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Volumn 331, Issue 2, 2005, Pages 614-620

Host cell binding of GRA10, a novel, constitutively secreted dense granular protein from Toxoplasma gondii

Author keywords

Excretory secretory proteins; GRA10; Host cell binding; RGD motif; Toxoplasma gondii; Transmembrane domain

Indexed keywords

AMINO ACID DERIVATIVE; COMPLEMENTARY DNA; MEMBRANE PROTEIN; MONOCLONAL ANTIBODY; POLYPEPTIDE; PROTEIN GRA10; PROTOZOAL DNA; PROTOZOAL PROTEIN; UNCLASSIFIED DRUG;

EID: 18044388730     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.03.218     Document Type: Article
Times cited : (25)

References (48)
  • 2
    • 0026901767 scopus 로고
    • AIDS commentary:toxoplasmic encephalitis in AIDS
    • B.J. Luft, and J.S. Remington AIDS commentary:toxoplasmic encephalitis in AIDS Clin. Infect. Dis. 15 1992 211 222
    • (1992) Clin. Infect. Dis. , vol.15 , pp. 211-222
    • Luft, B.J.1    Remington, J.S.2
  • 4
    • 0030956863 scopus 로고    scopus 로고
    • Sequential protein secretion from three distinct organelles of Toxoplasma gondii accompanies invasion of human fibroblasts
    • V.B. Carruthers, and L.D. Sibley Sequential protein secretion from three distinct organelles of Toxoplasma gondii accompanies invasion of human fibroblasts Eur. J. Cell Biol. 73 1997 114 123
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 114-123
    • Carruthers, V.B.1    Sibley, L.D.2
  • 5
    • 0037071541 scopus 로고    scopus 로고
    • Secretory traffic in the eukaryotic parasite Toxoplasma gondii: Less is more
    • K.A. Joiner, and D.S. Roos Secretory traffic in the eukaryotic parasite Toxoplasma gondii: less is more J. Cell Biol. 157 2002 557 563
    • (2002) J. Cell Biol. , vol.157 , pp. 557-563
    • Joiner, K.A.1    Roos, D.S.2
  • 6
    • 0034141202 scopus 로고    scopus 로고
    • Differential sorting and post-secretory targeting of proteins in parasitic invasion
    • H.M. Ngo, H.C. Hoppe, and K.A. Joiner Differential sorting and post-secretory targeting of proteins in parasitic invasion Trends Cell Biol. 10 2000 67 72
    • (2000) Trends Cell Biol. , vol.10 , pp. 67-72
    • Ngo, H.M.1    Hoppe, H.C.2    Joiner, K.A.3
  • 8
    • 0033224351 scopus 로고    scopus 로고
    • Secretion of micronemal proteins is associated with Toxoplasma invasion of host cells
    • V.B. Carruthers, O.K. Giddings, and L.D. Sibley Secretion of micronemal proteins is associated with Toxoplasma invasion of host cells Cell. Microbiol. 1 1999 225 235
    • (1999) Cell. Microbiol. , vol.1 , pp. 225-235
    • Carruthers, V.B.1    Giddings, O.K.2    Sibley, L.D.3
  • 9
    • 0038558167 scopus 로고    scopus 로고
    • Rapid invasion of host cells by Toxoplasma requires secretion of the MIC2-M2P adhesive protein complex
    • M.H. Huynh, K.E. Rabenau, J.M. Harper, W.L. Beatty, L.D. Sibley, and V.B. Carruthers Rapid invasion of host cells by Toxoplasma requires secretion of the MIC2-M2P adhesive protein complex EMBO J. 22 2003 2082 2090
    • (2003) EMBO J. , vol.22 , pp. 2082-2090
    • Huynh, M.H.1    Rabenau, K.E.2    Harper, J.M.3    Beatty, W.L.4    Sibley, L.D.5    Carruthers, V.B.6
  • 10
    • 0037672558 scopus 로고    scopus 로고
    • Pleiotropic effect due to targeted depletion of secretory rhoptry protein ROP2 in Toxoplasma gondii
    • V. Nakaar, H.M. Ngo, E.P. Aaronson, I. Coppens, T.T. Stedman, and K.A. Joiner Pleiotropic effect due to targeted depletion of secretory rhoptry protein ROP2 in Toxoplasma gondii J. Cell Sci. 116 2003 2311 2320
    • (2003) J. Cell Sci. , vol.116 , pp. 2311-2320
    • Nakaar, V.1    Ngo, H.M.2    Aaronson, E.P.3    Coppens, I.4    Stedman, T.T.5    Joiner, K.A.6
  • 11
    • 3042557931 scopus 로고    scopus 로고
    • Are rhoptries in Apicomplexan parasites secretory granules or secretory lysosomal granules?
