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Volumn 65, Issue 1, 1997, Pages 78-88

Host cell heparan sulfate proteoglycans mediate attachment and entry of Listeria monocytogenes, and the listerial surface protein ActA is involved in heparan sulfate receptor recognition

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CELL SURFACE RECEPTOR; HEPARAN SULFATE; PROTEOHEPARAN SULFATE;

EID: 0031035594     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.65.1.78-88.1997     Document Type: Article
Times cited : (159)

References (75)
  • 1
    • 0027323898 scopus 로고
    • Role of complement component C1q in phagocytosis of Listeria monocytogenes by murine macrophage-like cell lines
    • Alvarez-Domínguez, C., E. Carrasco-Marín, and F. Leyva-Cobián. 1993. Role of complement component C1q in phagocytosis of Listeria monocytogenes by murine macrophage-like cell lines. Infect. Immun. 61:3664-3672.
    • (1993) Infect. Immun. , vol.61 , pp. 3664-3672
    • Alvarez-Domínguez, C.1    Carrasco-Marín, E.2    Leyva-Cobián, F.3
  • 3
    • 0028091279 scopus 로고
    • Rapid clearance of malaria circumsporozoite protein (CS) by hepatocytes
    • Cerami, C., U. Frevert, P. Sinnis, B. Takacs, and V. Nussenzweig. 1994. Rapid clearance of malaria circumsporozoite protein (CS) by hepatocytes. J. Exp. Med. 179:695-701.
    • (1994) J. Exp. Med. , vol.179 , pp. 695-701
    • Cerami, C.1    Frevert, U.2    Sinnis, P.3    Takacs, B.4    Nussenzweig, V.5
  • 4
    • 0026795458 scopus 로고
    • The basolateral domain of the hepatocyte plasma membrane bears receptors for the circumsporozoite protein of Plasmodium falciparun sporozoites
    • Cerami, C., U. Frevert, P. Sinnis, B. Takacs, P. Clavijo, M. J. Santos, and V. Nussenzweig. 1992. The basolateral domain of the hepatocyte plasma membrane bears receptors for the circumsporozoite protein of Plasmodium falciparun sporozoites. Cell 70:1021-1033.
    • (1992) Cell , vol.70 , pp. 1021-1033
    • Cerami, C.1    Frevert, U.2    Sinnis, P.3    Takacs, B.4    Clavijo, P.5    Santos, M.J.6    Nussenzweig, V.7
  • 5
    • 0026469140 scopus 로고
    • Early pathogenesis of infection in the liver with the facultative intracellular bacteria Listeria monocytogenes, Francisella tularensis, and Salmonella typhimurium involves lysis of infected hepatocytes by leukocytes
    • Conlan, J. W., and R. J. North. 1992. Early pathogenesis of infection in the liver with the facultative intracellular bacteria Listeria monocytogenes, Francisella tularensis, and Salmonella typhimurium involves lysis of infected hepatocytes by leukocytes. Infect. Immun. 60:5164-5171.
    • (1992) Infect. Immun. , vol.60 , pp. 5164-5171
    • Conlan, J.W.1    North, R.J.2
  • 6
    • 0024893361 scopus 로고
    • Listeria monocytogenes, a model system for the molecular study of intracellular parasitism
    • Cossart, P., and J. Mengaud. 1989. Listeria monocytogenes, a model system for the molecular study of intracellular parasitism. Mol. Biol. Med. 6:463-474.
    • (1989) Mol. Biol. Med. , vol.6 , pp. 463-474
    • Cossart, P.1    Mengaud, J.2
  • 7
    • 0025320059 scopus 로고
    • Surface Listeria monocytogenes carbohydrate-binding components revealed by agglutination with neoglycoproteins
    • Cottin, J., O. Loiseau, R. Robert, C. Mahaza, B. Carbonnelle, and J. M. Senet. 1990. Surface Listeria monocytogenes carbohydrate-binding components revealed by agglutination with neoglycoproteins. FEMS Microbiol. Lett. 68:301-306.
    • (1990) FEMS Microbiol. Lett. , vol.68 , pp. 301-306
    • Cottin, J.1    Loiseau, O.2    Robert, R.3    Mahaza, C.4    Carbonnelle, B.5    Senet, J.M.6
  • 8
    • 0027292970 scopus 로고
    • Integral membrane heparan sulfate proteoglycans
    • David, G. 1993. Integral membrane heparan sulfate proteoglycans. FASEB J. 7:1023-1030.
    • (1993) FASEB J. , vol.7 , pp. 1023-1030
    • David, G.1
  • 9
    • 0021114739 scopus 로고
    • Structural differences in heparan sulfates according to the tissue and species of origin
    • Dietrich, C. P., H. B. Nader, and A. H. Strauss. 1983. Structural differences in heparan sulfates according to the tissue and species of origin. Biochem. Biophys. Res. Commun. 111:865-871.
