by dendritic cells and their redistribution to T cell areas. J. Exp. Med. 186, 1819-1829 (1997).
    • (1997) J. Exp. Med. , vol.186 , pp. 1819-1829
    • Reis E Sousa, C.1
  • 30
    • 0034619794 scopus 로고    scopus 로고
    • A Toll-like receptor recognizes bacterial DNA
    • Hemmi, H. et al. A Toll-like receptor recognizes bacterial DNA. Nature 408, 740-745 (2000).
    • (2000) Nature , vol.408 , pp. 740-745
    • Hemmi, H.1
  • 31
    • 40249088259 scopus 로고    scopus 로고
    • The DNA sugar backbone 2Ŷ deoxyribose determines toll-like receptor 9 activation
    • Haas, T. et al. The DNA sugar backbone 2Ŷ deoxyribose determines toll-like receptor 9 activation. Immunity 28, 315-323 (2008).
    • (2008) Immunity , vol.28 , pp. 315-323
    • Haas, T.1
  • 32
    • 0037061453 scopus 로고    scopus 로고
    • Chromatin-IgG complexes activate B cells by dual engagement of IgM and Toll-like receptors
    • Leadbetter, E. A. et al. Chromatin-IgG complexes activate B cells by dual engagement of IgM and Toll-like receptors. Nature 416, 603-607 (2002).
    • (2002) Nature , vol.416 , pp. 603-607
    • Leadbetter, E.A.1
  • 33
    • 22944490869 scopus 로고    scopus 로고
    • Toll-like receptor 9 controls anti-DNA autoantibody production in murine lupus
    • Christensen, S. R. et al. Toll-like receptor 9 controls anti-DNA autoantibody production in murine lupus. J. Exp. Med. 202, 321-331 (2005).
    • (2005) J. Exp. Med. , vol.202 , pp. 321-331
    • Christensen, S.R.1
  • 34
    • 40949110918 scopus 로고    scopus 로고
    • Toxoplasma gondii and Cryptosporidium parvum lack detectable DNA cytosine methylation
    • Gissot, M., Choi, S. W., Thompson, R. F., Greally, J. M. and Kim, K. Toxoplasma gondii and Cryptosporidium parvum lack detectable DNA cytosine methylation. Eukaryot. Cell 7, 537-540 (2008).
    • (2008) Eukaryot. Cell , vol.7 , pp. 537-540
    • Gissot, M.1    Choi, S.W.2    Thompson, R.F.3    Greally, J.M.4    Kim, K.5
  • 35
    • 19944430901 scopus 로고    scopus 로고
    • Toll-like receptor 9 mediates innate immune activation by the malaria pigment hemozoin
    • Coban, C. et al. Toll-like receptor 9 mediates innate immune activation by the malaria pigment hemozoin. J. Exp. Med. 201, 19-25 (2005).
    • (2005) J. Exp. Med. , vol.201 , pp. 19-25
    • Coban, C.1
  • 36
    • 33846911691 scopus 로고    scopus 로고
    • Malaria hemozoin is immunologically inert but radically enhances innate responses by presenting malaria DNA to Toll-like receptor 9
    • Parroche, P. et al. Malaria hemozoin is immunologically inert but radically enhances innate responses by presenting malaria DNA to Toll-like receptor 9. Proc. Natl Acad. Sci. USA 104, 1919-1924 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 1919-1924
    • Parroche, P.1
  • 37
    • 53349164200 scopus 로고    scopus 로고
    • Commensal DNA limits regulatory T cell conversion and is a natural adjuvant of intestinal immune responses
    • Hall, J. A. et al. Commensal DNA limits regulatory T cell conversion and is a natural adjuvant of intestinal immune responses. Immunity 29, 637-649 (2008).
    • (2008) Immunity , vol.29 , pp. 637-649
    • Hall, J.A.1
  • 38
    • 84866058423 scopus 로고    scopus 로고
    • TLR9 is important for protection against intestinal damage and for intestinal repair
    • Rose, W. A., Sakamoto, K. and Leifer, C. A. TLR9 is important for protection against intestinal damage and for intestinal repair. Sci. Rep. 2, 14 (2012).
    • (2012) Sci. Rep. , vol.2 , pp. 14
    • Rose, W.A.1    Sakamoto, K.2    Leifer, C.A.3
  • 39
    • 84864830852 scopus 로고    scopus 로고
    • Insights into inflammatory bowel disease using Toxoplasma gondii as an infectious trigger
    • Egan, C. E., Cohen, S. B. and Denkers, E. Y. Insights into inflammatory bowel disease using Toxoplasma gondii as an infectious trigger. Immunol. Cell Biol. 90, 668-675 (2012).
    • (2012) Immunol. Cell Biol. , vol.90 , pp. 668-675
    • Egan, C.E.1    Cohen, S.B.2    Denkers, E.Y.3
  • 40
    • 1642525756 scopus 로고    scopus 로고
    • Impaired production of proinflammatory cytokines and host resistance to acute infection with Trypanosoma cruzi in mice lacking functional myeloid differentiation factor 88
    • Campos, M. A. et al. Impaired production of proinflammatory cytokines and host resistance to acute infection with Trypanosoma cruzi in mice lacking functional myeloid differentiation factor 88. J. Immunol. 172, 1711-1718 (2004).
    • (2004) J. Immunol. , vol.172 , pp. 1711-1718
    • Campos, M.A.1
  • 41
    • 14844337835 scopus 로고    scopus 로고
    • Induction of proinflammatory responses in macrophages by the glycosylphosphatidylinositols of Plasmodium falciparum: Cell signaling receptors, glycosylphosphatidylinositol (GPI) structural requirement, and regulation of GPI activity
    • Krishnegowda, G. et al. Induction of proinflammatory responses in macrophages by the glycosylphosphatidylinositols of Plasmodium falciparum: cell signaling receptors, glycosylphosphatidylinositol (GPI) structural requirement, and regulation of GPI activity. J. Biol. Chem. 280, 8606-8616 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 8606-8616
    • Krishnegowda, G.1
  • 42
    • 2442666530 scopus 로고    scopus 로고
    • Toxoplasma gondii triggers myeloid differentiation factor 88-dependent IL-12 and chemokine ligand 2 (monocyte chemoattractant protein 1) responses using distinct parasite molecules and host receptors
    • Del Rio, L. et al. Toxoplasma gondii triggers myeloid differentiation factor 88-dependent IL-12 and chemokine ligand 2 (monocyte chemoattractant protein 1) responses using distinct parasite molecules and host receptors. J. Immunol. 172, 6954-6960 (2004).
    • (2004) J. Immunol. , vol.172 , pp. 6954-6960
    • Del Rio, L.1
  • 43
    • 0025058401 scopus 로고
    • Role of TNF and IL-1 in infections with Toxoplasma gondii
    • Chang, H. R., Grau, G. E. and Pechere, J. C. Role of TNF and IL-1 in infections with Toxoplasma gondii. Immunology 69, 33-37 (1990).
    • (1990) Immunology , vol.69 , pp. 33-37
    • Chang, H.R.1    Grau, G.E.2    Pechere, J.C.3
  • 44
    • 0026091204 scopus 로고
    • Tumor necrosis factor-α triggers antitoxoplasmal activity of IFN-γ primed macrophages
    • Sibley, L. D., Adams, L. B., Fukutomi, Y. and Krahenbuhl, J. L. Tumor necrosis factor-α triggers antitoxoplasmal activity of IFN-γ primed macrophages. J. Immunol. 147, 2340-2345 (1991).
    • (1991) J. Immunol. , vol.147 , pp. 2340-2345
    • Sibley, L.D.1    Adams, L.B.2    Fukutomi, Y.3    Krahenbuhl, J.L.4
  • 45
    • 0032055198 scopus 로고    scopus 로고
    • Crucial role of TNF receptor type 1 (p55), but not of TNF receptor type 2 (p75), in murine toxoplasmosis
    • Deckert-Schluter, M., Bluethmann, H., Rang, A., Hof, H. and Schluter, D. Crucial role of TNF receptor type 1 (p55), but not of TNF receptor type 2 (p75), in murine toxoplasmosis. J. Immunol. 160, 3427-3436 (1998).
