메뉴 건너뛰기




Volumn 1258, Issue 1, 2012, Pages 135-142

The protozoan pathogen Toxoplasma gondii targets the paracellular pathway to invade the intestinal epithelium

Author keywords

Invasion; Occludin; Tight junctions; Toxoplasma gondii

Indexed keywords

OCCLUDIN;

EID: 84862865662     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2012.06534.x     Document Type: Article
Times cited : (17)

References (87)
  • 1
    • 33344454729 scopus 로고    scopus 로고
    • Toxoplasmosis: beyond animals to humans
    • Sukthana, Y. 2006. Toxoplasmosis: beyond animals to humans. Trends Parasitol. 22: 137-142.
    • (2006) Trends Parasitol. , vol.22 , pp. 137-142
    • Sukthana, Y.1
  • 2
    • 67349248861 scopus 로고    scopus 로고
    • Toxoplasmosis: a history of clinical observations
    • Weiss, L.M. & J.P. Dubey 2009. Toxoplasmosis: a history of clinical observations. Int. J. Parasitol. 39: 895-901.
    • (2009) Int. J. Parasitol. , vol.39 , pp. 895-901
    • Weiss, L.M.1    Dubey, J.P.2
  • 3
    • 0036803121 scopus 로고    scopus 로고
    • Toxoplasma gondii: transmission, diagnosis and prevention
    • Hill, D. & J.P. Dubey 2002. Toxoplasma gondii: transmission, diagnosis and prevention. Clin. Microbiol. Infect. 8: 634-640.
    • (2002) Clin. Microbiol. Infect. , vol.8 , pp. 634-640
    • Hill, D.1    Dubey, J.P.2
  • 4
    • 77949658016 scopus 로고    scopus 로고
    • Toxoplasma gondii: epidemiology, feline clinical aspects, and prevention
    • Elmore, S.A., J.L. Jones, P.A. Conrad, et al 2010. Toxoplasma gondii: epidemiology, feline clinical aspects, and prevention. Trends Parasitol. 26: 190-196.
    • (2010) Trends Parasitol. , vol.26 , pp. 190-196
    • Elmore, S.A.1    Jones, J.L.2    Conrad, P.A.3
  • 5
    • 0347091255 scopus 로고    scopus 로고
    • Recent expansion of Toxoplasma through enhanced oral transmission
    • Su, C., D. Evans, R.H. Cole, et al 2003. Recent expansion of Toxoplasma through enhanced oral transmission. Science 299: 414-416.
    • (2003) Science , vol.299 , pp. 414-416
    • Su, C.1    Evans, D.2    Cole, R.H.3
  • 7
    • 37249017651 scopus 로고    scopus 로고
    • Isolation and genotyping of Toxoplasma gondii from Ugandan chickens reveals frequent multiple infections
    • Lindström, I., N. Sundar, J. Lindh, et al 2008. Isolation and genotyping of Toxoplasma gondii from Ugandan chickens reveals frequent multiple infections. Parasitology 135: 39-45.
    • (2008) Parasitology , vol.135 , pp. 39-45
    • Lindström, I.1    Sundar, N.2    Lindh, J.3
  • 8
    • 80052297406 scopus 로고    scopus 로고
    • Genetic characterisation of Toxoplasma gondii in wildlife from North America revealed widespread and high prevalence of the fourth clonal type
    • Dubey, J.P., G.V. Velmurugan, C. Rajendran, et al 2011. Genetic characterisation of Toxoplasma gondii in wildlife from North America revealed widespread and high prevalence of the fourth clonal type. Int. J. Parasitol. 41: 1139-1147.
    • (2011) Int. J. Parasitol. , vol.41 , pp. 1139-1147
    • Dubey, J.P.1    Velmurugan, G.V.2    Rajendran, C.3
  • 9
    • 57649225511 scopus 로고    scopus 로고
    • ESCMID Study Group on Clinical Parasitology
    • Prevention of toxoplasmosis in transplant patients
    • Derouin, F., H. Pelloux; ESCMID Study Group on Clinical Parasitology 2008. Prevention of toxoplasmosis in transplant patients. Clin. Microbiol. Infect. 14: 1089-1101.
    • (2008) Clin. Microbiol. Infect. , vol.14 , pp. 1089-1101
    • Derouin, F.1    Pelloux, H.2
  • 10
    • 51449108123 scopus 로고    scopus 로고
    • Control of the risk of human toxoplasmosis transmitted by meat
    • Kijlstra, A. & E. Jongert 2008. Control of the risk of human toxoplasmosis transmitted by meat. Int. J. Parasitol. 38: 1359-1370.
    • (2008) Int. J. Parasitol. , vol.38 , pp. 1359-1370
    • Kijlstra, A.1    Jongert, E.2
  • 11
    • 0031958697 scopus 로고    scopus 로고
    • Structures of Toxoplasma gondii tachyzoites, bradyzoites, and sporozoites and biology and development of tissue cysts
    • Dubey, J.P., D.S. Lindsay & C.A. Speer 1998. Structures of Toxoplasma gondii tachyzoites, bradyzoites, and sporozoites and biology and development of tissue cysts. Clin. Microbiol. Rev. 11: 267-299.
    • (1998) Clin. Microbiol. Rev. , vol.11 , pp. 267-299
    • Dubey, J.P.1    Lindsay, D.S.2    Speer, C.A.3
  • 13
    • 0014271555 scopus 로고
    • The fine structure and reproduction of Toxoplasma gondii
    • Sheffield, H.G. & M.L. Melton 1968. The fine structure and reproduction of Toxoplasma gondii. J. Parasitol. 54: 209-226.