    • H.M. Ngo, M. Yang, and K.A. Joiner Are rhoptries in Apicomplexan parasites secretory granules or secretory lysosomal granules? Mol. Microbiol. 52 2004 1531 1541
    • (2004) Mol. Microbiol. , vol.52 , pp. 1531-1541
    • Ngo, H.M.1    Yang, M.2    Joiner, K.A.3
  • 12
    • 0035833263 scopus 로고    scopus 로고
    • The Toxoplasma gondii protein ROP2 mediates host organelle association with the parasitophorous vacuole membrane
    • A.P. Sainai, and K.A. Joiner The Toxoplasma gondii protein ROP2 mediates host organelle association with the parasitophorous vacuole membrane J. Cell Biol. 154 2001 95 108
    • (2001) J. Cell Biol. , vol.154 , pp. 95-108
    • Sainai, A.P.1    Joiner, K.A.2
  • 13
    • 0030221960 scopus 로고    scopus 로고
    • Rhoptry organelles of the Apicomplexa: Their role in host cell invasion and intracellular survival
    • T. Sam-Yellowe Rhoptry organelles of the Apicomplexa: their role in host cell invasion and intracellular survival Parasitol. Today 12 1996 308 316
    • (1996) Parasitol. Today , vol.12 , pp. 308-316
    • Sam-Yellowe, T.1
  • 15
    • 0031808982 scopus 로고    scopus 로고
    • The parasitophorous vacuole membrane surrounding Plasmodium and Toxoplasma: An unusual compartment in infected cells
    • K. Lingelbach, and K.A. Joiner The parasitophorous vacuole membrane surrounding Plasmodium and Toxoplasma: an unusual compartment in infected cells J. Cell Sci. 111 1998 1467 1475
    • (1998) J. Cell Sci. , vol.111 , pp. 1467-1475
    • Lingelbach, K.1    Joiner, K.A.2
  • 16
    • 0033593430 scopus 로고    scopus 로고
    • Constitutive calcium-independent release of Toxoplasma gondii dense granules occurs through the NSF/SNAP/SNARE/Rab machinery
    • S. Chaturvedi, H. Qi, D. Coleman, A. Rodriguez, P. Hanson, B. Striepen, D.S. Roos, and K.A. Joiner Constitutive calcium-independent release of Toxoplasma gondii dense granules occurs through the NSF/SNAP/SNARE/Rab machinery J. Biol. Chem. 274 1999 2424 2431
    • (1999) J. Biol. Chem. , vol.274 , pp. 2424-2431
    • Chaturvedi, S.1    Qi, H.2    Coleman, D.3    Rodriguez, A.4    Hanson, P.5    Striepen, B.6    Roos, D.S.7    Joiner, K.A.8
  • 17
    • 0035287252 scopus 로고    scopus 로고
    • Detection and characterization of excretory/secretory proteins from Toxoplasma gondii by monoclonal antibodies
    • E.S. Son, and H.W. Nam Detection and characterization of excretory/secretory proteins from Toxoplasma gondii by monoclonal antibodies Korean J. Parasitol. 39 2001 49 56
    • (2001) Korean J. Parasitol. , vol.39 , pp. 49-56
    • Son, E.S.1    Nam, H.W.2
  • 18
    • 0041384445 scopus 로고    scopus 로고
    • Molecular cloning of ribosomal P protein in Toxoplasma gondii and the availability to detect antibody against recombinant protein in toxoplasmosis patients
    • H.J. Ahn, S. Kim, and H.W. Nam Molecular cloning of ribosomal P protein in Toxoplasma gondii and the availability to detect antibody against recombinant protein in toxoplasmosis patients Korean J. Parasitol. 41 2003 89 96
    • (2003) Korean J. Parasitol. , vol.41 , pp. 89-96
    • Ahn, H.J.1    Kim, S.2    Nam, H.W.3
  • 19
    • 0242661627 scopus 로고    scopus 로고
    • Molecular cloning of the 82-kDa heat shock protein (HSP90) of Toxoplasma gondii associated with the entry into and growth in host cells
    • H.J. Ahn, S. Kim, and H.W. Nam Molecular cloning of the 82-kDa heat shock protein (HSP90) of Toxoplasma gondii associated with the entry into and growth in host cells Biochem. Biophys. Res. Commun. 311 2003 654 659
    • (2003) Biochem. Biophys. Res. Commun. , vol.311 , pp. 654-659
    • Ahn, H.J.1    Kim, S.2    Nam, H.W.3
  • 20
    • 0033256913 scopus 로고    scopus 로고
    • Western blot analysis of stray cat sera against Toxoplasma gondii and the diagnostic availability of monoclonal antibodies in sandwich-ELISA