    • (1998) J. Immunol. , vol.160 , pp. 3427-3436
    • Deckert-Schluter, M.1    Bluethmann, H.2    Rang, A.3    Hof, H.4    Schluter, D.5
  • 46
    • 0031940206 scopus 로고    scopus 로고
    • Decreased resistance of TNF receptor p55- and p75-deficient mice to chronic toxoplasmosis despite normal activation of inducible nitric oxide synthase in vivo
    • Yap, G. S., Scharton-Kersten, T., Charest, H. and Sher, A. Decreased resistance of TNF receptor p55- and p75-deficient mice to chronic toxoplasmosis despite normal activation of inducible nitric oxide synthase in vivo. J. Immunol. 160, 1340-1345 (1998).
    • (1998) J. Immunol. , vol.160 , pp. 1340-1345
    • Yap, G.S.1    Scharton-Kersten, T.2    Charest, H.3    Sher, A.4
  • 47
    • 0028973003 scopus 로고
    • IL-1β is required for IL-12 to induce production of IFNγ by NK cells. A role for IL-1β in the T cell-independent mechanism of resistance against intracellular pathogens
    • Hunter, C. A., Chizzonite, R. and Remington, J. S. IL-1β is required for IL-12 to induce production of IFNγ by NK cells. A role for IL-1β in the T cell-independent mechanism of resistance against intracellular pathogens. J. Immunol. 155, 4347-4354 (1995).
    • (1995) J. Immunol. , vol.155 , pp. 4347-4354
    • Hunter, C.A.1    Chizzonite, R.2    Remington, J.S.3
  • 48
    • 73349099711 scopus 로고    scopus 로고
    • Early response of mucosal epithelial cells during Toxoplasma gondii infection
    • Ju, C. H., Chockalingam, A. and Leifer, C. A. Early response of mucosal epithelial cells during Toxoplasma gondii infection. J. Immunol. 183, 7420-7427 (2009).
    • (2009) J. Immunol. , vol.183 , pp. 7420-7427
    • Ju, C.H.1    Chockalingam, A.2    Leifer, C.A.3
  • 49
    • 0042854698 scopus 로고    scopus 로고
    • TLR2 as an essential molecule for protective immunity against Toxoplasma gondii infection
    • Mun, H. S. et al. TLR2 as an essential molecule for protective immunity against Toxoplasma gondii infection. Int. Immunol. 15, 1081-1087 (2003).
    • (2003) Int. Immunol. , vol.15 , pp. 1081-1087
    • Mun, H.S.1
  • 50
    • 77954005130 scopus 로고    scopus 로고
    • Endogenous ligands of TLR2 and TLR4: Agonists or assistants?
    • Erridge, C. Endogenous ligands of TLR2 and TLR4: agonists or assistants? J. Leukoc. Biol. 87, 989-999 (2010).
    • (2010) J. Leukoc. Biol. , vol.87 , pp. 989-999
    • Erridge, C.1
  • 51
    • 0036784614 scopus 로고    scopus 로고
    • Cutting edge: Toll-like receptor (TLR)2- and TLR4-mediated pathogen recognition in resistance to airborne infection with Mycobacterium tuberculosis
    • Reiling, N. et al. Cutting edge: Toll-like receptor (TLR)2- and TLR4-mediated pathogen recognition in resistance to airborne infection with Mycobacterium tuberculosis. J. Immunol. 169, 3480-3484 (2002).
    • (2002) J. Immunol. , vol.169 , pp. 3480-3484
    • Reiling, N.1
  • 52
    • 77956546698 scopus 로고    scopus 로고
    • Immunological reactions in response to apicomplexan glycosylphosphatidylinositols
    • Debierre-Grockiego, F. and Schwarz, R. T. Immunological reactions in response to apicomplexan glycosylphosphatidylinositols. Glycobiology 20, 801-811 (2010).
    • (2010) Glycobiology , vol.20 , pp. 801-811
    • Debierre-Grockiego, F.1    Schwarz, R.T.2
  • 53
    • 79956110876 scopus 로고    scopus 로고
    • Proinflammatory responses by glycosylphosphatidyl-inositols (GPIs) of Plasmodium falciparum are mainly mediated through the recognition of TLR2/TLR1
    • Zhu, J., Krishnegowda, G., Li, G. and Gowda, D. C. Proinflammatory responses by glycosylphosphatidyl-inositols (GPIs) of Plasmodium falciparum are mainly mediated through the recognition of TLR2/TLR1. Exp. Parasitol. 128, 205-211 (2011).
    • (2011) Exp. Parasitol. , vol.128 , pp. 205-211
    • Zhu, J.1    Krishnegowda, G.2    Li, G.3    Gowda, D.C.4
  • 54
    • 23344436402 scopus 로고    scopus 로고
    • Toll-like receptor 4 mediates tolerance in macrophages stimulated with Toxoplasma gondii-derived heat shock protein 70
    • Mun, H. S. et al. Toll-like receptor 4 mediates tolerance in macrophages stimulated with Toxoplasma gondii-derived heat shock protein 70. Infect. Immun. 73, 4634-4642 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 4634-4642
    • Mun, H.S.1
  • 55
    • 79251522140 scopus 로고    scopus 로고
    • NALP1 influences susceptibility to human congenital toxoplasmosis, proinflammatory cytokine response, and fate of Toxoplasma gondii-infected monocytic cells
    • Witola, W. H. et al. NALP1 influences susceptibility to human congenital toxoplasmosis, proinflammatory cytokine response, and fate of Toxoplasma gondii-infected monocytic cells. Infect. Immun. 79, 756-766 (2011).
    • (2011) Infect. Immun. , vol.79 , pp. 756-766
    • Witola, W.H.1
  • 56
    • 84883444752 scopus 로고    scopus 로고
    • Human innate immunity to Toxoplasma gondii is mediated by host caspase-1 and ASC and parasite GRA15
    • Gov, L., Karimzadeh, A., Ueno, N. and Lodoen, M. B. Human innate immunity to Toxoplasma gondii is mediated by host caspase-1 and ASC and parasite GRA15. mBio 4, e00255-e00213 (2013).
    • (2013) MBio , vol.4
    • Gov, L.1    Karimzadeh, A.2    Ueno, N.3    Lodoen, M.B.4
  • 58
    • 0027939611 scopus 로고
    • Parasite-induced IL-12 stimulates early IFNγ synthesis and resistance during acute infection with Toxoplasma gondii
    • Gazzinelli, R. T. et al. Parasite-induced IL-12 stimulates early IFNγ synthesis and resistance during acute infection with Toxoplasma gondii. J. Immunol. 153, 2533-2543 (1994).
    • (1994) J. Immunol. , vol.153 , pp. 2533-2543
    • Gazzinelli, R.T.1
  • 60
    • 0028348030 scopus 로고
    • Interleukin-12 enhances murine survival against acute toxoplasmosis
    • Khan, I. A., Matsuura, T. and Kasper, L. H. Interleukin-12 enhances murine survival against acute toxoplasmosis. Infect. Immun. 62, 1639-1642 (1994).
    • (1994) Infect. Immun. , vol.62 , pp. 1639-1642
    • Khan, I.A.1    Matsuura, T.2    Kasper, L.H.3
  • 61
    • 0030970867 scopus 로고    scopus 로고
    • Inducible nitric oxide is essential for host control of persistent but not acute infection with the intracellular pathogen Toxoplasma gondii
    • Scharton-Kersten, T. M., Yap, G., Magram, J. and Sher, A. Inducible nitric oxide is essential for host control of persistent but not acute infection with the intracellular pathogen Toxoplasma gondii. J. Exp. Med. 185, 1261-1273 (1997).