    • (1968) J. Parasitol. , vol.54 , pp. 209-226
    • Sheffield, H.G.1    Melton, M.L.2
  • 14
    • 0030294163 scopus 로고    scopus 로고
    • In the absence of endogenous IFN-γ, mice develop unimpaired IL-12 responses to Toxoplasma gondii while failing to control acute infection
    • Scharton-Kersten, T.M., T.A. Wynn, E.Y. Denkers, et al 1996. In the absence of endogenous IFN-γ, mice develop unimpaired IL-12 responses to Toxoplasma gondii while failing to control acute infection. J. Immunol. 157: 4045-4054.
    • (1996) J. Immunol. , vol.157 , pp. 4045-4054
    • Scharton-Kersten, T.M.1    Wynn, T.A.2    Denkers, E.Y.3
  • 15
    • 0027953833 scopus 로고
    • Experimental induction of bradyzoite-specific antigen expression and cyst formation by the RH strain of Toxoplasma gondii in vitro
    • Soête, M., D. Camus & J.F. Dubremetz 1994. Experimental induction of bradyzoite-specific antigen expression and cyst formation by the RH strain of Toxoplasma gondii in vitro. Exp. Parasitol. 78: 361-370.
    • (1994) Exp. Parasitol. , vol.78 , pp. 361-370
    • Soête, M.1    Camus, D.2    Dubremetz, J.F.3
  • 16
    • 0031692801 scopus 로고    scopus 로고
    • Toxoplasma gondii bradyzoites form spontaneously during sporozoite-initiated development
    • Jerome, M.E., J.R. Radke, W. Bohne, et al 1998. Toxoplasma gondii bradyzoites form spontaneously during sporozoite-initiated development. Infect. Immun. 66: 4838-4844.
    • (1998) Infect. Immun. , vol.66 , pp. 4838-4844
    • Jerome, M.E.1    Radke, J.R.2    Bohne, W.3
  • 18
    • 0031278877 scopus 로고    scopus 로고
    • Bradyzoite-induced murine toxoplasmosis: stage conversion, pathogenesis, and tissue cyst formation in mice fed bradyzoites of different strains of Toxoplasma gondii
    • Dubey, J.P. 1997. Bradyzoite-induced murine toxoplasmosis: stage conversion, pathogenesis, and tissue cyst formation in mice fed bradyzoites of different strains of Toxoplasma gondii. J. Eukaryot Microbiol. 44: 592-602.
    • (1997) J. Eukaryot Microbiol. , vol.44 , pp. 592-602
    • Dubey, J.P.1
  • 19
    • 0033563272 scopus 로고    scopus 로고
    • Intraepithelial lymphocytes traffic to the intestine and enhance resistance to Toxoplasma gondii oral infection
    • Buzoni-Gatel, D., H. Debbabi, M. Moretto, et al 1999. Intraepithelial lymphocytes traffic to the intestine and enhance resistance to Toxoplasma gondii oral infection. J. Immunol. 162: 5846-5852.
    • (1999) J. Immunol. , vol.162 , pp. 5846-5852
    • Buzoni-Gatel, D.1    Debbabi, H.2    Moretto, M.3
  • 20
    • 30144432329 scopus 로고    scopus 로고
    • CD11c- and CD11b-expressing mouse leukocytes transport single Toxoplasma gondii tachyzoites to the brain
    • Courret, N., S. Darche, P. Sonigo, et al 2006. CD11c- and CD11b-expressing mouse leukocytes transport single Toxoplasma gondii tachyzoites to the brain. Blood 107: 309-316.
    • (2006) Blood , vol.107 , pp. 309-316
    • Courret, N.1    Darche, S.2    Sonigo, P.3
  • 21
    • 0029016818 scopus 로고
    • Invasion of Toxoplasma gondii occurs by active penetration of the host cell
    • Morisaki, J.H., J.E. Heuser & L.D. Sibley 1995. Invasion of Toxoplasma gondii occurs by active penetration of the host cell. J. Cell Sci. 108: 2457-2464.
    • (1995) J. Cell Sci. , vol.108 , pp. 2457-2464
    • Morisaki, J.H.1    Heuser, J.E.2    Sibley, L.D.3
  • 22
    • 0013975252 scopus 로고
    • A cinematographic study of the penetration of cultured cells by Toxoplasma gondii
    • Hirai, K., K. Hirato & R. Yanagawa 1966. A cinematographic study of the penetration of cultured cells by Toxoplasma gondii. Jpn J. Vet. Res. 14: 81-90.
    • (1966) Jpn J. Vet. Res. , vol.14 , pp. 81-90
    • Hirai, K.1    Hirato, K.2    Yanagawa, R.3
  • 23
    • 0032128434 scopus 로고    scopus 로고
    • Advances in the life cycle of Toxoplasma gondii
    • Dubey, J.P. 1998. Advances in the life cycle of Toxoplasma gondii. Int. J. Parasitol. 28: 1019-1024.
    • (1998) Int. J. Parasitol. , vol.28 , pp. 1019-1024
    • Dubey, J.P.1
  • 24
    • 0029796640 scopus 로고    scopus 로고
    • Attachment of Toxoplasma gondii to host cells is host cell cycle dependent
    • Grimwood, J., J.R. Mineo & L.H. Kasper 1996. Attachment of Toxoplasma gondii to host cells is host cell cycle dependent. Infect. Immun. 64: 4099-4104.