    • (1983) Biochem. Biophys. Res. Commun. , vol.111 , pp. 865-871
    • Dietrich, C.P.1    Nader, H.B.2    Strauss, A.H.3
  • 10
    • 0026577663 scopus 로고
    • A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin
    • Domann, E., J. Wehland, M. Rohde, S. Pistor, M. Hartl, W. Goebel, M. Leimeister-Wächter, M. Wuencher, and T. Chakraborty. 1992. A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin. EMBO J. 11:1981-1990.
    • (1992) EMBO J. , vol.11 , pp. 1981-1990
    • Domann, E.1    Wehland, J.2    Rohde, M.3    Pistor, S.4    Hartl, M.5    Goebel, W.6    Leimeister-Wächter, M.7    Wuencher, M.8    Chakraborty, T.9
  • 11
    • 0029063839 scopus 로고
    • Entry of Listeria monocytogenes into hepatocytes requires expression of InlB, a surface protein of the internalin multigene family
    • Dramsi, S., I. Biswas, E. Maguin, L. Braun, P. Mastroeni, and P. Cossart. 1995. Entry of Listeria monocytogenes into hepatocytes requires expression of InlB, a surface protein of the internalin multigene family. Mol. Microbiol. 16:251-261.
    • (1995) Mol. Microbiol. , vol.16 , pp. 251-261
    • Dramsi, S.1    Biswas, I.2    Maguin, E.3    Braun, L.4    Mastroeni, P.5    Cossart, P.6
  • 12
    • 0030019928 scopus 로고    scopus 로고
    • Molecular and genetic determinants involved in invasion of mammalian cells by Listeria monocytogenes
    • Dramsi, S., M. Lebrun, and P. Cossart. 1996. Molecular and genetic determinants involved in invasion of mammalian cells by Listeria monocytogenes. Curr. Top. Microbiol. Immunol. 209:61-77.
    • (1996) Curr. Top. Microbiol. Immunol. , vol.209 , pp. 61-77
    • Dramsi, S.1    Lebrun, M.2    Cossart, P.3
  • 13
    • 0025870732 scopus 로고
    • Roles of complement receptor type 3 in phagocytosis of Listeria monocytogenes by inflammatory mouse peritoneal macrophages
    • Drevets, D. A., and P. A. Campbell. 1991. Roles of complement receptor type 3 in phagocytosis of Listeria monocytogenes by inflammatory mouse peritoneal macrophages. Infect. Immun. 59:2645-2652.
    • (1991) Infect. Immun. , vol.59 , pp. 2645-2652
    • Drevets, D.A.1    Campbell, P.A.2
  • 14
    • 0028857073 scopus 로고
    • Listeria monocytogenes infects human endothelial cells by two distinct mechanisms
    • Drevets, D. A., R. T. Sawyer, T. A. Potter, and P. A. Campbell. 1995. Listeria monocytogenes infects human endothelial cells by two distinct mechanisms. Infect. Immun. 63:4268-4276.
    • (1995) Infect. Immun. , vol.63 , pp. 4268-4276
    • Drevets, D.A.1    Sawyer, R.T.2    Potter, T.A.3    Campbell, P.A.4
  • 15
    • 0024297813 scopus 로고
    • Tumor formation dependent on proteoglycan biosynthesis
    • Esko, J. D., K. S. Rostand, and J. L. Weinke. 1988. Tumor formation dependent on proteoglycan biosynthesis. Science 241:1092-1096.
    • (1988) Science , vol.241 , pp. 1092-1096
    • Esko, J.D.1    Rostand, K.S.2    Weinke, J.L.3
  • 16
    • 0025908740 scopus 로고
    • Bacterial entry into eukaryotic cells
    • Falkow, S. 1991. Bacterial entry into eukaryotic cells. Cell 65:1099-1102.
    • (1991) Cell , vol.65 , pp. 1099-1102
    • Falkow, S.1
  • 17
  • 18
    • 0025951915 scopus 로고
    • Listeria monocytogenes, a food-borne pathogen
    • Farber, J. M., and P. I. Peterkin. 1991. Listeria monocytogenes, a food-borne pathogen. Microbiol. Rev. 55:476-511.
    • (1991) Microbiol. Rev. , vol.55 , pp. 476-511
    • Farber, J.M.1    Peterkin, P.I.2
  • 19
    • 0025043439 scopus 로고
    • Cell adhesion and invasion mechanisms in microbial pathogenesis
    • Finlay, B. B. 1990. Cell adhesion and invasion mechanisms in microbial pathogenesis. Curr. Opin. Cell Biol. 2:815-820.