    • W.M. Sohn, and H.W. Nam Western blot analysis of stray cat sera against Toxoplasma gondii and the diagnostic availability of monoclonal antibodies in sandwich-ELISA Korean J. Parasitol. 37 1999 249 256
    • (1999) Korean J. Parasitol. , vol.37 , pp. 249-256
    • Sohn, W.M.1    Nam, H.W.2
  • 21
    • 0035964868 scopus 로고    scopus 로고
    • Protease activity and host cell binding of the 42-kDa rhoptry protein from Toxoplasma gondii after secretion
    • H.J. Ahn, K.J. Song, E.S. Son, J.C. Shin, and H.W. Nam Protease activity and host cell binding of the 42-kDa rhoptry protein from Toxoplasma gondii after secretion Biochem. Biophys. Res. Commun. 287 2001 630 635
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 630-635
    • Ahn, H.J.1    Song, K.J.2    Son, E.S.3    Shin, J.C.4    Nam, H.W.5
  • 22
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte, and R.F. Doolittle A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157 1982 105 132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 23
    • 0024212067 scopus 로고    scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • M.A. Frohman, M.K. Dush, and G.R. Martin Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer Proc. Natl. Acad. Sci. USA 85 1998 8998 9002
    • (1998) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 24
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • C. Bordier Phase separation of integral membrane proteins in Triton X-114 solution J. Biol. Chem. 256 1981 1604 1607
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 25
    • 0024394362 scopus 로고
    • Context effects and inefficient initiation at non-AUG codons in eucaryotic cell-free translation systems
    • M. Kozak Context effects and inefficient initiation at non-AUG codons in eucaryotic cell-free translation systems Mol. Cell. Biol. 9 1989 5073 5080
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5073-5080
    • Kozak, M.1
  • 27
    • 0033990607 scopus 로고    scopus 로고
    • Identification and molecular characterization of GRA8, a novel, proline-rich, dense granule protein of Toxoplasma gondii
    • K.L. Carey, C.G. Donahue, and G.E. Ward Identification and molecular characterization of GRA8, a novel, proline-rich, dense granule protein of Toxoplasma gondii Mol. Biochem. Parasitol. 105 2002 25 37
    • (2002) Mol. Biochem. Parasitol. , vol.105 , pp. 25-37
    • Carey, K.L.1    Donahue, C.G.2    Ward, G.E.3
  • 28
    • 0028169529 scopus 로고
    • Dense granule organelles of Toxoplasma gondii: Their role in the host-parasite relationship
    • M.-F. Cesbron-Delauw Dense granule organelles of Toxoplasma gondii: their role in the host-parasite relationship Parasitol. Today 10 1994 293 296
    • (1994) Parasitol. Today , vol.10 , pp. 293-296
    • Cesbron-Delauw, M.-F.1
  • 29
    • 0029051349 scopus 로고
    • Biochemical and molecular characterization of nucleoside triphosphate hydrolase isozymes from the parasitic protozoan Toxoplasma gondii
    • T. Asai, S. Miura, L.D. Sibley, H. Okabayashi, and T. Takeuchi Biochemical and molecular characterization of nucleoside triphosphate hydrolase isozymes from the parasitic protozoan Toxoplasma gondii J. Biol. Chem. 270 1995 11391 11397
    • (1995) J. Biol. Chem. , vol.270 , pp. 11391-11397
    • Asai, T.1    Miura, S.2    Sibley, L.D.3    Okabayashi, H.4    Takeuchi, T.5
  • 30
    • 0038353220 scopus 로고    scopus 로고
    • The relationship between nucleoside triphosphate hydrolase (NTPase) isoform and Toxoplasma strain virulence in rat and human toxoplasmosis
    • M. Johnson, K. Broady, M.C. Angelici, and A. Johnson The relationship between nucleoside triphosphate hydrolase (NTPase) isoform and Toxoplasma strain virulence in rat and human toxoplasmosis Microbes Infect. 5 2003 797 806