    • (1996) Infect. Immun. , vol.64 , pp. 4099-4104
    • Grimwood, J.1    Mineo, J.R.2    Kasper, L.H.3
  • 25
    • 42149153850 scopus 로고    scopus 로고
    • Infection with Toxoplasma gondii results in dysregulation of the host cell cycle
    • Molestina, R.E., N. El-Guendy & A.P. Sinai 2008. Infection with Toxoplasma gondii results in dysregulation of the host cell cycle. Cell Microbiol. 10: 1153-1165.
    • (2008) Cell Microbiol. , vol.10 , pp. 1153-1165
    • Molestina, R.E.1    El-Guendy, N.2    Sinai, A.P.3
  • 26
    • 0344851907 scopus 로고    scopus 로고
    • Kinetics of the initial rounds of cell division of Toxoplasma gondii
    • Woodmansee, D.B. 2003. Kinetics of the initial rounds of cell division of Toxoplasma gondii. J. Parasitol. 89: 895-898.
    • (2003) J. Parasitol. , vol.89 , pp. 895-898
    • Woodmansee, D.B.1
  • 27
    • 0031853577 scopus 로고    scopus 로고
    • Toxoplasma gondii: an ultrastructural study of host-cell invasion by the bradyzoite stage
    • Sasono, P.M. & J.E. Smith 1998. Toxoplasma gondii: an ultrastructural study of host-cell invasion by the bradyzoite stage. Parasitol. Res. 84: 640-645.
    • (1998) Parasitol. Res. , vol.84 , pp. 640-645
    • Sasono, P.M.1    Smith, J.E.2
  • 28
    • 10744227649 scopus 로고    scopus 로고
    • Molecular mimicry of a CCR5 binding-domain in the microbial activation of dendritic cells
    • Aliberti, J., J.G. Valenzuela, V.B. Carruthers, et al 2003. Molecular mimicry of a CCR5 binding-domain in the microbial activation of dendritic cells. Nat. Immunol. 4: 485-490.
    • (2003) Nat. Immunol. , vol.4 , pp. 485-490
    • Aliberti, J.1    Valenzuela, J.G.2    Carruthers, V.B.3
  • 29
    • 63149149461 scopus 로고    scopus 로고
    • The Toxoplasma gondii-shuttling function of dendritic cells is linked to the parasite genotype
    • Lambert, H., P.P. Vutova, W.C. Adams, et al 2009. The Toxoplasma gondii-shuttling function of dendritic cells is linked to the parasite genotype. Infect. Immun. 77: 1679-1688.
    • (2009) Infect. Immun. , vol.77 , pp. 1679-1688
    • Lambert, H.1    Vutova, P.P.2    Adams, W.C.3
  • 30
    • 15944368914 scopus 로고    scopus 로고
    • Transepithelial migration of Toxoplasma gondii involves an interaction of intercellular adhesion molecule 1 (ICAM-1) with the parasite adhesin MIC2
    • Barragan, A., F. Brossier & L.D. Sibley 2005. Transepithelial migration of Toxoplasma gondii involves an interaction of intercellular adhesion molecule 1 (ICAM-1) with the parasite adhesin MIC2. Cell Microbiol. 7: 561-568.
    • (2005) Cell Microbiol. , vol.7 , pp. 561-568
    • Barragan, A.1    Brossier, F.2    Sibley, L.D.3
  • 31
    • 0028305138 scopus 로고
    • Dynamics of cadherin/catenin complex formation: novel protein interactions and pathways of complex assembly
    • Hinck, L., I.S. Näthke, J. Papkoff & W.J. Nelson 1994. Dynamics of cadherin/catenin complex formation: novel protein interactions and pathways of complex assembly. J. Cell Biol. 125: 1327-1340.
    • (1994) J. Cell Biol. , vol.125 , pp. 1327-1340
    • Hinck, L.1    Näthke, I.S.2    Papkoff, J.3    Nelson, W.J.4
  • 32
    • 0026687386 scopus 로고
    • Plakoglobin, or an 83-kD homologue distinct from β-catenin, interacts with E-cadherin and N-cadherin
    • Knudsen, K.A. & M.J. Wheelock 1992. Plakoglobin, or an 83-kD homologue distinct from β-catenin, interacts with E-cadherin and N-cadherin. J. Cell Biol. 118: 671-679.
    • (1992) J. Cell Biol. , vol.118 , pp. 671-679
    • Knudsen, K.A.1    Wheelock, M.J.2
  • 33
    • 0033605347 scopus 로고    scopus 로고
    • Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and α catenin
    • Itoh, M., K. Morita & S. Tsukita 1999. Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and α catenin. J. Biol. Chem. 274: 5981-5986.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5981-5986
    • Itoh, M.1    Morita, K.2    Tsukita, S.3
  • 34
    • 0034665316 scopus 로고    scopus 로고
    • ICAM-1-coupled cytoskeletal rearrangements and transendothelial lymphocyte migration involve intracellular calcium signaling in brain endothelial cell lines
    • Etienne-Manneville, S., J.B. Manneville, P. Adamson, et al 2000. ICAM-1-coupled cytoskeletal rearrangements and transendothelial lymphocyte migration involve intracellular calcium signaling in brain endothelial cell lines. J. Immunol. 165: 3375-3383.
    • (2000) J. Immunol. , vol.165 , pp. 3375-3383
    • Etienne-Manneville, S.1    Manneville, J.B.2    Adamson, P.3
  • 35
    • 0023644247 scopus 로고
    • Purified intercellular adhesion molecule-1 (ICAM-1) is a ligand for lymphocyte function-associated antigen 1 (LFA-1)
    • Marlin, S.D. & T.A. Springer 1987. Purified intercellular adhesion molecule-1 (ICAM-1) is a ligand for lymphocyte function-associated antigen 1 (LFA-1). Cell 51: 813-819.