    • (1990) Curr. Opin. Cell Biol. , vol.2 , pp. 815-820
    • Finlay, B.B.1
  • 20
    • 0024382180 scopus 로고
    • Common themes in microbial pathogenicity
    • Finlay, B. B., and S. Falkow. 1989. Common themes in microbial pathogenicity. Microbiol. Rev. 53:210-230.
    • (1989) Microbiol. Rev. , vol.53 , pp. 210-230
    • Finlay, B.B.1    Falkow, S.2
  • 21
    • 0027457377 scopus 로고
    • Malaria circumsporozoite protein binds to heparan sulfate proteoglycans associated with the surface membrane of hepatocytes
    • Frevert, U., P. Sinnis, C. Cerami, W. Shreffler, B. Takacs, and V. Nussenzweig. 1993. Malaria circumsporozoite protein binds to heparan sulfate proteoglycans associated with the surface membrane of hepatocytes. J. Exp. Med. 177:1287-1298.
    • (1993) J. Exp. Med. , vol.177 , pp. 1287-1298
    • Frevert, U.1    Sinnis, P.2    Cerami, C.3    Shreffler, W.4    Takacs, B.5    Nussenzweig, V.6
  • 22
    • 0029079119 scopus 로고
    • Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function
    • Friedrich, E., E. Gouin, R. Hellio, C. Kocks, P. Cossart, and D. Louvard. 1995. Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function. EMBO J. 14:2731-2744.
    • (1995) EMBO J. , vol.14 , pp. 2731-2744
    • Friedrich, E.1    Gouin, E.2    Hellio, R.3    Kocks, C.4    Cossart, P.5    Louvard, D.6
  • 23
    • 0026773096 scopus 로고
    • An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin
    • Friedrich, E., K. Vancompernolle, C. Huet, M. Goethals, J. Finidori, J. Vandekerckhove, and D. Louvard. 1992. An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin. Cell 70:81-92.
    • (1992) Cell , vol.70 , pp. 81-92
    • Friedrich, E.1    Vancompernolle, K.2    Huet, C.3    Goethals, M.4    Finidori, J.5    Vandekerckhove, J.6    Louvard, D.7
  • 24
    • 0025739814 scopus 로고
    • Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from Gram-positive cocci
    • Gaillard, J.-L., P. Berche, C. Frehel, E. Gouin, and P. Cossart. 1991. Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from Gram-positive cocci. Cell 65:1127-1141.
    • (1991) Cell , vol.65 , pp. 1127-1141
    • Gaillard, J.-L.1    Berche, P.2    Frehel, C.3    Gouin, E.4    Cossart, P.5
  • 25
    • 0023617861 scopus 로고
    • In vitro model of penetration and intracellular growth of Listeria monocytogenes in the human enterocyte-like cell line Caco-2
    • Gaillard, J.-L., P. Berche, J. Mounier, S. Richard, and P. J. Sansonetti. 1987. In vitro model of penetration and intracellular growth of Listeria monocytogenes in the human enterocyte-like cell line Caco-2. Infect. Immun. 55:2822-2829.
    • (1987) Infect. Immun. , vol.55 , pp. 2822-2829
    • Gaillard, J.-L.1    Berche, P.2    Mounier, J.3    Richard, S.4    Sansonetti, P.J.5
  • 26
    • 9244261112 scopus 로고    scopus 로고
    • Effect of cell polarization and differentiation on entry of Listeria monocytogenes into the enterocyte-like Caco-2 cell line
    • Gaillard, J.-L., and B. B. Finlay. 1996. Effect of cell polarization and differentiation on entry of Listeria monocytogenes into the enterocyte-like Caco-2 cell line. Infect. Immun. 64:1299-1308.
    • (1996) Infect. Immun. , vol.64 , pp. 1299-1308
    • Gaillard, J.-L.1    Finlay, B.B.2
  • 27
    • 0030060151 scopus 로고    scopus 로고
    • The inlAB locus mediates the entry of Listeria monocytogenes into hepatocytes in vivo
    • Gaillard, J.-L., F. Jaubert, and P. Berche. 1996. The inlAB locus mediates the entry of Listeria monocytogenes into hepatocytes in vivo. J. Exp. Med. 183:359-369.
    • (1996) J. Exp. Med. , vol.183 , pp. 359-369
    • Gaillard, J.-L.1    Jaubert, F.2    Berche, P.3
  • 28
    • 0026687374 scopus 로고
    • Purification and characterization of Listeria monocytogenes phosphatidylinositol-specific phospholipase C
    • Goldfine, H., and K. Knob. 1992. Purification and characterization of Listeria monocytogenes phosphatidylinositol-specific phospholipase C. Infect. Immun. 60:4059-1067.
