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Volumn 77, Issue 9, 2003, Pages 5370-5377

Conformational changes, plasma membrane penetration, and infection by human rhinovirus type 2: Role of receptors and low pH

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN; BAFILOMYCIN; LOW DENSITY LIPOPROTEIN RECEPTOR; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; MEMBRANE RECEPTOR; VERY LOW DENSITY LIPOPROTEIN RECEPTOR; VIRUS RNA;

EID: 0037405104     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.77.9.5370-5377.2003     Document Type: Article
Times cited : (50)

References (38)
  • 1
    • 0033408492 scopus 로고    scopus 로고
    • Human rhinovirus HRV14 uncoats from early endosomes in the presence of bafilomycin
    • Bayer, N., E. Prchla, M. Schwab, D. Blaas, and R. Fuchs. 1999. Human rhinovirus HRV14 uncoats from early endosomes in the presence of bafilomycin. FEBS Lett. 463:175-178.
    • (1999) FEBS Lett. , vol.463 , pp. 175-178
    • Bayer, N.1    Prchla, E.2    Schwab, M.3    Blaas, D.4    Fuchs, R.5
  • 2
    • 0031743946 scopus 로고    scopus 로고
    • Effect of bafilomycin Al and nocodazole on endocytic transport in HeLa cells: Implications for viral uncoating and infection
    • Bayer, N., D. Schober, E. Prchla, R. F. Murphy, D. Blaas, and R. Fuchs. 1998. Effect of bafilomycin Al and nocodazole on endocytic transport in HeLa cells: implications for viral uncoating and infection. J. Virol. 72:9645-9655.
    • (1998) J. Virol. , vol.72 , pp. 9645-9655
    • Bayer, N.1    Schober, D.2    Prchla, E.3    Murphy, R.F.4    Blaas, D.5    Fuchs, R.6
  • 4
    • 0002453664 scopus 로고
    • Virus culture
    • D. R. Harper (ed.). Blackwell Scientific Publications, London, United Kingdom
    • Blake, K., and S. O'Connell. 1993. Virus culture, p. 81-122. In D. R. Harper (ed.), Virology Labfax. Blackwell Scientific Publications, London, United Kingdom.
    • (1993) Virology Labfax , pp. 81-122
    • Blake, K.1    O'Connell, S.2
  • 5
    • 0030758231 scopus 로고    scopus 로고
    • LDL receptor structure: Calcium cages, acid baths and recycling receptors
    • Brown, M. S., J. Herz, and J. L. Goldstein. 1997. LDL receptor structure: calcium cages, acid baths and recycling receptors. Nature 388:629-630.
    • (1997) Nature , vol.388 , pp. 629-630
    • Brown, M.S.1    Herz, J.2    Goldstein, J.L.3
  • 6
    • 0029063466 scopus 로고
    • Kinetics and thermodynamics of virus binding to receptor. Studies with rhinovirus, intercellular adhesion molecule-1 (ICAM-1), and surface plasmon resonance
    • Casasnovas, M., and T. A. Springer. 1995. Kinetics and thermodynamics of virus binding to receptor. Studies with rhinovirus, intercellular adhesion molecule-1 (ICAM-1), and surface plasmon resonance. J. Biol. Chem. 270:13216-13224.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13216-13224
    • Casasnovas, M.1    Springer, T.A.2
  • 7
    • 0023091262 scopus 로고
    • Acid-dependent ligand dissociation and recycling of LDL receptor mediated by growth factor homology region
    • Davis, C. G., J. L. Goldstein, T. C. Sudhof, R. G. Anderson, D. W. Russell, and M. S. Brown. 1987. Acid-dependent ligand dissociation and recycling of LDL receptor mediated by growth factor homology region. Nature 326:760-765.
    • (1987) Nature , vol.326 , pp. 760-765
    • Davis, C.G.1    Goldstein, J.L.2    Sudhof, T.C.3    Anderson, R.G.4    Russell, D.W.5    Brown, M.S.6
  • 8
    • 0031887229 scopus 로고    scopus 로고
    • Calcium induces a conformational change in the ligand binding domain of the low density lipoprotein receptor
    • Dirlam-Schatz, K. A., and A. D. Attie. 1998. Calcium induces a conformational change in the ligand binding domain of the low density lipoprotein receptor. J. Lipid Res. 39:402-411.
    • (1998) J. Lipid Res. , vol.39 , pp. 402-411
    • Dirlam-Schatz, K.A.1    Attie, A.D.2
  • 10
    • 0026081331 scopus 로고
    • Stabilization of human rhinovirus serotype-2 against pH-induced conformational change by antiviral compounds
    • Gruenberger, M., D. Pevear, G. D. Diana, E. Kuechler, and D. Blaas. 1991. Stabilization of human rhinovirus serotype-2 against pH-induced conformational change by antiviral compounds. J. Gen. Virol. 72:431-433.