    • (1997) J. Exp. Med. , vol.185 , pp. 1261-1273
    • Scharton-Kersten, T.M.1    Yap, G.2    Magram, J.3    Sher, A.4
  • 62
    • 3242805827 scopus 로고    scopus 로고
    • IL-23 provides a limited mechanism of resistance to acute toxoplasmosis in the absence of IL-12
    • Lieberman, L. A. et al. IL-23 provides a limited mechanism of resistance to acute toxoplasmosis in the absence of IL-12. J. Immunol. 173, 1887-1893 (2004).
    • (2004) J. Immunol. , vol.173 , pp. 1887-1893
    • Lieberman, L.A.1
  • 63
    • 0037313578 scopus 로고    scopus 로고
    • Interleukin-12 and the regulation of innate resistance and adaptive immunity
    • Trinchieri, G. Interleukin-12 and the regulation of innate resistance and adaptive immunity. Nature Rev. Immunol. 3, 133-146 (2003).
    • (2003) Nature Rev. Immunol. , vol.3 , pp. 133-146
    • Trinchieri, G.1
  • 64
    • 0030294163 scopus 로고    scopus 로고
    • In the absence of endogenous IFNγ, mice develop unimpaired IL-12 responses to Toxoplasma gondii while failing to control acute infection
    • Scharton-Kersten, T. M. et al. In the absence of endogenous IFNγ, mice develop unimpaired IL-12 responses to Toxoplasma gondii while failing to control acute infection. J. Immunol. 157, 4045-4054 (1996).
    • (1996) J. Immunol. , vol.157 , pp. 4045-4054
    • Scharton-Kersten, T.M.1
  • 65
    • 0030664056 scopus 로고    scopus 로고
    • Interferon consensus sequence binding protein-deficient mice display impaired resistance to intracellular infection due to a primary defect in interleukin 12 p40 induction
    • Scharton-Kersten, T., Contursi, C., Masumi, A., Sher, A. and Ozato, K. Interferon consensus sequence binding protein-deficient mice display impaired resistance to intracellular infection due to a primary defect in interleukin 12 p40 induction. J. Exp. Med. 186, 1523-1534 (1997).
    • (1997) J. Exp. Med. , vol.186 , pp. 1523-1534
    • Scharton-Kersten, T.1    Contursi, C.2    Masumi, A.3    Sher, A.4    Ozato, K.5
  • 66
    • 80051915459 scopus 로고    scopus 로고
    • CD8α+ dendritic cells are the critical source of interleukin-12 that controls acute infection by Toxoplasma gondii tachyzoites
    • Mashayekhi, M. et al. CD8α+ dendritic cells are the critical source of interleukin-12 that controls acute infection by Toxoplasma gondii tachyzoites. Immunity 35, 249-259 (2011).
    • (2011) Immunity , vol.35 , pp. 249-259
    • Mashayekhi, M.1
  • 67
    • 17844380477 scopus 로고    scopus 로고
    • Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction
    • Honda, K. et al. Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction. Nature 434, 1035-1040 (2005).
    • (2005) Nature , vol.434 , pp. 1035-1040
    • Honda, K.1
  • 68
    • 15044345461 scopus 로고    scopus 로고
    • Integral role of IRF-5 in the gene induction programme activated by Toll-like receptors
    • Takaoka, A. et al. Integral role of IRF-5 in the gene induction programme activated by Toll-like receptors. Nature 434, 243-249 (2005).
    • (2005) Nature , vol.434 , pp. 243-249
    • Takaoka, A.1
  • 69
    • 0027264849 scopus 로고
    • Interleukin 12 is required for the T-lymphocyte-independent induction of interferon-γ by an intracellular parasite and induces resistance in T-cell-deficient hosts
    • Gazzinelli, R. T., Hieny, S., Wynn, T. A., Wolf, S. and Sher, A. Interleukin 12 is required for the T-lymphocyte-independent induction of interferon-γ by an intracellular parasite and induces resistance in T-cell-deficient hosts. Proc. Natl Acad. Sci. USA 90, 6115-6119 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6115-6119
    • Gazzinelli, R.T.1    Hieny, S.2    Wynn, T.A.3    Wolf, S.4    Sher, A.5
  • 70
    • 0028272528 scopus 로고
    • Production of γ-interferon by natural killer cells from Toxoplasma gondii-infected SCID mice: Regulation by interleukin-10, interleukin-12, and tumor necrosis factor-α
    • Hunter, C. A., Subauste, C. S., Van Cleave, V. H. and Remington, J. S. Production of γ-interferon by natural killer cells from Toxoplasma gondii-infected SCID mice: regulation by interleukin-10, interleukin-12, and tumor necrosis factor-α. Infect. Immun. 62, 2818-2824 (1994).
    • (1994) Infect. Immun. , vol.62 , pp. 2818-2824
    • Hunter, C.A.1    Subauste, C.S.2    Van Cleave, V.H.3    Remington, J.S.4
  • 71
    • 56449097442 scopus 로고    scopus 로고
    • Batf3 deficiency reveals a critical role for CD8α+ dendritic cells in cytotoxic T cell immunity
    • Hildner, K. et al. Batf3 deficiency reveals a critical role for CD8α+ dendritic cells in cytotoxic T cell immunity. Science 322, 1097-1100 (2008).
    • (2008) Science , vol.322 , pp. 1097-1100
    • Hildner, K.1
  • 72
    • 0037011021 scopus 로고    scopus 로고
    • ICSBP is essential for the development of mouse type i interferon-producing cells and for the generation and activation of CD8α+ dendritic cells
    • Schiavoni, G. et al. ICSBP is essential for the development of mouse type I interferon-producing cells and for the generation and activation of CD8α+ dendritic cells. J. Exp. Med. 196, 1415-1425 (2002).
    • (2002) J. Exp. Med. , vol.196 , pp. 1415-1425
    • Schiavoni, G.1
  • 73
    • 0037310617 scopus 로고    scopus 로고
    • Cutting edge: IFN consensus sequence binding protein/IFN regulatory factor 8 drives the development of type i IFN-producing plasmacytoid dendritic cells
    • Tsujimura, H., Tamura, T. and Ozato, K. Cutting edge: IFN consensus sequence binding protein/IFN regulatory factor 8 drives the development of type I IFN-producing plasmacytoid dendritic cells. J. Immunol. 170, 1131-1135 (2003).
    • (2003) J. Immunol. , vol.170 , pp. 1131-1135
    • Tsujimura, H.1    Tamura, T.2    Ozato, K.3
  • 74
    • 84867884822 scopus 로고    scopus 로고
    • Compensatory dendritic cell development mediated by BATF-IRF interactions
    • Tussiwand, R. et al. Compensatory dendritic cell development mediated by BATF-IRF interactions. Nature 490, 502-507 (2012).
    • (2012) Nature , vol.490 , pp. 502-507
    • Tussiwand, R.1
  • 75
    • 84876469090 scopus 로고    scopus 로고
    • CD8α+ DCs can be induced in the absence of transcription factors Id2, Nfil3, and Batf3
    • Seillet, C. et al. CD8α+ DCs can be induced in the absence of transcription factors Id2, Nfil3, and Batf3. Blood 121, 1574-1583 (2013).
    • (2013) Blood , vol.121 , pp. 1574-1583
    • Seillet, C.1
  • 76
    • 74549167783 scopus 로고    scopus 로고
    • Regulation of adaptive immunity by the innate immune system
    • Iwasaki, A. and Medzhitov, R. Regulation of adaptive immunity by the innate immune system. Science 327, 291-295 (2010).
    • (2010) Science , vol.327 , pp. 291-295
    • Iwasaki, A.1    Medzhitov, R.2
  • 77
    • 33748848754 scopus 로고    scopus 로고
    • On regulation of phagosome maturation and antigen presentation
    • Blander, J. M. and Medzhitov, R. On regulation of phagosome maturation and antigen presentation. Nature Immunol. 7, 1029-1035 (2006).
    • (2006) Nature Immunol , vol.7 , pp. 1029-1035
    • Blander, J.M.1    Medzhitov, R.2
  • 78
    • 4143086928 scopus 로고    scopus 로고
    • Enhanced dendritic cell antigen capture via Toll-like receptor-induced actin remodeling
    • West, M. A. et al. Enhanced dendritic cell antigen capture via Toll-like receptor-induced actin remodeling. Science 305, 1153-1157 (2004).