    • (1992) Infect. Immun. , vol.60 , pp. 4059-11067
    • Goldfine, H.1    Knob, K.2
  • 29
    • 0029011237 scopus 로고
    • iactA of Listeria ivanovii, although distantly related to Listeria monocytogenes actA, restores actin tail formation in an L. monocytogenes actA mutant
    • Gouin, E., P. Dehoux, J. Mengaud, C. Kocks, and P. Cossart. 1995. iactA of Listeria ivanovii, although distantly related to Listeria monocytogenes actA, restores actin tail formation in an L. monocytogenes actA mutant. Infect. Immun. 63:2729-2737.
    • (1995) Infect. Immun. , vol.63 , pp. 2729-2737
    • Gouin, E.1    Dehoux, P.2    Mengaud, J.3    Kocks, C.4    Cossart, P.5
  • 30
    • 0023741662 scopus 로고
    • Properdin, the terminal complement components, thrombospondin and the circumsporozoite protein of malaria parasites contain similar sequence motifs
    • Goundis, D., and K. R. Reid. 1988. Properdin, the terminal complement components, thrombospondin and the circumsporozoite protein of malaria parasites contain similar sequence motifs. Nature 335:82-85.
    • (1988) Nature , vol.335 , pp. 82-85
    • Goundis, D.1    Reid, K.R.2
  • 32
    • 0028148526 scopus 로고
    • Sulfated glycoconjugate receptors for the Bordetella pertussis adhesin filamentous hemagglutinin (FHA) and mapping of the heparin-binding domain of FHA
    • Hannah, J. H., F. D. Menozzi, G. Renauld, C. Locht, and M. J. Brennan. 1994. Sulfated glycoconjugate receptors for the Bordetella pertussis adhesin filamentous hemagglutinin (FHA) and mapping of the heparin-binding domain of FHA. Infect. Immun. 62:5010-5019.
    • (1994) Infect. Immun. , vol.62 , pp. 5010-5019
    • Hannah, J.H.1    Menozzi, F.D.2    Renauld, G.3    Locht, C.4    Brennan, M.J.5
  • 33
    • 0026507880 scopus 로고
    • Proteoglycans: Many forms and many functions
    • Hardingham, T. E., and A. J. Fosang. 1992. Proteoglycans: many forms and many functions. FASEB J. 6:861-870.
    • (1992) FASEB J. , vol.6 , pp. 861-870
    • Hardingham, T.E.1    Fosang, A.J.2
  • 34
    • 0027240384 scopus 로고
    • Heparin-binding EGF-like growth factor stimulation of smooth muscle cell migration: Dependence on interactions with cell surface heparan sulfate
    • Higashiyama, S., J. A. Abraham, and M. Klagsbrun. 1993. Heparin-binding EGF-like growth factor stimulation of smooth muscle cell migration: dependence on interactions with cell surface heparan sulfate. J. Cell Biol. 122:933-940.
    • (1993) J. Cell Biol. , vol.122 , pp. 933-940
    • Higashiyama, S.1    Abraham, J.A.2    Klagsbrun, M.3
  • 35
    • 0025269617 scopus 로고
    • 4)α1-1Cer) and has sequence homology with other proteins that bind sulfated glycoconjugates
    • 4)α1-1Cer) and has sequence homology with other proteins that bind sulfated glycoconjugates. J. Biol. Chem. 265:2852-2855.
    • (1989) J. Biol. Chem. , vol.265 , pp. 2852-2855
    • Holt, G.D.1    Pangburn, M.K.2    Ginsburg, V.3
  • 36
    • 0028256449 scopus 로고
    • Borrelia burgdorferi bind to epithelial cell proteoglycans
    • Isaacs, R. D. 1994. Borrelia burgdorferi bind to epithelial cell proteoglycans. J. Clin. Invest. 93:809-819.
    • (1994) J. Clin. Invest. , vol.93 , pp. 809-819
    • Isaacs, R.D.1
  • 37
    • 0025847743 scopus 로고
    • Glycosaminoglycans: Molecular properties, protein interactions, and role in physiological processes
    • Jackson, R. L., S. J. Busch, and A. D. Cardin. 1991. Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes. Physiol. Rev. 2:481-523.
    • (1991) Physiol. Rev. , vol.2 , pp. 481-523
    • Jackson, R.L.1    Busch, S.J.2    Cardin, A.D.3
  • 38
    • 0027462422 scopus 로고
    • Immunity to intracellular bacteria
    • Kaufmann, S. H. E. 1993. Immunity to intracellular bacteria. Annu. Rev. Immunol. 11:129-163.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 129-163
    • Kaufmann, S.H.E.1
  • 39
    • 0025950158 scopus 로고
    • A dual receptor system is required for basic fibroblast growth factor activity
    • Klagsburn, K., and A. Baird. 1991. A dual receptor system is required for basic fibroblast growth factor activity. Cell 67:229-231.