    • (1987) Cell , vol.51 , pp. 813-819
    • Marlin, S.D.1    Springer, T.A.2
  • 36
    • 7844228766 scopus 로고    scopus 로고
    • Activated T-lymphocytes express occludin, a component of tight junctions
    • Alexander, J.S., T. Dayton, C. Davis, et al 1998. Activated T-lymphocytes express occludin, a component of tight junctions. Inflammation 22: 573-582.
    • (1998) Inflammation , vol.22 , pp. 573-582
    • Alexander, J.S.1    Dayton, T.2    Davis, C.3
  • 37
    • 18844429991 scopus 로고    scopus 로고
    • Intraepithelial lymphocytes express junctional molecules in murine small intestine
    • Inagaki-Ohara, K., A. Sawaguchi, T. Suganuma, et al 2005. Intraepithelial lymphocytes express junctional molecules in murine small intestine. Biochem. Biophys. Res. Commun. 331: 977-983.
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 977-983
    • Inagaki-Ohara, K.1    Sawaguchi, A.2    Suganuma, T.3
  • 38
    • 0035321325 scopus 로고    scopus 로고
    • Dendritic cells express tight junction proteins and penetrate gut epithelial monolayers to sample bacteria
    • Rescigno, M., M. Urbano, B. Valzasina, et al 2001. Dendritic cells express tight junction proteins and penetrate gut epithelial monolayers to sample bacteria. Nat. Immunol. 2: 361-367.
    • (2001) Nat. Immunol. , vol.2 , pp. 361-367
    • Rescigno, M.1    Urbano, M.2    Valzasina, B.3
  • 39
    • 0030737802 scopus 로고    scopus 로고
    • Time lapse video microscopy and ultrastructure of penetrating sporozoites, types 1 and 2 parasitophorous vacuoles, and the transformation of sporozoites to tachyzoites of the VEG strain of Toxoplasma gondii
    • Speer, C.A., J.P. Dubey, J.A. Blixt & K. Prokop 1997. Time lapse video microscopy and ultrastructure of penetrating sporozoites, types 1 and 2 parasitophorous vacuoles, and the transformation of sporozoites to tachyzoites of the VEG strain of Toxoplasma gondii. J. Parasitol. 83: 565-574.
    • (1997) J. Parasitol. , vol.83 , pp. 565-574
    • Speer, C.A.1    Dubey, J.P.2    Blixt, J.A.3    Prokop, K.4
  • 41
    • 33748124825 scopus 로고    scopus 로고
    • Intraepithelial γδ+ lymphocytes maintain the integrity of intestinal epithelial tight junctions in response to infection
    • Dalton, J.E., S.M. Cruickshank, C.E. Egan, et al 2006. Intraepithelial γδ+ lymphocytes maintain the integrity of intestinal epithelial tight junctions in response to infection. Gastroenterology 131: 818-829.
    • (2006) Gastroenterology , vol.131 , pp. 818-829
    • Dalton, J.E.1    Cruickshank, S.M.2    Egan, C.E.3
  • 42
    • 84862856007 scopus 로고    scopus 로고
    • The interactions of Toxoplasma gondii with epithelial tight junctions. Ph.D. thesis, University of East Anglia
    • Weight, C. 2011. The interactions of Toxoplasma gondii with epithelial tight junctions. Ph.D. thesis, University of East Anglia
    • (2011)
    • Weight, C.1
  • 43
    • 0037087260 scopus 로고    scopus 로고
    • Lamina propria CD4+ T lymphocytes synergize with murine intestinal epithelial cells to enhance proinflammatory response against an intracellular pathogen
    • Mennechet, F.J.D., L.H. Kasper, N. Rachinel, et al 2002. Lamina propria CD4+ T lymphocytes synergize with murine intestinal epithelial cells to enhance proinflammatory response against an intracellular pathogen. J. Immunol. 168: 2988-2996.
    • (2002) J. Immunol. , vol.168 , pp. 2988-2996
    • Mennechet, F.J.D.1    Kasper, L.H.2    Rachinel, N.3
  • 44
    • 78650042696 scopus 로고    scopus 로고
    • Regulation of chemokine responses in intestinal epithelial cells by stress and Toxoplasma gondii infection
    • Gopal, R., D. Birdsell & F.P. Monroy 2011. Regulation of chemokine responses in intestinal epithelial cells by stress and Toxoplasma gondii infection. Parasite Immunol. 33: 12-24.
    • (2011) Parasite Immunol. , vol.33 , pp. 12-24
    • Gopal, R.1    Birdsell, D.2    Monroy, F.P.3
  • 45
    • 0027416808 scopus 로고
    • Rat intestinal epithelial cell line IEC-6 is activated by recombinant interferon-gamma to inhibit replication of the coccidian Toxoplasma gondii
    • Dimier, I.H. & D.T. Bout 1993. Rat intestinal epithelial cell line IEC-6 is activated by recombinant interferon-gamma to inhibit replication of the coccidian Toxoplasma gondii. Eur. J. Immunol. 23: 981-983.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 981-983
    • Dimier, I.H.1    Bout, D.T.2
  • 46
    • 0442329280 scopus 로고    scopus 로고
    • Toxoplasma gondii: changes of transepithelial ion transport in infected HT29/B6 cell monolayers
    • Kowalik, S., W. Clauss & H. Zahner 2004. Toxoplasma gondii: changes of transepithelial ion transport in infected HT29/B6 cell monolayers. Parasitol. Res. 92: 152-158.