    • (2004) Science , vol.305 , pp. 1153-1157
    • West, M.A.1
  • 79
    • 84893101766 scopus 로고    scopus 로고
    • CD103-CD11b+ dendritic cells regulate the sensitivity of CD4 T-cell responses to bacterial flagellin
    • Atif, S. M., Uematsu, S., Akira, S. and McSorley, S. J. CD103-CD11b+ dendritic cells regulate the sensitivity of CD4 T-cell responses to bacterial flagellin. Mucosal Immunol. 1, 25 (2013).
    • (2013) Mucosal Immunol , vol.1 , pp. 25
    • Atif, S.M.1    Uematsu, S.2    Akira, S.3    McSorley, S.J.4
  • 80
    • 78650368903 scopus 로고    scopus 로고
    • TLR5 functions as an endocytic receptor to enhance flagellin-specific adaptive immunity
    • Letran, S. E. et al. TLR5 functions as an endocytic receptor to enhance flagellin-specific adaptive immunity. Eur. J. Immunol. 41, 29-38 (2011).
    • (2011) Eur. J. Immunol. , vol.41 , pp. 29-38
    • Letran, S.E.1
  • 81
    • 84872688583 scopus 로고    scopus 로고
    • Parasite-induced TH1 cells and intestinal dysbiosis cooperate in IFNγ-dependent elimination of Paneth cells
    • Raetz, M. et al. Parasite-induced TH1 cells and intestinal dysbiosis cooperate in IFNγ-dependent elimination of Paneth cells. Nature Immunol. 14, 136-142 (2013).
    • (2013) Nature Immunol , vol.14 , pp. 136-142
    • Raetz, M.1
  • 82
    • 51549098030 scopus 로고    scopus 로고
    • TLR adaptor MyD88 is essential for pathogen control during oral Toxoplasma gondii infection but not adaptive immunity induced by a vaccine strain of the parasite
    • Sukhumavasi, W. et al. TLR adaptor MyD88 is essential for pathogen control during oral Toxoplasma gondii infection but not adaptive immunity induced by a vaccine strain of the parasite. J. Immunol. 181, 3464-3473 (2008).
    • (2008) J. Immunol. , vol.181 , pp. 3464-3473
    • Sukhumavasi, W.1
  • 83
    • 79951904892 scopus 로고    scopus 로고
    • Invasion and intracellular survival by protozoan parasites
    • Sibley, L. D. Invasion and intracellular survival by protozoan parasites. Immunol. Rev. 240, 72-91 (2011).
    • (2011) Immunol. Rev. , vol.240 , pp. 72-91
    • Sibley, L.D.1
  • 84
    • 0345151828 scopus 로고    scopus 로고
    • Toxoplasma gondii resides in a vacuole that avoids fusion with host cell endocytic and exocytic vesicular trafficking pathways
    • Mordue, D. G., Hakansson, S., Niesman, I. and Sibley, L. D. Toxoplasma gondii resides in a vacuole that avoids fusion with host cell endocytic and exocytic vesicular trafficking pathways. Exp. Parasitol. 92, 87-99 (1999).
    • (1999) Exp. Parasitol. , vol.92 , pp. 87-99
    • Mordue, D.G.1    Hakansson, S.2    Niesman, I.3    Sibley, L.D.4
  • 85
    • 4043119714 scopus 로고    scopus 로고
    • Functional inactivation of immature dendritic cells by the intracellular parasite Toxoplasma gondii
    • McKee, A. S., Dzierszinski, F., Boes, M., Roos, D. S. and Pearce, E. J. Functional inactivation of immature dendritic cells by the intracellular parasite Toxoplasma gondii. J. Immunol. 173, 2632-2640 (2004).
    • (2004) J. Immunol. , vol.173 , pp. 2632-2640
    • McKee, A.S.1    Dzierszinski, F.2    Boes, M.3    Roos, D.S.4    Pearce, E.J.5
  • 86
    • 33748135929 scopus 로고    scopus 로고
    • Diverse mechanisms employed by Toxoplasma gondii to inhibit IFNγ-induced major histocompatibility complex class II gene expression
    • Lang, C., Algner, M., Beinert, N., Gross, U. and Luder, C. G. Diverse mechanisms employed by Toxoplasma gondii to inhibit IFNγ-induced major histocompatibility complex class II gene expression. Microbes Infect. 8, 1994-2005 (2006).
    • (2006) Microbes Infect , vol.8 , pp. 1994-2005
    • Lang, C.1    Algner, M.2    Beinert, N.3    Gross, U.4    Luder, C.G.5
  • 87
    • 70449566047 scopus 로고    scopus 로고
    • Dysregulation of macrophage signal transduction by Toxoplasma gondii: Past progress and recent advances
    • Leng, J., Butcher, B. A. and Denkers, E. Y. Dysregulation of macrophage signal transduction by Toxoplasma gondii: past progress and recent advances. Parasite Immunol. 31, 717-728 (2009).
    • (2009) Parasite Immunol , vol.31 , pp. 717-728
    • Leng, J.1    Butcher, B.A.2    Denkers, E.Y.3
  • 88
    • 0031278412 scopus 로고    scopus 로고
    • Intracellular fate of vacuoles containing Toxoplasma gondii is determined at the time of formation and depends on the mechanism of entry
    • Mordue, D. G. and Sibley, L. D. Intracellular fate of vacuoles containing Toxoplasma gondii is determined at the time of formation and depends on the mechanism of entry. J. Immunol. 159, 4452-4459 (1997).
    • (1997) J. Immunol. , vol.159 , pp. 4452-4459
    • Mordue, D.G.1    Sibley, L.D.2
  • 89
    • 12844278885 scopus 로고    scopus 로고
    • Class i major histocompatibility complex presentation of antigens that escape from the parasitophorous vacuole of Toxoplasma gondii
    • Gubbels, M. J., Striepen, B., Shastri, N., Turkoz, M. and Robey, E. A. Class I major histocompatibility complex presentation of antigens that escape from the parasitophorous vacuole of Toxoplasma gondii. Infect. Immun. 73, 703-711 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 703-711
    • Gubbels, M.J.1    Striepen, B.2    Shastri, N.3    Turkoz, M.4    Robey, E.A.5
  • 90
    • 35748974538 scopus 로고    scopus 로고
    • Presentation of Toxoplasma gondii antigens via the endogenous major histocompatibility complex class i pathway in nonprofessional and professional antigen-presenting cells
    • Dzierszinski, F. et al. Presentation of Toxoplasma gondii antigens via the endogenous major histocompatibility complex class I pathway in nonprofessional and professional antigen-presenting cells. Infect. Immun. 75, 5200-5209 (2007).
    • (2007) Infect. Immun. , vol.75 , pp. 5200-5209
    • Dzierszinski, F.1
  • 91
    • 0030783010 scopus 로고    scopus 로고
    • Association of host cell endoplasmic reticulum and mitochondria with the Toxoplasma gondii parasitophorous vacuole membrane: A high affinity interaction
    • Sinai, A. P., Webster, P. and Joiner, K. A. Association of host cell endoplasmic reticulum and mitochondria with the Toxoplasma gondii parasitophorous vacuole membrane: a high affinity interaction. J. Cell Sci. 110, 2117-2128 (1997).
    • (1997) J. Cell Sci. , vol.110 , pp. 2117-2128
    • Sinai, A.P.1    Webster, P.2    Joiner, K.A.3
  • 92
    • 63049095770 scopus 로고    scopus 로고
    • Host ER-parasitophorous vacuole interaction provides a route of entry for antigen cross-presentation in Toxoplasma gondii-infected dendritic cells
    • Goldszmid, R. S. et al. Host ER-parasitophorous vacuole interaction provides a route of entry for antigen cross-presentation in Toxoplasma gondii-infected dendritic cells. J. Exp. Med. 206, 399-410 (2009).