    • (1991) Cell , vol.67 , pp. 229-231
    • Klagsburn, K.1    Baird, A.2
  • 40
    • 0026515440 scopus 로고
    • L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein
    • Kocks, C., E. Gouin, M. Tabouret, P. Berche, H. Ohayon, and P. Cossart. 1992. L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 68:521-531.
    • (1992) Cell , vol.68 , pp. 521-531
    • Kocks, C.1    Gouin, E.2    Tabouret, M.3    Berche, P.4    Ohayon, H.5    Cossart, P.6
  • 41
    • 0028985135 scopus 로고
    • The actin-polymerization protein from Listeria ivanovii is a large repeat protein which shows only limited amino acid sequence homology to ActA from Listeria monocytogenes
    • Kreft, J., M. Dumbsky, and S. Theiss. 1995. The actin-polymerization protein from Listeria ivanovii is a large repeat protein which shows only limited amino acid sequence homology to ActA from Listeria monocytogenes. FEMS Microbiol. Lett. 126:113-122.
    • (1995) FEMS Microbiol. Lett. , vol.126 , pp. 113-122
    • Kreft, J.1    Dumbsky, M.2    Theiss, S.3
  • 42
    • 0024581874 scopus 로고
    • Identification of an extracellular protein of Listeria monocytogenes possibly involved in intracellular uptake by mammalian cells
    • Kuhn, M., and W. Goebel. 1989. Identification of an extracellular protein of Listeria monocytogenes possibly involved in intracellular uptake by mammalian cells. Infect. Immun. 57:55-61.
    • (1989) Infect. Immun. , vol.57 , pp. 55-61
    • Kuhn, M.1    Goebel, W.2
  • 43
    • 0030024449 scopus 로고    scopus 로고
    • Actin-based bacterial motility: Towards a definition of the minimal requirements
    • Lasa, I., and P. Cossart. 1996. Actin-based bacterial motility: towards a definition of the minimal requirements. Trends Cell Biol. 6:109-114.
    • (1996) Trends Cell Biol. , vol.6 , pp. 109-114
    • Lasa, I.1    Cossart, P.2
  • 44
    • 0029609261 scopus 로고
    • The amino-terminal part of ActA is critical for the actin-based motility of Lisieria monocytogenes; the central proline-rich region acts as a stimulator
    • Lasa, I., V. David, E. Gouin, J.-B. Marchand, and P. Cossart. 1995. The amino-terminal part of ActA is critical for the actin-based motility of Lisieria monocytogenes; the central proline-rich region acts as a stimulator. Mol. Microbiol. 18:425-436.
    • (1995) Mol. Microbiol. , vol.18 , pp. 425-436
    • Lasa, I.1    David, V.2    Gouin, E.3    Marchand, J.-B.4    Cossart, P.5
  • 45
    • 0027178590 scopus 로고
    • The filamentous haemagglutinin, a multifaceted adhesin produced by virulent Bordetella spp
    • Locht, C., P. Bertin, F. D. Menozzi, and G. Renauld. 1993. The filamentous haemagglutinin, a multifaceted adhesin produced by virulent Bordetella spp. Mol. Microbiol. 9:653-660.
    • (1993) Mol. Microbiol. , vol.9 , pp. 653-660
    • Locht, C.1    Bertin, P.2    Menozzi, F.D.3    Renauld, G.4
  • 46
    • 0027360382 scopus 로고
    • A heparin-binding activity on Leishmania amastigotes which mediates adhesion to cellular proteoglycans
    • Love, D. C., J. D. Esko, and D. M. Mosser. 1993. A heparin-binding activity on Leishmania amastigotes which mediates adhesion to cellular proteoglycans. J. Cell Biol. 123:759-766.
    • (1993) J. Cell Biol. , vol.123 , pp. 759-766
    • Love, D.C.1    Esko, J.D.2    Mosser, D.M.3
  • 47
    • 0025976408 scopus 로고
    • Identification of phosphatidylinositol-specific phospholipase C activity in Listeria monocytogenes: A novel type of virulence factor?
    • Mengaud, J., C. Braun-Breton, and P. Cossart. 1991. Identification of phosphatidylinositol-specific phospholipase C activity in Listeria monocytogenes: a novel type of virulence factor? Mol. Microbiol. 5:367-372.