    • (2004) Parasitol. Res. , vol.92 , pp. 152-158
    • Kowalik, S.1    Clauss, W.2    Zahner, H.3
  • 47
    • 0031949214 scopus 로고    scopus 로고
    • The surface of Toxoplasma tachyzoites is dominated by a family of glycosylphosphatidylinositol-anchored antigens related to SAG1
    • Manger, I.D., A.B. Hehl & J.C. Boothroyd 1998. The surface of Toxoplasma tachyzoites is dominated by a family of glycosylphosphatidylinositol-anchored antigens related to SAG1. Infect. Immun. 66: 2237-2244.
    • (1998) Infect. Immun. , vol.66 , pp. 2237-2244
    • Manger, I.D.1    Hehl, A.B.2    Boothroyd, J.C.3
  • 48
    • 0026489950 scopus 로고
    • Laminin on Toxoplasma gondii mediates parasite binding to the β1 integrin receptor α6β1 on human foreskin fibroblasts and Chinese hamster ovary cells
    • Furtado, G.C., Y. Cao & K.A. Joiner 1992b. Laminin on Toxoplasma gondii mediates parasite binding to the β1 integrin receptor α6β1 on human foreskin fibroblasts and Chinese hamster ovary cells. Infect. Immun. 60: 4925-4931.
    • (1992) Infect. Immun. , vol.60 , pp. 4925-4931
    • Furtado, G.C.1    Cao, Y.2    Joiner, K.A.3
  • 49
    • 0026629423 scopus 로고
    • Laminin enhances binding of Toxoplasma gondii tachyzoites to J774 murine macrophage cells
    • Furtado, G.C., M. Slowik, H.K. Kleinman & K.A. Joiner 1992a. Laminin enhances binding of Toxoplasma gondii tachyzoites to J774 murine macrophage cells. Infect. Immun. 60: 2337-2342.
    • (1992) Infect. Immun. , vol.60 , pp. 2337-2342
    • Furtado, G.C.1    Slowik, M.2    Kleinman, H.K.3    Joiner, K.A.4
  • 50
    • 0027246020 scopus 로고
    • Antibodies to Toxoplasma gondii major surface protein (SAG-1, P30) inhibit infection of host cells and are produced in murine intestine after peroral infection
    • Mineo, J.R., R. McLeod, D. Mack, et al 1993. Antibodies to Toxoplasma gondii major surface protein (SAG-1, P30) inhibit infection of host cells and are produced in murine intestine after peroral infection. J. Immunol. 150: 3951-3964.
    • (1993) J. Immunol. , vol.150 , pp. 3951-3964
    • Mineo, J.R.1    McLeod, R.2    Mack, D.3
  • 51
    • 77958515323 scopus 로고    scopus 로고
    • Binding of Toxoplasma gondii glycosylphosphatidylinositols to galectin-3 is required for their recognition by macrophages
    • Debierre-Grockiego, F., S. Niehus, B. Coddeville, et al 2010. Binding of Toxoplasma gondii glycosylphosphatidylinositols to galectin-3 is required for their recognition by macrophages. J. Biol. Chem. 285: 32744-32750.
    • (2010) J. Biol. Chem. , vol.285 , pp. 32744-32750
    • Debierre-Grockiego, F.1    Niehus, S.2    Coddeville, B.3
  • 52
    • 33644666110 scopus 로고    scopus 로고
    • A novel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex
    • Saouros, S., B. Edwards-Jones, M. Reiss, et al 2005. A novel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex. J. Biol. Chem. 280: 38583-38591.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38583-38591
    • Saouros, S.1    Edwards-Jones, B.2    Reiss, M.3
  • 53
    • 0032528078 scopus 로고    scopus 로고
    • Host cell surface sialic acid residues are involved on the process of penetration of Toxoplasma gondii into mammalian cells
    • Monteiro, V.G., C.P. Soares & W. de Souza 1998. Host cell surface sialic acid residues are involved on the process of penetration of Toxoplasma gondii into mammalian cells. FEMS Microbiol. Lett. 164: 323-327.
    • (1998) FEMS Microbiol. Lett. , vol.164 , pp. 323-327
    • Monteiro, V.G.1    Soares, C.P.2    de Souza, W.3
  • 54
    • 0034907082 scopus 로고    scopus 로고
    • The surface antigen SAG3 mediates the attachment of Toxoplasma gondii to cell-surface proteoglycans
    • Jacquet, A., L. Coulon, J.D. Nève, et al 2001. The surface antigen SAG3 mediates the attachment of Toxoplasma gondii to cell-surface proteoglycans. Mol. Biochem. Parasitol. 116: 35-44.
    • (2001) Mol. Biochem. Parasitol. , vol.116 , pp. 35-44
    • Jacquet, A.1    Coulon, L.2    Nève, J.D.3
  • 55
    • 0343517492 scopus 로고    scopus 로고
    • Toxoplasma gondii uses sulfated proteoglycans for substrate and host cell attachment
    • Carruthers, V.B., S. Håkansson, O.K. Giddings & L.D. Sibley 2000. Toxoplasma gondii uses sulfated proteoglycans for substrate and host cell attachment. Infect. Immun. 68: 4005-4011.