    • (2009) J. Exp. Med. , vol.206 , pp. 399-410
    • Goldszmid, R.S.1
  • 93
    • 47849095938 scopus 로고    scopus 로고
    • Immunodominant, protective response to the parasite Toxoplasma gondii requires antigen processing in the endoplasmic reticulum
    • Blanchard, N. et al. Immunodominant, protective response to the parasite Toxoplasma gondii requires antigen processing in the endoplasmic reticulum. Nature Immunol. 9, 937-944 (2008).
    • (2008) Nature Immunol. , vol.9 , pp. 937-944
    • Blanchard, N.1
  • 94
    • 79960859396 scopus 로고    scopus 로고
    • Subcellular antigen location influences T-cell activation during acute infection with Toxoplasma gondii
    • Gregg, B. et al. Subcellular antigen location influences T-cell activation during acute infection with Toxoplasma gondii. PLoS ONE 6, 28 (2011).
    • (2011) PLoS ONE , vol.6 , pp. 28
    • Gregg, B.1
  • 95
    • 70049090747 scopus 로고    scopus 로고
    • Dynamic Imaging of CD8+ T cells and dendritic cells during infection with Toxoplasma gondii
    • John, B. et al. Dynamic Imaging of CD8+ T cells and dendritic cells during infection with Toxoplasma gondii. PLoS Pathog. 5, 3 (2009).
    • (2009) PLoS Pathog , vol.5 , pp. 3
    • John, B.1
  • 96
    • 84864585429 scopus 로고    scopus 로고
    • Toxoplasma co-opts host cells it does not invade
    • Koshy, A. A. et al. Toxoplasma co-opts host cells it does not invade. PLoS Pathog. 8, 26 (2012).
    • (2012) PLoS Pathog , vol.8 , pp. 26
    • Koshy, A.A.1
  • 97
    • 77950433922 scopus 로고    scopus 로고
    • Differential regulation of effector-and central-memory responses to Toxoplasma gondii Infection by IL-12 revealed by tracking of Tgd057-specific CD8+ T cells
    • Wilson, D. C. et al. Differential regulation of effector-and central-memory responses to Toxoplasma gondii Infection by IL-12 revealed by tracking of Tgd057-specific CD8+ T cells. PLoS Pathog. 6, 1000815 (2010).
    • (2010) PLoS Pathog , vol.6 , pp. 1000815
    • Wilson, D.C.1
  • 98
    • 0034662258 scopus 로고    scopus 로고
    • Cutting edge: IL-12 is required for the maintenance of IFNγ production in T cells mediating chronic resistance to the intracellular pathogen, Toxoplasma gondii
    • Yap, G., Pesin, M. and Sher, A. Cutting edge: IL-12 is required for the maintenance of IFNγ production in T cells mediating chronic resistance to the intracellular pathogen, Toxoplasma gondii. J. Immunol. 165, 628-631 (2000).
    • (2000) J. Immunol. , vol.165 , pp. 628-631
    • Yap, G.1    Pesin, M.2    Sher, A.3
  • 99
    • 0030297825 scopus 로고    scopus 로고
    • Toxoplasma gondii: Evidence for interleukin-12-dependent and-independent pathways of interferon-γ production induced by an attenuated parasite strain
    • Scharton-Kersten, T., Caspar, P., Sher, A. and Denkers, E. Y. Toxoplasma gondii: evidence for interleukin-12-dependent and-independent pathways of interferon-γ production induced by an attenuated parasite strain. Exp. Parasitol. 84, 102-114 (1996).
    • (1996) Exp. Parasitol. , vol.84 , pp. 102-114
    • Scharton-Kersten, T.1    Caspar, P.2    Sher, A.3    Denkers, E.Y.4
  • 100
    • 84879545667 scopus 로고    scopus 로고
    • TLR-independent neutrophil-derived IFNγ is important for host resistance to intracellular pathogens
    • Sturge, C. R. et al. TLR-independent neutrophil-derived IFNγ is important for host resistance to intracellular pathogens. Proc. Natl Acad. Sci. USA 110, 10711-10716 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 10711-10716
    • Sturge, C.R.1
  • 101
    • 58849160457 scopus 로고    scopus 로고
    • Recognition of Toxoplasma gondii by TLR11 prevents parasite-induced immunopathology
    • Yarovinsky, F., Hieny, S. and Sher, A. Recognition of Toxoplasma gondii by TLR11 prevents parasite-induced immunopathology. J. Immunol. 181, 8478-8484 (2008).
    • (2008) J. Immunol. , vol.181 , pp. 8478-8484
    • Yarovinsky, F.1    Hieny, S.2    Sher, A.3
  • 102
    • 0020502358 scopus 로고
    • Identification of interferon-γ as the lymphokine that activates human macrophage oxidative metabolism and antimicrobial activity
    • Nathan, C. F., Murray, H. W., Wiebe, M. E. and Rubin, B. Y. Identification of interferon-γ as the lymphokine that activates human macrophage oxidative metabolism and antimicrobial activity. J. Exp. Med. 158, 670-689 (1983).
    • (1983) J. Exp. Med. , vol.158 , pp. 670-689
    • Nathan, C.F.1    Murray, H.W.2    Wiebe, M.E.3    Rubin, B.Y.4
  • 103
    • 0022386733 scopus 로고
    • Activation of tissue macrophages from AIDS patients: In vitro response of AIDS alveolar macrophages to lymphokines and interferon-γ
    • Murray, H. W., Gellene, R. A., Libby, D. M., Rothermel, C. D. and Rubin, B. Y. Activation of tissue macrophages from AIDS patients: in vitro response of AIDS alveolar macrophages to lymphokines and interferon-γ. J. Immunol. 135, 2374-2377 (1985).
    • (1985) J. Immunol. , vol.135 , pp. 2374-2377
    • Murray, H.W.1    Gellene, R.A.2    Libby, D.M.3    Rothermel, C.D.4    Rubin, B.Y.5
  • 104
    • 0000056144 scopus 로고
    • Interferon-γ blocks the growth of Toxoplasma gondii in human fibroblasts by inducing the host cells to degrade tryptophan
    • Pfefferkorn, E. R. Interferon-γ blocks the growth of Toxoplasma gondii in human fibroblasts by inducing the host cells to degrade tryptophan. Proc. Natl Acad. Sci. USA 81, 908-912 (1984).
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 908-912
    • Pfefferkorn, E.R.1
  • 105
    • 0022503270 scopus 로고
    • Characterization of an indoleamine 2,3-dioxygenase induced by γ-interferon in cultured human fibroblasts
    • Pfefferkorn, E. R., Rebhun, S. and Eckel, M. Characterization of an indoleamine 2,3-dioxygenase induced by γ-interferon in cultured human fibroblasts. J. Interferon Res. 6, 267-279 (1986).
    • (1986) J. Interferon Res. , vol.6 , pp. 267-279
    • Pfefferkorn, E.R.1    Rebhun, S.2    Eckel, M.3
  • 106
    • 34249295962 scopus 로고    scopus 로고
    • Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice
    • Ball, H. J. et al. Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice. Gene 396, 203-213 (2007).
    • (2007) Gene , vol.396 , pp. 203-213
    • Ball, H.J.1
  • 107
    • 34547643025 scopus 로고    scopus 로고
    • Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan
    • Metz, R. et al. Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan. Cancer Res. 67, 7082-7087 (2007).
    • (2007) Cancer Res , vol.67 , pp. 7082-7087
    • Metz, R.1
  • 108
    • 84555187508 scopus 로고    scopus 로고
    • Opposing biological functions of tryptophan catabolizing enzymes during intracellular infection
    • Divanovic, S. et al. Opposing biological functions of tryptophan catabolizing enzymes during intracellular infection. J. Infect. Dis. 205, 152-161 (2012).