    • (2003) Microbes Infect. , vol.5 , pp. 797-806
    • Johnson, M.1    Broady, K.2    Angelici, M.C.3    Johnson, A.4
  • 31
    • 0346668362 scopus 로고    scopus 로고
    • Functional analysis of Toxoplasma gondii protease inhibitor I
    • M.T. Morris, A. Coppin, S. Tomavo, and V.B. Carruthers Functional analysis of Toxoplasma gondii protease inhibitor I J. Biol. Chem. 277 2002 45259 45266
    • (2002) J. Biol. Chem. , vol.277 , pp. 45259-45266
    • Morris, M.T.1    Coppin, A.2    Tomavo, S.3    Carruthers, V.B.4
  • 33
    • 0342995731 scopus 로고    scopus 로고
    • The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process
    • H. Do, D. Falcone, J. Lin, D.W. Andrews, and A.E. Johnson The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process Cell 85 1996 369 378
    • (1996) Cell , vol.85 , pp. 369-378
    • Do, H.1    Falcone, D.2    Lin, J.3    Andrews, D.W.4    Johnson, A.E.5
  • 34
    • 0032521215 scopus 로고    scopus 로고
    • GRA7, an excretory 29 kDa Toxoplasma gondii dense granule antigen released by infected host cells
    • H.G. Fischer, S. Stachelhaus, M. Sahm, H.E. Meyer, and G. Reichmann GRA7, an excretory 29 kDa Toxoplasma gondii dense granule antigen released by infected host cells Mol. Biochem. Parasitol. 91 1998 251 262
    • (1998) Mol. Biochem. Parasitol. , vol.91 , pp. 251-262
    • Fischer, H.G.1    Stachelhaus, S.2    Sahm, M.3    Meyer, H.E.4    Reichmann, G.5
  • 35
    • 0028244837 scopus 로고
    • A soluble secretory protein of the intracellular parasite Toxoplasma gondii associates with the parasitophorous vacuole membrane through hydrophobic interactions
    • P.N. Ossorio, J.F. Dubremetz, and K.A. Joiner A soluble secretory protein of the intracellular parasite Toxoplasma gondii associates with the parasitophorous vacuole membrane through hydrophobic interactions J. Biol. Chem. 269 1994 15350 15357
    • (1994) J. Biol. Chem. , vol.269 , pp. 15350-15357
    • Ossorio, P.N.1    Dubremetz, J.F.2    Joiner, K.A.3
  • 36
    • 0028587841 scopus 로고
    • Cloning of a cDNA encoding the dense granule protein GRA3 from Toxoplasma gondii
    • D. Bermudes, J.F. Dubremetz, A. Achbarou, and K.A. Joiner Cloning of a cDNA encoding the dense granule protein GRA3 from Toxoplasma gondii Mol. Biochem. Parasitol. 68 1994 247 257
    • (1994) Mol. Biochem. Parasitol. , vol.68 , pp. 247-257
    • Bermudes, D.1    Dubremetz, J.F.2    Achbarou, A.3    Joiner, K.A.4
  • 38
    • 0030889496 scopus 로고    scopus 로고
    • Consensus sequence of translational initiation sites from Toxoplasma gondii genes
    • F. Seeber Consensus sequence of translational initiation sites from Toxoplasma gondii genes Parasitol. Res. 83 1997 309 311
    • (1997) Parasitol. Res. , vol.83 , pp. 309-311
    • Seeber, F.1
  • 39
    • 0028363745 scopus 로고
    • Isolation, cDNA sequences and biochemical characterization of the major cyclosporin-binding proteins of Toxoplasma gondii
    • K.P. High, K.A. Joiner, and R.E. Handschumacher Isolation, cDNA sequences and biochemical characterization of the major cyclosporin-binding proteins of Toxoplasma gondii J. Biol. Chem. 269 1994 9105 9112
    • (1994) J. Biol. Chem. , vol.269 , pp. 9105-9112
    • High, K.P.1    Joiner, K.A.2    Handschumacher, R.E.3
  • 40
    • 0032947846 scopus 로고    scopus 로고
    • Transmembrane insertion of the Toxoplasma gondii GRA5 protein occurs after soluble secretion into the host cell
    • L. Lecordier, C. Mercier, L.D. Sibley, and M.F. Cesbron-Delauw Transmembrane insertion of the Toxoplasma gondii GRA5 protein occurs after soluble secretion into the host cell Mol. Biol. Cell 10 1999 1277 1287
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1277-1287
    • Lecordier, L.1    Mercier, C.2    Sibley, L.D.3    Cesbron-Delauw, M.F.4