    • (2000) Infect. Immun. , vol.68 , pp. 4005-4011
    • Carruthers, V.B.1    Håkansson, S.2    Giddings, O.K.3    Sibley, L.D.4
  • 56
    • 76249095009 scopus 로고    scopus 로고
    • Members of a novel protein family containing microneme adhesive repeat domains act as sialic acid-binding lectins during host cell invasion by apicomplexan parasites
    • Friedrich, N., J.M. Santos, Y. Liu, et al 2010. Members of a novel protein family containing microneme adhesive repeat domains act as sialic acid-binding lectins during host cell invasion by apicomplexan parasites. J. Biol. Chem. 285: 2064-2076.
    • (2010) J. Biol. Chem. , vol.285 , pp. 2064-2076
    • Friedrich, N.1    Santos, J.M.2    Liu, Y.3
  • 57
    • 0037128925 scopus 로고    scopus 로고
    • A novel polymer of tubulin forms the conoid of Toxoplasma gondii
    • Hu, K., D.S. Roos & J.M. Murray 2002. A novel polymer of tubulin forms the conoid of Toxoplasma gondii. J. Cell. Biol. 156: 1039-1050.
    • (2002) J. Cell. Biol. , vol.156 , pp. 1039-1050
    • Hu, K.1    Roos, D.S.2    Murray, J.M.3
  • 58
    • 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
    • Mordue, D.G., N. Desai, M. Dustin & L.D. Sibley 1999. 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: 1783-1792.
    • (1999) J. Exp. Med. , vol.190 , pp. 1783-1792
    • Mordue, D.G.1    Desai, N.2    Dustin, M.3    Sibley, L.D.4
  • 59
    • 0343162619 scopus 로고    scopus 로고
    • Time-lapse video microscopy of gliding motility in Toxoplasma gondii reveals a novel, biphasic mechanism of cell locomotion
    • Håkansson, S., H. Morisaki, J. Heuser & L.D. Sibley 1999. Time-lapse video microscopy of gliding motility in Toxoplasma gondii reveals a novel, biphasic mechanism of cell locomotion. Mol. Biol. Cell. 10: 3539-3547.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 3539-3547
    • Håkansson, S.1    Morisaki, H.2    Heuser, J.3    Sibley, L.D.4
  • 60
    • 0030770219 scopus 로고    scopus 로고
    • Participation of myosin in gliding motility and host cell invasion by Toxoplasma gondii
    • Dobrowolski, J.M., V.B. Carruthers & L.D. Sibley 1997. Participation of myosin in gliding motility and host cell invasion by Toxoplasma gondii. Mol. Microbiol. 26: 163-173.
    • (1997) Mol. Microbiol. , vol.26 , pp. 163-173
    • Dobrowolski, J.M.1    Carruthers, V.B.2    Sibley, L.D.3
  • 61
    • 0029869791 scopus 로고    scopus 로고
    • Toxoplasma invasion of mammalian cells is powered by the actin cytoskeleton of the parasite
    • Dobrowolski, J.M. & L.D. Sibley 1996. Toxoplasma invasion of mammalian cells is powered by the actin cytoskeleton of the parasite. Cell 84: 933-939.
    • (1996) Cell , vol.84 , pp. 933-939
    • Dobrowolski, J.M.1    Sibley, L.D.2
  • 62
    • 0035074932 scopus 로고    scopus 로고
    • Calmodulin distribution and the actomyosin cytoskeleton in Toxoplasma gondii
    • Pezzella-D'Alessandro, N., H.L. Moal, A. Bonhomme, et al 2001. Calmodulin distribution and the actomyosin cytoskeleton in Toxoplasma gondii. J. Histochem. Cytochem. 49: 445-454.
    • (2001) J. Histochem. Cytochem. , vol.49 , pp. 445-454
    • Pezzella-D'Alessandro, N.1    Moal, H.L.2    Bonhomme, A.3
  • 63
    • 0037328668 scopus 로고    scopus 로고
    • Actin filament polymerization regulates gliding motility by apicomplexan parasites
    • Wetzel, D.M., S. Håkansson, K. Hu, et al 2003. Actin filament polymerization regulates gliding motility by apicomplexan parasites. Mol. Biol. Cell 14: 396-406.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 396-406
    • Wetzel, D.M.1    Håkansson, S.2    Hu, K.3
  • 64
    • 61849132162 scopus 로고    scopus 로고
    • Host cell entry by apicomplexa parasites requires actin polymerization in the host cell
    • Gonzalez, V., A. Combe, V. David, et al 2009. Host cell entry by apicomplexa parasites requires actin polymerization in the host cell. Cell Host Microbe 5: 259-272.
    • (2009) Cell Host Microbe , vol.5 , pp. 259-272
    • Gonzalez, V.1    Combe, A.2    David, V.3
  • 65
    • 71049186393 scopus 로고    scopus 로고
    • Dynamin inhibitor impairs Toxoplasma gondii invasion
    • Caldas, L.A., M. Attias & W. de Souza 2009. Dynamin inhibitor impairs Toxoplasma gondii invasion. FEMS Microbiol. Lett. 301: 103-108.
    • (2009) FEMS Microbiol. Lett. , vol.301 , pp. 103-108
    • Caldas, L.A.1    Attias, M.2    de Souza, W.3
  • 66
    • 32544432516 scopus 로고    scopus 로고
    • Tight junctions: molecular architecture and function
    • Aijaz, S., M.S. Balda & K. Matter 2006. Tight junctions: molecular architecture and function. Int. Rev. Cytol. 248: 261-298.
    • (2006) Int. Rev. Cytol. , vol.248 , pp. 261-298
    • Aijaz, S.1    Balda, M.S.2    Matter, K.3
  • 67
    • 0030596197 scopus 로고    scopus 로고
    • The MIC1 microneme protein of Toxoplasma gondii contains a duplicated receptor-like domain and binds to host cell surface
    • Fourmaux, M.N., A. Achbarou, O. Mercereau-Puijalon, et al 1996. The MIC1 microneme protein of Toxoplasma gondii contains a duplicated receptor-like domain and binds to host cell surface. Mol. Biochem. Parasitol. 83: 201-210.