    • (2012) J. Infect. Dis. , vol.205 , pp. 152-161
    • Divanovic, S.1
  • 109
    • 0025219762 scopus 로고
    • Microbiostatic effect of murine-activated macrophages for Toxoplasma gondii. Role for synthesis of inorganic nitrogen oxides from L-arginine
    • Adams, L. B., Hibbs, J. B. Jr., Taintor, R. R. and Krahenbuhl, J. L. Microbiostatic effect of murine-activated macrophages for Toxoplasma gondii. Role for synthesis of inorganic nitrogen oxides from L-arginine. J. Immunol. 144, 2725-2729 (1990).
    • (1990) J. Immunol. , vol.144 , pp. 2725-2729
    • Adams, L.B.1    Hibbs Jr., J.B.2    Taintor, R.R.3    Krahenbuhl, J.L.4
  • 110
    • 4844227764 scopus 로고    scopus 로고
    • Antimicrobial reactive oxygen and nitrogen species: Concepts and controversies
    • Fang, F. C. Antimicrobial reactive oxygen and nitrogen species: concepts and controversies. Nature Rev. Microbiol. 2, 820-832 (2004).
    • (2004) Nature Rev. Microbiol. , vol.2 , pp. 820-832
    • Fang, F.C.1
  • 111
    • 1542375414 scopus 로고    scopus 로고
    • Toxoplasma gondii lacks the enzymes required for de novo arginine biosynthesis and arginine starvation triggers cyst formation
    • Fox, B. A., Gigley, J. P. and Bzik, D. J. Toxoplasma gondii lacks the enzymes required for de novo arginine biosynthesis and arginine starvation triggers cyst formation. Int. J. Parasitol. 34, 323-331 (2004).
    • (2004) Int. J. Parasitol. , vol.34 , pp. 323-331
    • Fox, B.A.1    Gigley, J.P.2    Bzik, D.J.3
  • 112
    • 84893144953 scopus 로고    scopus 로고
    • Toxoplasma gondii rhoptry kinase ROP16 activates STAT3 and STAT6 resulting in cytokine inhibition and arginase-1-dependent growth control
    • Butcher, B. A. et al. Toxoplasma gondii rhoptry kinase ROP16 activates STAT3 and STAT6 resulting in cytokine inhibition and arginase-1-dependent growth control. PLoS Pathog. 7, 8 (2011).
    • (2011) PLoS Pathog , vol.7 , pp. 8
    • Butcher, B.A.1
  • 113
    • 56349093356 scopus 로고    scopus 로고
    • Toll-like receptor-induced arginase 1 in macrophages thwarts effective immunity against intracellular pathogens
    • El Kasmi, K. C. et al. Toll-like receptor-induced arginase 1 in macrophages thwarts effective immunity against intracellular pathogens. Nature Immunol. 9, 1399-1406 (2008).
    • (2008) Nature Immunol , vol.9 , pp. 1399-1406
    • El Kasmi, K.C.1
  • 114
    • 0033526013 scopus 로고    scopus 로고
    • Effector cells of both nonhemopoietic and hemopoietic origin are required for interferon (IFN)-γ- and tumor necrosis factor (TNF)- α-dependent host resistance to the intracellular pathogen, Toxoplasma gondii
    • Yap, G. S. and Sher, A. Effector cells of both nonhemopoietic and hemopoietic origin are required for interferon (IFN)-γ- and tumor necrosis factor (TNF)- α-dependent host resistance to the intracellular pathogen, Toxoplasma gondii. J. Exp. Med. 189, 1083-1092 (1999).
    • (1999) J. Exp. Med. , vol.189 , pp. 1083-1092
    • Yap, G.S.1    Sher, A.2
  • 115
    • 0344171941 scopus 로고    scopus 로고
    • Inhibition of inducible nitric oxide synthase exacerbates chronic cerebral toxoplasmosis in Toxoplasma gondii-susceptible C57BL/6 mice but does not reactivate the latent disease in T. Gondii-resistant BALB/c mice
    • Schluter, D. et al. Inhibition of inducible nitric oxide synthase exacerbates chronic cerebral toxoplasmosis in Toxoplasma gondii-susceptible C57BL/6 mice but does not reactivate the latent disease in T. gondii-resistant BALB/c mice. J. Immunol. 162, 3512-3518 (1999).
    • (1999) J. Immunol. , vol.162 , pp. 3512-3518
    • Schluter, D.1
  • 116
    • 0032530950 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase is not required for long-term vaccine-based immunity against Toxoplasma gondii
    • Khan, I. A., Matsuura, T. and Kasper, L. H. Inducible nitric oxide synthase is not required for long-term vaccine-based immunity against Toxoplasma gondii. J. Immunol. 161, 2994-3000 (1998).
    • (1998) J. Immunol. , vol.161 , pp. 2994-3000
    • Khan, I.A.1    Matsuura, T.2    Kasper, L.H.3
  • 117
    • 0034119470 scopus 로고    scopus 로고
    • Induction of tumor necrosis factor-α and inducible nitric oxide synthase fails to prevent toxoplasmic encephalitis in the absence of interferon-γ in genetically resistant BALB/c mice
    • Suzuki, Y., Kang, H., Parmley, S., Lim, S. and Park, D. Induction of tumor necrosis factor-α and inducible nitric oxide synthase fails to prevent toxoplasmic encephalitis in the absence of interferon-γ in genetically resistant BALB/c mice. Microbes Infect. 2, 455-462 (2000).
    • (2000) Microbes Infect , vol.2 , pp. 455-462
    • Suzuki, Y.1    Kang, H.2    Parmley, S.3    Lim, S.4    Park, D.5
  • 118
    • 0026516690 scopus 로고
    • L-arginine-dependent reactive nitrogen intermediates and the antimicrobial effect of activated human mononuclear phagocytes
    • Murray, H. W. and Teitelbaum, R. F. L-arginine-dependent reactive nitrogen intermediates and the antimicrobial effect of activated human mononuclear phagocytes. J. Infect. Dis. 165, 513-517 (1992).
    • (1992) J. Infect. Dis. , vol.165 , pp. 513-517
    • Murray, H.W.1    Teitelbaum, R.F.2
  • 119
    • 0018704363 scopus 로고
    • Macrophage oxygen-dependent antimicrobial activity. II. The role of oxygen intermediates
    • Murray, H. W., Juangbhanich, C. W., Nathan, C. F. and Cohn, Z. A. Macrophage oxygen-dependent antimicrobial activity. II. The role of oxygen intermediates. J. Exp. Med. 150, 950-964 (1979).
    • (1979) J. Exp. Med. , vol.150 , pp. 950-964
    • Murray, H.W.1    Juangbhanich, C.W.2    Nathan, C.F.3    Cohn, Z.A.4
  • 120
    • 0018834868 scopus 로고
    • Failure to trigger the oxidative metabolic burst by normal macrophages: Possible mechanism for survival of intracellular pathogens
    • Wilson, C. B., Tsai, V. and Remington, J. S. Failure to trigger the oxidative metabolic burst by normal macrophages: possible mechanism for survival of intracellular pathogens. J. Exp. Med. 151, 328-346 (1980).
    • (1980) J. Exp. Med. , vol.151 , pp. 328-346
    • Wilson, C.B.1    Tsai, V.2    Remington, J.S.3
  • 121
    • 0024464277 scopus 로고
    • Macrophage oxidative metabolism and intracellular Toxoplasma gondii
    • Chang, H. R. and Pechere, J. C. Macrophage oxidative metabolism and intracellular Toxoplasma gondii. Microb. Pathog. 7, 37-44 (1989).
    • (1989) Microb. Pathog. , vol.7 , pp. 37-44
    • Chang, H.R.1    Pechere, J.C.2
  • 122
    • 1142298755 scopus 로고    scopus 로고
    • P47 GTPases: Regulators of immunity to intracellular pathogens
    • Taylor, G. A. and Feng, C. G, and Sher, A. p47 GTPases: regulators of immunity to intracellular pathogens. Nature Rev. Immunol. 4, 100-109 (2004).