    • (1991) Mol. Microbiol. , vol.5 , pp. 367-372
    • Mengaud, J.1    Braun-Breton, C.2    Cossart, P.3
  • 48
    • 0029869384 scopus 로고    scopus 로고
    • E-cadherin is the receptor tor internalin, a surface protein required for entry of L. monocytogenes into epithelial cells
    • Mengaud, J., H. Ohayon, P. Gounon, R. M. Mége, and P. Cossart. 1996. E-cadherin is the receptor tor internalin, a surface protein required for entry of L. monocytogenes into epithelial cells. Cell 84:923-932.
    • (1996) Cell , vol.84 , pp. 923-932
    • Mengaud, J.1    Ohayon, H.2    Gounon, P.3    Mége, R.M.4    Cossart, P.5
  • 49
    • 0025177306 scopus 로고
    • Interaction of glycoprotein gIII with a cellular heparin-like substance mediates adsorption of pseudorabies virus
    • Mettenleiter, T. C., L. Zsak, F. Zuckermann, N. Sugg, H. Kern, and T. Ben-Porat. 1990. Interaction of glycoprotein gIII with a cellular heparin-like substance mediates adsorption of pseudorabies virus. J. Virol. 64:278-286.
    • (1990) J. Virol. , vol.64 , pp. 278-286
    • Mettenleiter, T.C.1    Zsak, L.2    Zuckermann, F.3    Sugg, N.4    Kern, H.5    Ben-Porat, T.6
  • 50
    • 0027272019 scopus 로고
    • Localization of the ActA polypeptide of Listeria monocytogenes in infected tissue culture cell lines: ActA is not associated with actin "comets."
    • Niebuhr, K., T. Chakraborty, M. Rohde, T. Gazlig, B. Jansen, P. Köllner, and J. Wehland. 1993. Localization of the ActA polypeptide of Listeria monocytogenes in infected tissue culture cell lines: ActA is not associated with actin "comets." Infect. Immun. 61:2793-2802.
    • (1993) Infect. Immun. , vol.61 , pp. 2793-2802
    • Niebuhr, K.1    Chakraborty, T.2    Rohde, M.3    Gazlig, T.4    Jansen, B.5    Köllner, P.6    Wehland, J.7
  • 51
    • 0025943946 scopus 로고
    • A novel T. cruzi heparin-binding protein promotes fibroblast adhesion and penetration of engineered bacteria and trypanosomes into mammalian cells
    • Ortega-Barria, E., and E. A. Pereira. 1991. A novel T. cruzi heparin-binding protein promotes fibroblast adhesion and penetration of engineered bacteria and trypanosomes into mammalian cells. Cell 67:411-421.
    • (1991) Cell , vol.67 , pp. 411-421
    • Ortega-Barria, E.1    Pereira, E.A.2
  • 52
    • 0026716363 scopus 로고
    • Malaria sporozoites and circumsporozoite proteins bind specifically to sulfated glycoconjugates
    • Pancake, S. J., G. D. Holt, S. Mellouk, and S. L. Hoffman, 1992. Malaria sporozoites and circumsporozoite proteins bind specifically to sulfated glycoconjugates. J. Cell Biol. 117:1351-1357.
    • (1992) J. Cell Biol. , vol.117 , pp. 1351-1357
    • Pancake, S.J.1    Holt, G.D.2    Mellouk, S.3    Hoffman, S.L.4
  • 53
    • 0029294733 scopus 로고
    • The bacterial actin nucleator protein ActA of Listeria monocytogenes contains multiple binding sites for host microfilament proteins
    • Pistor, S., T. Chakraborty, U. Walter, and J. Wehland. 1995. The bacterial actin nucleator protein ActA of Listeria monocytogenes contains multiple binding sites for host microfilament proteins. Curr. Biol. 5:517-525.
    • (1995) Curr. Biol. , vol.5 , pp. 517-525
    • Pistor, S.1    Chakraborty, T.2    Walter, U.3    Wehland, J.4
  • 54
    • 0026587933 scopus 로고
    • Molecular determinants of Listeria monocytogenes pathogenesis
    • Portnoy, D. A., T. Chakraborty, W. Gnebel, and P. Cossart. 1992. Molecular determinants of Listeria monocytogenes pathogenesis. Infect. Immun. 60: 1263-1267.
    • (1992) Infect. Immun. , vol.60 , pp. 1263-1267
    • Portnoy, D.A.1    Chakraborty, T.2    Gnebel, W.3    Cossart, P.4
  • 55
    • 0015348582 scopus 로고
    • Experimental Listeria enteritis. I. An electron microscopic study of the epithelial phase in experimental Listeria infection
    • Rácz, P., K. Tenner, and E. Mérö. 1972. Experimental Listeria enteritis. I. An electron microscopic study of the epithelial phase in experimental Listeria infection. Lab. Invest. 26:694-700.