    • (1996) Mol. Biochem. Parasitol. , vol.83 , pp. 201-210
    • Fourmaux, M.N.1    Achbarou, A.2    Mercereau-Puijalon, O.3
  • 68
    • 0036473089 scopus 로고    scopus 로고
    • A family of transmembrane microneme proteins of Toxoplasma gondii contain EGF-like domains and function as escorters
    • Meissner, M., M. Reiss, N. Viebig, et al 2002. A family of transmembrane microneme proteins of Toxoplasma gondii contain EGF-like domains and function as escorters. J. Cell. Sci. 115: 563-574.
    • (2002) J. Cell. Sci. , vol.115 , pp. 563-574
    • Meissner, M.1    Reiss, M.2    Viebig, N.3
  • 69
    • 0031044707 scopus 로고    scopus 로고
    • Molecular characterisation of an expressed sequence tag locus of Toxoplasma gondii encoding the micronemal protein MIC2
    • Wan, K.L., V.B. Carruthers, L.D. Sibley & J.W. Ajioka 1997. Molecular characterisation of an expressed sequence tag locus of Toxoplasma gondii encoding the micronemal protein MIC2. Mol. Biochem. Parasitol. 84: 203-214.
    • (1997) Mol. Biochem. Parasitol. , vol.84 , pp. 203-214
    • Wan, K.L.1    Carruthers, V.B.2    Sibley, L.D.3    Ajioka, J.W.4
  • 70
    • 77951026559 scopus 로고    scopus 로고
    • Identification of the moving junction complex of Toxoplasma gondii: a collaboration between distinct secretory organelles
    • Alexander, D.L., J. Mital, G.E. Ward, et al 2005. Identification of the moving junction complex of Toxoplasma gondii: a collaboration between distinct secretory organelles. PLoS Pathog. 1: e17.
    • (2005) PLoS Pathog. , vol.1
    • Alexander, D.L.1    Mital, J.2    Ward, G.E.3
  • 71
    • 0032927424 scopus 로고    scopus 로고
    • Mobilization of intracellular calcium stimulates microneme discharge in Toxoplasma gondii
    • Carruthers, V.B. & L.D. Sibley 1999. Mobilization of intracellular calcium stimulates microneme discharge in Toxoplasma gondii. Mol. Microbiol. 31: 421-428.
    • (1999) Mol. Microbiol. , vol.31 , pp. 421-428
    • Carruthers, V.B.1    Sibley, L.D.2
  • 72
    • 0041402826 scopus 로고    scopus 로고
    • Intracellular calcium stores in Toxoplasma gondii govern invasion of host cells
    • Lovett, J.L. & L.D. Sibley 2003. Intracellular calcium stores in Toxoplasma gondii govern invasion of host cells. J. Cell. Sci. 116: 3009-3016.
    • (2003) J. Cell. Sci. , vol.116 , pp. 3009-3016
    • Lovett, J.L.1    Sibley, L.D.2
  • 73
    • 0038558167 scopus 로고    scopus 로고
    • Rapid invasion of host cells by Toxoplasma requires secretion of the MIC2-M2AP adhesive protein complex
    • Huynh, M.H., K.E. Rabenau, J.M. Harper, et al 2003. Rapid invasion of host cells by Toxoplasma requires secretion of the MIC2-M2AP adhesive protein complex. EMBO J. 22: 2082-2090.
    • (2003) EMBO J. , vol.22 , pp. 2082-2090
    • Huynh, M.H.1    Rabenau, K.E.2    Harper, J.M.3
  • 74
    • 67649537958 scopus 로고    scopus 로고
    • MIC6 associates with aldolase in host cell invasion by Toxoplasma gondii
    • Zheng, B., A. He, M. Gan, et al 2009. MIC6 associates with aldolase in host cell invasion by Toxoplasma gondii. Parasitol Res. 105: 441-445.
    • (2009) Parasitol Res. , vol.105 , pp. 441-445
    • Zheng, B.1    He, A.2    Gan, M.3
  • 75
    • 0035830936 scopus 로고    scopus 로고
    • The toxoplasma micronemal protein MIC4 is an adhesin composed of six conserved apple domains
    • Brecht, S., V.B. Carruthers, D.J. Ferguson, et al 2001. The toxoplasma micronemal protein MIC4 is an adhesin composed of six conserved apple domains. J. Biol. Chem. 276: 4119-4127.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4119-4127
    • Brecht, S.1    Carruthers, V.B.2    Ferguson, D.J.3
  • 76
    • 26644451857 scopus 로고    scopus 로고
    • Proteomic analysis of rhoptry organelles reveals many novel constituents for host-parasite interactions in Toxoplasma gondii
    • Bradley, P.J., C. Ward, S.J. Cheng, et al 2005. Proteomic analysis of rhoptry organelles reveals many novel constituents for host-parasite interactions in Toxoplasma gondii. J. Biol. Chem. 280: 34245-34258.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34245-34258
    • Bradley, P.J.1    Ward, C.2    Cheng, S.J.3
  • 77
    • 79952231758 scopus 로고    scopus 로고
    • The RON2-AMA1 interaction is a critical step in moving junction-dependent invasion by apicomplexan parasites
    • Lamarque, M., S. Besteiro, J. Papoin, et al 2011. The RON2-AMA1 interaction is a critical step in moving junction-dependent invasion by apicomplexan parasites. PLoS Pathog. 7: e1001276.