    • (2004) Nature Rev. Immunol. , vol.4 , pp. 100-109
    • Taylor, G.A.1    Feng, C.G.2    Sher, A.3
  • 123
    • 84893065750 scopus 로고    scopus 로고
    • The interferon-inducible p47 (IRG) GTPases in vertebrates: Loss of the cell autonomous resistance mechanism in the human lineage
    • Bekpen, C. et al. The interferon-inducible p47 (IRG) GTPases in vertebrates: loss of the cell autonomous resistance mechanism in the human lineage. Genome Biol. 6, 31 (2005).
    • (2005) Genome Biol , vol.6 , pp. 31
    • Bekpen, C.1
  • 124
    • 0034681123 scopus 로고    scopus 로고
    • Pathogen-specific loss of host resistance in mice lacking the IFNγ-inducible gene IGTP
    • Taylor, G. A. et al. Pathogen-specific loss of host resistance in mice lacking the IFNγ-inducible gene IGTP. Proc. Natl Acad. Sci. USA 97, 751-755 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 751-755
    • Taylor, G.A.1
  • 125
    • 0035898464 scopus 로고    scopus 로고
    • Inactivation of LRG-47 and IRG-47 reveals a family of interferon gamma-inducible genes with essential, pathogen-specific roles in resistance to infection
    • Collazo, C. M. et al. Inactivation of LRG-47 and IRG-47 reveals a family of interferon gamma-inducible genes with essential, pathogen-specific roles in resistance to infection. J. Exp. Med. 194, 181-188 (2001).
    • (2001) J. Exp. Med. , vol.194 , pp. 181-188
    • Collazo, C.M.1
  • 126
    • 79959228478 scopus 로고    scopus 로고
    • The IFNγ-inducible GTPase, Irga6, protects mice against Toxoplasma gondii but not against Plasmodium berghei and some other intracellular pathogens
    • Liesenfeld, O. et al. The IFNγ-inducible GTPase, Irga6, protects mice against Toxoplasma gondii but not against Plasmodium berghei and some other intracellular pathogens. PLoS ONE 6, 17 (2011).
    • (2011) PLoS ONE , vol.6 , pp. 17
    • Liesenfeld, O.1
  • 127
    • 78650194774 scopus 로고    scopus 로고
    • Phosphorylation of immunity-related GTPases by a Toxoplasma gondii-secreted kinase promotes macrophage survival and virulence
    • Fentress, S. J. et al. Phosphorylation of immunity-related GTPases by a Toxoplasma gondii-secreted kinase promotes macrophage survival and virulence. Cell Host Microbe 8, 484-495 (2010).
    • (2010) Cell Host Microbe , vol.8 , pp. 484-495
    • Fentress, S.J.1
  • 128
    • 61449117883 scopus 로고    scopus 로고
    • Disruption of the Toxoplasma gondii parasitophorous vacuole by IFNγ-inducible immunity-related GTPases (IRG proteins) triggers necrotic cell death
    • Zhao, Y. O., Khaminets, A., Hunn, J. P. and Howard, J. C. Disruption of the Toxoplasma gondii parasitophorous vacuole by IFNγ-inducible immunity-related GTPases (IRG proteins) triggers necrotic cell death. PLoS Pathog. 5, 6 (2009).
    • (2009) PLoS Pathog , vol.5 , pp. 6
    • Zhao, Y.O.1    Khaminets, A.2    Hunn, J.P.3    Howard, J.C.4
  • 129
    • 4043065683 scopus 로고    scopus 로고
    • Mechanisms regulating the positioning of mouse p47 resistance GTPases LRG-47 and IIGP1 on cellular membranes: Retargeting to plasma membrane induced by phagocytosis
    • Martens, S. et al. Mechanisms regulating the positioning of mouse p47 resistance GTPases LRG-47 and IIGP1 on cellular membranes: retargeting to plasma membrane induced by phagocytosis. J. Immunol. 173, 2594-2606 (2004).
    • (2004) J. Immunol. , vol.173 , pp. 2594-2606
    • Martens, S.1
  • 130
    • 19744378057 scopus 로고    scopus 로고
    • P47 GTPases regulate Toxoplasma gondii survival in activated macrophages
    • Butcher, B. A. et al. p47 GTPases regulate Toxoplasma gondii survival in activated macrophages. Infect. Immun. 73, 3278-3286 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 3278-3286
    • Butcher, B.A.1
  • 131
    • 53549109432 scopus 로고    scopus 로고
    • Regulatory interactions between IRG resistance GTPases in the cellular response to Toxoplasma gondii
    • Hunn, J. P. et al. Regulatory interactions between IRG resistance GTPases in the cellular response to Toxoplasma gondii. EMBO J. 27, 2495-2509 (2008).
    • (2008) EMBO J , vol.27 , pp. 2495-2509
    • Hunn, J.P.1
  • 132
    • 77649258180 scopus 로고    scopus 로고
    • Localisation and mislocalisation of the interferon-inducible immunity-related GTPase Irgm1 (LRG-47) in mouse cells
    • Zhao, Y. O., Konen-Waisman, S., Taylor, G. A., Martens, S. and Howard, J. C. Localisation and mislocalisation of the interferon-inducible immunity-related GTPase, Irgm1 (LRG-47) in mouse cells. PLoS ONE 5, 0008648 (2010).
    • (2010) PLoS ONE , vol.5 , pp. 0008648
    • Zhao, Y.O.1    Konen-Waisman, S.2    Taylor, G.A.3    Martens, S.4    Howard, J.C.5
  • 133
    • 83655167092 scopus 로고    scopus 로고
    • The immunity-related GTPase Irgm3 relieves endoplasmic reticulum stress response during coxsackievirus B3 infection via a PI3K/Akt dependent pathway
    • Liu, Z. et al. The immunity-related GTPase Irgm3 relieves endoplasmic reticulum stress response during coxsackievirus B3 infection via a PI3K/Akt dependent pathway. Cell. Microbiol. 14, 133-146 (2012).
    • (2012) Cell. Microbiol. , vol.14 , pp. 133-146
    • Liu, Z.1
  • 134
    • 0030978494 scopus 로고    scopus 로고
    • The inducibly expressed GTPase localizes to the endoplasmic reticulum, independently of GTP binding
    • Taylor, G. A. et al. The inducibly expressed GTPase localizes to the endoplasmic reticulum, independently of GTP binding. J. Biol. Chem. 272, 10639-10645 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 10639-10645
    • Taylor, G.A.1
  • 135
    • 65549154275 scopus 로고    scopus 로고
    • Balance of Irgm protein activities determines IFNγ-induced host defense
    • Henry, S. C. et al. Balance of Irgm protein activities determines IFNγ-induced host defense. J. Leukoc. Biol. 85, 877-885 (2009).
    • (2009) J. Leukoc. Biol. , vol.85 , pp. 877-885
    • Henry, S.C.1
  • 136
    • 77954430293 scopus 로고    scopus 로고
    • Coordinated loading of IRG resistance GTPases on to the Toxoplasma gondii parasitophorous vacuole
    • Khaminets, A. et al. Coordinated loading of IRG resistance GTPases on to the Toxoplasma gondii parasitophorous vacuole. Cell. Microbiol. 12, 939-961 (2010).
    • (2010) Cell. Microbiol. , vol.12 , pp. 939-961
    • Khaminets, A.1
  • 137
    • 33748444233 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane stripping and autophagic elimination of Toxoplasma gondii in primed effector macrophages
    • Ling, Y. M. et al. Vacuolar and plasma membrane stripping and autophagic elimination of Toxoplasma gondii in primed effector macrophages. J. Exp. Med. 203, 2063-2071 (2006).
    • (2006) J. Exp. Med. , vol.203 , pp. 2063-2071
    • Ling, Y.M.1
  • 138
    • 49649126253 scopus 로고    scopus 로고
    • Disruption of Toxoplasma gondii parasitophorous vacuoles by the mouse p47-resistance GTPases
    • Martens, S. et al. Disruption of Toxoplasma gondii parasitophorous vacuoles by the mouse p47-resistance GTPases. PLoS Pathog. 1, 18 (2005).
    • (2005) PLoS Pathog , vol.1 , pp. 18
    • Martens, S.1
  • 139
    • 77957687715 scopus 로고    scopus 로고
    • The mouse resistance protein Irgm1 (LRG-47): A regulator or an effector of pathogen defense?