    • (1972) Lab. Invest. , vol.26 , pp. 694-700
    • Rácz, P.1    Tenner, K.2    Mérö, E.3
  • 56
    • 0027683068 scopus 로고
    • The coordinated regulation of heparan sulfate, syndecans and cell behavior
    • Rapraeger, A. C. 1993. The coordinated regulation of heparan sulfate, syndecans and cell behavior. Curr. Opin. Cell Biol. 5:844-853.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 844-853
    • Rapraeger, A.C.1
  • 57
    • 0023741661 scopus 로고
    • A highly conserved amino-acid sequence in thrombospondin, properdin and in proteins from sporozoites and blood stages of human malaria parasite
    • Robson, K. J. H., J. R. S. Hall, M. W. Jennings, T. J. R. Harris, K. Marsh, C. I. Newbold, V. E. Tate, and D. J. Weatherall. 1988. A highly conserved amino-acid sequence in thrombospondin, properdin and in proteins from sporozoites and blood stages of human malaria parasite. Nature 335:79-85.
    • (1988) Nature , vol.335 , pp. 79-85
    • Robson, K.J.H.1    Hall, J.R.S.2    Jennings, M.W.3    Harris, T.J.R.4    Marsh, K.5    Newbold, C.I.6    Tate, V.E.7    Weatherall, D.J.8
  • 58
    • 0027202612 scopus 로고
    • Attachment factors of Bordetella pertussis: Mimicry of eukaryotic cell recognition molecules
    • Sandros, J., and E. Tuomanen. 1993. Attachment factors of Bordetella pertussis: mimicry of eukaryotic cell recognition molecules. Trends Microbiol. 1:192-195.
    • (1993) Trends Microbiol. , vol.1 , pp. 192-195
    • Sandros, J.1    Tuomanen, E.2
  • 59
    • 0028825543 scopus 로고
    • Regulation of growth factor activation by proteoglycans: What is the role of the low affinity receptors?
    • Schlesinger, J., I. Lax, and M. Lemmon. 1995. Regulation of growth factor activation by proteoglycans: what is the role of the low affinity receptors? Cell 83:357-360.
    • (1995) Cell , vol.83 , pp. 357-360
    • Schlesinger, J.1    Lax, I.2    Lemmon, M.3
  • 62
    • 0026551062 scopus 로고
    • Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans
    • Shieh, M.-T., D. WuDunn, R. I. Montgomery, J. D. Esko, and P. G. Spear. 1992. Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans. J. Cell Biol. 116:1273-1281.
    • (1992) J. Cell Biol. , vol.116 , pp. 1273-1281
    • Shieh, M.-T.1    WuDunn, D.2    Montgomery, R.I.3    Esko, J.D.4    Spear, P.G.5
  • 63
    • 0028303174 scopus 로고
    • Structural and functional properties of region II-plus of the malaria circumsporozoite protein
    • Sinnis, P., P. Clavijo, D. Fenyö, B. T. Chait, C. Cerami, and V. Nussenzweig. 1994. Structural and functional properties of region II-plus of the malaria circumsporozoite protein. J. Exp. Med. 186:297-300.
    • (1994) J. Exp. Med. , vol.186 , pp. 297-300
    • Sinnis, P.1    Clavijo, P.2    Fenyö, D.3    Chait, B.T.4    Cerami, C.5    Nussenzweig, V.6
  • 64
    • 0028828198 scopus 로고
    • The two distinct phospholipases C of Listeria monocytogenes have overlapping roles in escape from a vacuole and cell-to-cell spread
    • Smith, G. A., H. Marquis, S. Jones, N. C. Johnston, D. A. Portnoy, and H. Goldfine. 1995. The two distinct phospholipases C of Listeria monocytogenes have overlapping roles in escape from a vacuole and cell-to-cell spread. Infect. Immun. 63:4231-4237.
    • (1995) Infect. Immun. , vol.63 , pp. 4231-4237
    • Smith, G.A.1    Marquis, H.2    Jones, S.3    Johnston, N.C.4    Portnoy, D.A.5    Goldfine, H.6
  • 65
    • 0026806511 scopus 로고
    • Localization and characterization of a heparin binding domain peptide of human von Willebrand factor
    • Sobel, M., D. F. Soler, J. C. Kermode, and R. B. Harris. 1992. Localization and characterization of a heparin binding domain peptide of human von Willebrand factor. J. Biol. Chem. 267:8857-8862.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8857-8862
    • Sobel, M.1    Soler, D.F.2    Kermode, J.C.3    Harris, R.B.4
  • 66
    • 0025719988 scopus 로고
    • Characterization of a novel heparan sulfate proteoglycan found in extracellular matrix of liver sinusoids and basement membranes
    • Soroka, C. J., and M. G. Farqhar. 1991. Characterization of a novel heparan sulfate proteoglycan found in extracellular matrix of liver sinusoids and basement membranes. J. Cell Biol. 113:1213-1241.