    • (2011) PLoS Pathog. , vol.7
    • Lamarque, M.1    Besteiro, S.2    Papoin, J.3
  • 78
    • 62149116563 scopus 로고    scopus 로고
    • Novel components of the Apicomplexan moving junction reveal conserved and coccidia-restricted elements
    • Straub, K.W., S.J. Cheng, C.S. Sohn & P.J. Bradley 2009. Novel components of the Apicomplexan moving junction reveal conserved and coccidia-restricted elements. Cell Microbiol. 11: 590-603.
    • (2009) Cell Microbiol. , vol.11 , pp. 590-603
    • Straub, K.W.1    Cheng, S.J.2    Sohn, C.S.3    Bradley, P.J.4
  • 79
    • 79953287282 scopus 로고    scopus 로고
    • The moving junction protein RON8 facilitates firm attachment and host cell invasion in Toxoplasma gondii
    • Straub, K.W., E.D. Peng, B.E. Hajagos, et al 2011. The moving junction protein RON8 facilitates firm attachment and host cell invasion in Toxoplasma gondii. PLoS Pathog. 7: e1002007.
    • (2011) PLoS Pathog. , vol.7
    • Straub, K.W.1    Peng, E.D.2    Hajagos, B.E.3
  • 80
    • 33847332992 scopus 로고    scopus 로고
    • ROP18 is a rhoptry kinase controlling the intracellular proliferation of Toxoplasma gondii
    • Hajj, H.E., M. Lebrun, S.T. Arold, et al 2007. ROP18 is a rhoptry kinase controlling the intracellular proliferation of Toxoplasma gondii. PLoS Pathog. 3: e14.
    • (2007) PLoS Pathog. , vol.3
    • Hajj, H.E.1    Lebrun, M.2    Arold, S.T.3
  • 81
    • 33845705275 scopus 로고    scopus 로고
    • A secreted serine-threonine kinase determines virulence in the eukaryotic pathogen Toxoplasma gondii
    • Taylor, S., A. Barragan, C. Su, et al 2006. A secreted serine-threonine kinase determines virulence in the eukaryotic pathogen Toxoplasma gondii. Science 314: 1776-1780.
    • (2006) Science , vol.314 , pp. 1776-1780
    • Taylor, S.1    Barragan, A.2    Su, C.3
  • 82
    • 33846322896 scopus 로고    scopus 로고
    • Toxoplasma co-opts host gene expression by injection of a polymorphic kinase homologue
    • Saeij, J.P.J., S. Coller, J.P. Boyle, et al 2007. Toxoplasma co-opts host gene expression by injection of a polymorphic kinase homologue. Nature 445: 324-327.
    • (2007) Nature , vol.445 , pp. 324-327
    • Saeij, J.P.J.1    Coller, S.2    Boyle, J.P.3
  • 83
    • 0036734602 scopus 로고    scopus 로고
    • Modulation of cellular cholesterol transport and homeostasis by Rab11
    • Hölttä-Vuori, M., K. Tanhuanpää, W. Möbius, et al 2002. Modulation of cellular cholesterol transport and homeostasis by Rab11. Mol. Biol. Cell. 13: 3107-3122.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 3107-3122
    • Hölttä-Vuori, M.1    Tanhuanpää, K.2    Möbius, W.3
  • 84
    • 0033980626 scopus 로고    scopus 로고
    • Toxofilin, a novel actin-binding protein from Toxoplasma gondii, sequesters actin monomers and caps actin filaments
    • Poupel, O., H. Boleti, S. Axisa, et al 2000. Toxofilin, a novel actin-binding protein from Toxoplasma gondii, sequesters actin monomers and caps actin filaments. Mol. Biol. Cell. 11: 355-368.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 355-368
    • Poupel, O.1    Boleti, H.2    Axisa, S.3
  • 85
    • 33846461190 scopus 로고    scopus 로고
    • Toxoplasma gondii targets a protein phosphatase 2C to the nuclei of infected host cells
    • Gilbert, L.A., S. Ravindran, J.M. Turetzky, et al 2007. Toxoplasma gondii targets a protein phosphatase 2C to the nuclei of infected host cells. Eukaryot. Cell 6: 73-83.
    • (2007) Eukaryot. Cell , vol.6 , pp. 73-83
    • Gilbert, L.A.1    Ravindran, S.2    Turetzky, J.M.3
  • 86
    • 69249223011 scopus 로고    scopus 로고
    • A Toxoplasma type 2C serine-threonine phosphatase is involved in parasite growth in the mammalian host cell
    • Jan, G., V. Delorme, N. Saksouk, et al. 2009. A Toxoplasma type 2C serine-threonine phosphatase is involved in parasite growth in the mammalian host cell. Microbes Infect. 11: 935-945.
    • (2009) Microbes Infect. , vol.11 , pp. 935-945
    • Jan, G.1    Delorme, V.2    Saksouk, N.3
  • 87
    • 0036213194 scopus 로고    scopus 로고
    • A role for Toxoplasma gondii type 1 ser/thr protein phosphatase in host cell invasion
    • Delorme, V., A. Garcia, X. Cayla & I. Tardieux 2002. A role for Toxoplasma gondii type 1 ser/thr protein phosphatase in host cell invasion. Microbes Infect. 4: 271-278.
    • (2002) Microbes Infect. , vol.4 , pp. 271-278
    • Delorme, V.1    Garcia, A.2    Cayla, X.3    Tardieux, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.