  • 41
    • 0027199059 scopus 로고
    • Kinetics and pattern of organelle exocytosis during Toxoplasma gondii/host-cell interaction
    • J.F. Dubremetz, A. Achbarou, D. Bermudes, and K.A. Joiner Kinetics and pattern of organelle exocytosis during Toxoplasma gondii/host-cell interaction Parasitol. Res. 79 1993 402 408
    • (1993) Parasitol. Res. , vol.79 , pp. 402-408
    • Dubremetz, J.F.1    Achbarou, A.2    Bermudes, D.3    Joiner, K.A.4
  • 42
    • 0030783010 scopus 로고    scopus 로고
    • Association of host cell endoplasmic reticulum and mitochondria with the Toxoplasma gondii parasitophorous vacuole membrane: A high affinity interaction
    • A.P. Sinai, P. Webster, and K.A. Joiner Association of host cell endoplasmic reticulum and mitochondria with the Toxoplasma gondii parasitophorous vacuole membrane: a high affinity interaction J. Cell Sci. 110 1997 2117 2128
    • (1997) J. Cell Sci. , vol.110 , pp. 2117-2128
    • Sinai, A.P.1    Webster, P.2    Joiner, K.A.3
  • 43
    • 0028115808 scopus 로고
    • The parasitophorous vacuole membrane surrounding intracellular Toxoplasma gondii functions as a molecular sieve
    • J.C. Schwab, C.J. Beckers, and K.A. Joiner The parasitophorous vacuole membrane surrounding intracellular Toxoplasma gondii functions as a molecular sieve Proc. Natl. Acad. Sci. USA 91 1994 509 513
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 509-513
    • Schwab, J.C.1    Beckers, C.J.2    Joiner, K.A.3
  • 44
    • 0032519416 scopus 로고    scopus 로고
    • Toxoplasma gondii-infected cells are resistant to multiple inducers of apoptosis
    • P.B. Nash, M.B. Purner, R.P. Leon, P. Clarke, R.C. Duke, and T.J. Curiel Toxoplasma gondii-infected cells are resistant to multiple inducers of apoptosis J. Immunol. 160 1998 1824 1830
    • (1998) J. Immunol. , vol.160 , pp. 1824-1830
    • Nash, P.B.1    Purner, M.B.2    Leon, R.P.3    Clarke, P.4    Duke, R.C.5    Curiel, T.J.6
  • 45
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • D.J. Leahy, I. Aukhil, and H.P. Erickson 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region Cell 84 1996 155 164
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 47
    • 0034177534 scopus 로고    scopus 로고
    • T-cell clones raised from chronically infected healthy humans by stimulation with Toxoplasma gondii excretory-secretory antigens cross-react with live tachyzoites: Characterization of the fine antigenic specificity of the clones and implications for vaccine development
    • I. Prigione, P. Facchetti, L. Lecordier, D. Deslee, S. Chiesa, M.F. Cesbron-Delauw, and V. Pistoia T-cell clones raised from chronically infected healthy humans by stimulation with Toxoplasma gondii excretory-secretory antigens cross-react with live tachyzoites: characterization of the fine antigenic specificity of the clones and implications for vaccine development J. Immunol. 164 2000 3741 3748
    • (2000) J. Immunol. , vol.164 , pp. 3741-3748
    • Prigione, I.1    Facchetti, P.2    Lecordier, L.3    Deslee, D.4    Chiesa, S.5    Cesbron-Delauw, M.F.6    Pistoia, V.7
  • 48
    • 0034919861 scopus 로고    scopus 로고
    • Towards the Toxoplasma gondii proteome: Position of 13 parasite excretory antigens on a standardized map of two-dimensionally separated tachyzoite proteins
    • H. Dlugonska, K. Dytnerska, G. Reichmann, S. Stachellhaus, and H.G. Fischer Towards the Toxoplasma gondii proteome: position of 13 parasite excretory antigens on a standardized map of two-dimensionally separated tachyzoite proteins Parasitol. Res. 87 2001 634 637
    • (2001) Parasitol. Res. , vol.87 , pp. 634-637
    • Dlugonska, H.1    Dytnerska, K.2    Reichmann, G.3    Stachellhaus, S.4    Fischer, H.G.5


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