    • (1991) J. Cell Biol. , vol.113 , pp. 1213-1241
    • Soroka, C.J.1    Farqhar, M.G.2
  • 67
    • 0028092177 scopus 로고
    • Exploitation of microfilament proteins by Listeria monocytogenes: Microvillus-like composition of the comet tails and vectorial spreading in polarized epithelial sheets
    • Temm-Grove, C., B. M. Jockusch, M. Rohde, K. Niebuhr, T. Chakraborty, and J. Wehland. 1994. Exploitation of microfilament proteins by Listeria monocytogenes: microvillus-like composition of the comet tails and vectorial spreading in polarized epithelial sheets. J. Cell Sci. 107:2951-2960.
    • (1994) J. Cell Sci. , vol.107 , pp. 2951-2960
    • Temm-Grove, C.1    Jockusch, B.M.2    Rohde, M.3    Niebuhr, K.4    Chakraborty, T.5    Wehland, J.6
  • 68
    • 0027316090 scopus 로고
    • The wily ways of a parasite: Induction of actin assembly by Listeria
    • Tilney, L. G., and M. S. Tilney. 1993. The wily ways of a parasite: induction of actin assembly by Listeria. Trends Microbiol. 1:25-31.
    • (1993) Trends Microbiol. , vol.1 , pp. 25-31
    • Tilney, L.G.1    Tilney, M.S.2
  • 69
    • 0027065504 scopus 로고
    • G- to F-actin modulation by a single amino acid substitution in the actin binding site of actobindin and thymosin β4
    • Vanconpernolle, K., M. Goethals, C. Huet, D. Louvard, and J. Vandekerckhove. 1992. G- to F-actin modulation by a single amino acid substitution in the actin binding site of actobindin and thymosin β4. EMBO J. 11:4739-4746.
    • (1992) EMBO J. , vol.11 , pp. 4739-4746
    • Vanconpernolle, K.1    Goethals, M.2    Huet, C.3    Louvard, D.4    Vandekerckhove, J.5
  • 70
    • 0029027169 scopus 로고
    • Binding of syndecan-like cell surface proteoglycan receptors is required for Neisseria gonorrhoeae entry into human mucosal cells
    • van Putten, J. P. M., and S. M. Paul. 1995. Binding of syndecan-like cell surface proteoglycan receptors is required for Neisseria gonorrhoeae entry into human mucosal cells. EMBO J. 14:2144-2154.
    • (1995) EMBO J. , vol.14 , pp. 2144-2154
    • Van Putten, J.P.M.1    Paul, S.M.2
  • 71
    • 0026502412 scopus 로고
    • Nucleotidc sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread
    • Vázquez-Boland, J. A., C. Kocks, S. Dramsi, H. Ohayon, C. Geoffroy, J. Mengaud, and P. Cossart. 1992. Nucleotidc sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread. Infect. Immun. 60:219-230.
    • (1992) Infect. Immun. , vol.60 , pp. 219-230
    • Vázquez-Boland, J.A.1    Kocks, C.2    Dramsi, S.3    Ohayon, H.4    Geoffroy, C.5    Mengaud, J.6    Cossart, P.7
  • 73
    • 0027292986 scopus 로고
    • Bacterial proteins binding to the mammalian extracellular matrix
    • Westerlund, B., and T. K. Korhonen. 1993. Bacterial proteins binding to the mammalian extracellular matrix. Mol. Microbiol. 9:687-694.
    • (1993) Mol. Microbiol. , vol.9 , pp. 687-694
    • Westerlund, B.1    Korhonen, T.K.2
  • 74
    • 0027235483 scopus 로고
    • Multiplication of Listeria monocytogenes in a murine hepatocyte cell line
    • Wood, S., N. Maroushek, and C. Czuprynski. 1993. Multiplication of Listeria monocytogenes in a murine hepatocyte cell line. Infect. Immun. 61:3068-3072.
    • (1993) Infect. Immun. , vol.61 , pp. 3068-3072
    • Wood, S.1    Maroushek, N.2    Czuprynski, C.3
  • 75
    • 0026744148 scopus 로고
    • Cell surface heparan sulfate proteoglycans
    • Yanagishita, M., and V. C. Hascall. 1992. Cell surface heparan sulfate proteoglycans. J. Biol. Chem. 267:9451-9454.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9451-9454
    • Yanagishita, M.1    Hascall, V.C.2


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