    • Hunn, J. P. and Howard, J. C. The mouse resistance protein Irgm1 (LRG-47): a regulator or an effector of pathogen defense? PLoS Pathog. 6, 1001008 (2010).
    • (2010) PLoS Pathog , vol.6 , pp. 1001008
    • Hunn, J.P.1    Howard, J.C.2
  • 140
    • 61649097480 scopus 로고    scopus 로고
    • Interferon-inducible immunity-related GTPase Irgm1 regulates IFNγ-dependent host defense, lymphocyte survival and autophagy
    • Feng, C. G., Zheng, L., Lenardo, M. J. and Sher, A. Interferon-inducible immunity-related GTPase Irgm1 regulates IFNγ-dependent host defense, lymphocyte survival and autophagy. Autophagy 5, 232-234 (2009).
    • (2009) Autophagy , vol.5 , pp. 232-234
    • Feng, C.G.1    Zheng, L.2    Lenardo, M.J.3    Sher, A.4
  • 141
    • 76149089546 scopus 로고    scopus 로고
    • Regulation of macrophage motility by Irgm1
    • Henry, S. C. et al. Regulation of macrophage motility by Irgm1. J. Leukoc. Biol. 87, 333-343 (2010).
    • (2010) J. Leukoc. Biol. , vol.87 , pp. 333-343
    • Henry, S.C.1
  • 142
    • 54549089752 scopus 로고    scopus 로고
    • The immunity-related GTPase Irgm1 promotes the expansion of activated CD4+ T cell populations by preventing interferon-γ-induced cell death
    • Feng, C. G. et al. The immunity-related GTPase Irgm1 promotes the expansion of activated CD4+ T cell populations by preventing interferon-γ-induced cell death. Nature Immunol. 9, 1279-1287 (2008).
    • (2008) Nature Immunol , vol.9 , pp. 1279-1287
    • Feng, C.G.1
  • 143
    • 37549048915 scopus 로고    scopus 로고
    • The p47 GTPase Lrg-47 (Irgm1) links host defense and hematopoietic stem cell proliferation
    • Feng, C. G., Weksberg, D. C., Taylor, G. A., Sher, A. and Goodell, M. A. The p47 GTPase Lrg-47 (Irgm1) links host defense and hematopoietic stem cell proliferation. Cell Stem Cell 2, 83-89 (2008).
    • (2008) Cell Stem Cell , vol.2 , pp. 83-89
    • Feng, C.G.1    Weksberg, D.C.2    Taylor, G.A.3    Sher, A.4    Goodell, M.A.5
  • 144
    • 84876857964 scopus 로고    scopus 로고
    • Guanylate-binding protein 1 (Gbp1) contributes to cell-autonomous immunity against Toxoplasma gondii
    • Selleck, E. M. et al. Guanylate-binding protein 1 (Gbp1) contributes to cell-autonomous immunity against Toxoplasma gondii. PLoS Pathog. 9, 25 (2013).
    • (2013) PLoS Pathog , vol.9 , pp. 25
    • Selleck, E.M.1
  • 145
    • 79960362772 scopus 로고    scopus 로고
    • ATF6β is a host cellular target of the Toxoplasma gondii virulence factor ROP18
    • Yamamoto, M. et al. ATF6β is a host cellular target of the Toxoplasma gondii virulence factor ROP18. J. Exp. Med. 208, 1533-1546 (2011).
    • (2011) J. Exp. Med. , vol.208 , pp. 1533-1546
    • Yamamoto, M.1
  • 146
    • 84870848874 scopus 로고    scopus 로고
    • The polymorphic pseudokinase ROP5 controls virulence in Toxoplasma gondii by regulating the active kinase ROP18
    • Behnke, M. S. et al. The polymorphic pseudokinase ROP5 controls virulence in Toxoplasma gondii by regulating the active kinase ROP18. PLoS Pathog. 8, 8 (2012).
    • (2012) PLoS Pathog , vol.8 , pp. 8
    • Behnke, M.S.1
  • 147
    • 78650210471 scopus 로고    scopus 로고
    • Phosphorylation of mouse immunity-related GTPase (IRG) resistance proteins is an evasion strategy for virulent Toxoplasma gondii
    • Steinfeldt, T. et al. Phosphorylation of mouse immunity-related GTPase (IRG) resistance proteins is an evasion strategy for virulent Toxoplasma gondii. PLoS Biol. 8, 1000576 (2010).
    • (2010) PLoS Biol , vol.8 , pp. 1000576
    • Steinfeldt, T.1
  • 149
    • 50449091647 scopus 로고    scopus 로고
    • Deletion polymorphism upstream of IRGM associated with altered IRGM expression and Crohn's disease
    • McCarroll, S. A. et al. Deletion polymorphism upstream of IRGM associated with altered IRGM expression and Crohn's disease. Nature Genet. 40, 1107-1112 (2008).
    • (2008) Nature Genet , vol.40 , pp. 1107-1112
    • McCarroll, S.A.1
  • 150
    • 38849193453 scopus 로고    scopus 로고
    • Extensive characterization of IFN-induced GTPases mGBP1 to mGBP10 involved in host defense
    • Degrandi, D. et al. Extensive characterization of IFN-induced GTPases mGBP1 to mGBP10 involved in host defense. J. Immunol. 179, 7729-7740 (2007).
    • (2007) J. Immunol. , vol.179 , pp. 7729-7740
    • Degrandi, D.1
  • 151
    • 84862209716 scopus 로고    scopus 로고
    • Analyses of murine GBP homology clusters based on in silico, in vitro and in vivo studies
    • Kresse, A. et al. Analyses of murine GBP homology clusters based on in silico, in vitro and in vivo studies. BMC Genomics 9, 1471-2164 (2008).
    • (2008) BMC Genomics , vol.9 , pp. 1471-2164
    • Kresse, A.1
  • 152
    • 84865371084 scopus 로고    scopus 로고
    • A cluster of interferon-γ-inducible p65 GTPases plays a critical role in host defense against Toxoplasma gondii
    • Yamamoto, M. et al. A cluster of interferon-γ-inducible p65 GTPases plays a critical role in host defense against Toxoplasma gondii. Immunity 37, 302-313 (2012).
    • (2012) Immunity , vol.37 , pp. 302-313
    • Yamamoto, M.1
  • 153
    • 84871941976 scopus 로고    scopus 로고
    • Murine guanylate binding protein 2 (mGBP2) controls Toxoplasma gondii replication
    • Degrandi, D. et al. Murine guanylate binding protein 2 (mGBP2) controls Toxoplasma gondii replication. Proc. Natl Acad. Sci. USA 110, 294-299 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 294-299
    • Degrandi, D.1
  • 154
    • 84879547102 scopus 로고    scopus 로고
    • IRG and GBP host resistance factors target aberrant "non-self" vacuoles characterized by the missing of "self" IRGM proteins
    • Haldar, A. K. et al. IRG and GBP host resistance factors target aberrant, "non-self" vacuoles characterized by the missing of "self" IRGM proteins. PLoS Pathog. 9, 13 (2013).
    • (2013) PLoS Pathog. , vol.9 , pp. 13
    • Haldar, A.K.1
  • 155
    • 22144452520 scopus 로고    scopus 로고
    • The evolution of vertebrate Toll-like receptors
    • Roach, J. C. et al. The evolution of vertebrate Toll-like receptors. Proc. Natl Acad. Sci. USA 102, 9577-9582 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 9577-9582
    • Roach, J.C.1
  • 156
    • 80054792189 scopus 로고    scopus 로고
    • Toxoplasma gondii effectors are master regulators of the inflammatory response
    • Melo, M. B., Jensen, K. D. and Saeij, J. P. Toxoplasma gondii effectors are master regulators of the inflammatory response. Trends Parasitol. 27, 487-495 (2011).
    • (2011) Trends Parasitol , vol.27 , pp. 487-495
    • Melo, M.B.1    Jensen, K.D.2    Saeij, J.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.