    • (1991) J. Gen. Virol. , vol.72 , pp. 431-433
    • Gruenberger, M.1    Pevear, D.2    Diana, G.D.3    Kuechler, E.4    Blaas, D.5
  • 11
    • 0018853517 scopus 로고
    • On the entry of Semliki Forest virus into BHK-21 cells
    • Helenius, A., J. Kartenbeck, K. Simons, and E. Fries. 1980. On the entry of Semliki Forest virus into BHK-21 cells. J. Cell Biol. 84:404-420.
    • (1980) J. Cell Biol. , vol.84 , pp. 404-420
    • Helenius, A.1    Kartenbeck, J.2    Simons, K.3    Fries, E.4
  • 12
    • 0036670673 scopus 로고    scopus 로고
    • The concerted conformational changes during human rhinovirus 2 uncoating
    • Hewat, E., E. Neumann, and D. Blaas. 2002. The concerted conformational changes during human rhinovirus 2 uncoating. Mol. Cell 10:317-326.
    • (2002) Mol. Cell , vol.10 , pp. 317-326
    • Hewat, E.1    Neumann, E.2    Blaas, D.3
  • 13
    • 0030007379 scopus 로고    scopus 로고
    • Structure of a neutralizing antibody bound bivalently to human rhinovirus 2
    • Hewat, E. A., and D. Blaas. 1996. Structure of a neutralizing antibody bound bivalently to human rhinovirus 2. EMBO J. 15:1515-1523.
    • (1996) EMBO J. , vol.15 , pp. 1515-1523
    • Hewat, E.A.1    Blaas, D.2
  • 14
    • 0034410936 scopus 로고    scopus 로고
    • The cellular receptor to human rhinovirus 2 binds around the 5-fold axis and not in the canyon: A structural view
    • Hewat, E. A., E. Neumann, J. F. Conway, R. Moser, B. Ronacher, T. C. Marlovits, and D. Blaas. 2000. The cellular receptor to human rhinovirus 2 binds around the 5-fold axis and not in the canyon: a structural view. EMBO J. 19:6317-6325.
    • (2000) EMBO J. , vol.19 , pp. 6317-6325
    • Hewat, E.A.1    Neumann, E.2    Conway, J.F.3    Moser, R.4    Ronacher, B.5    Marlovits, T.C.6    Blaas, D.7
  • 16
    • 0027473611 scopus 로고
    • Formation of rhinovirus-soluble ICAM-1 complexes and conformational changes in the virion
    • Hoover-Litty, H., and J. M. Greve. 1993. Formation of rhinovirus-soluble ICAM-1 complexes and conformational changes in the virion. J. Virol. 67:390-397.
    • (1993) J. Virol. , vol.67 , pp. 390-397
    • Hoover-Litty, H.1    Greve, J.M.2
  • 17
    • 0034730626 scopus 로고    scopus 로고
    • Vesicle-reconstituted low density lipoprotein receptor. Visualization by cryoelectron microscopy
    • Jeon, H., and G. G. Shipley. 2000. Vesicle-reconstituted low density lipoprotein receptor. Visualization by cryoelectron microscopy. J. Biol. Chem. 275:30458-30464.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30458-30464
    • Jeon, H.1    Shipley, G.G.2
  • 18
    • 0033571522 scopus 로고    scopus 로고
    • Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor
    • Kolatkar, P. R., J. Bella, N. H. Olson, C. M. Bator, T. S. Baker, and M. G. Rossmann. 1999. Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor. EMBO J. 18:6249-6259.
    • (1999) EMBO J. , vol.18 , pp. 6249-6259
    • Kolatkar, P.R.1    Bella, J.2    Olson, N.H.3    Bator, C.M.4    Baker, T.S.5    Rossmann, M.G.6
  • 19
    • 0015319658 scopus 로고
    • Naturally occurring and artificially produced components of three rhinoviruses
    • Korant, B. D., K. Lonberg-Holm, J. Noble, and J. T. Stasny. 1972. Naturally occurring and artificially produced components of three rhinoviruses. Virology 48:71-86.
    • (1972) Virology , vol.48 , pp. 71-86
    • Korant, B.D.1    Lonberg-Holm, K.2    Noble, J.3    Stasny, J.T.4
  • 20
    • 0017169901 scopus 로고
    • Interaction of liposomes with subviral particles of poliovirus type 2 and rhinovirus type 2
    • Lonberg-Holm, K., L. B. Gosser, and E. J. Shimshick. 1976. Interaction of liposomes with subviral particles of poliovirus type 2 and rhinovirus type 2. J. Virol. 19:746-749.
    • (1976) J. Virol. , vol.19 , pp. 746-749
    • Lonberg-Holm, K.1    Gosser, L.B.2    Shimshick, E.J.3
  • 21
    • 0015867230 scopus 로고
    • Comparison of in vitro and cell-mediated alteration of a human rhinovirus and its inhibition by sodium dodecyl sulfate
    • Lonberg-Holm, K., and J. Noble-Harvey. 1973. Comparison of in vitro and cell-mediated alteration of a human rhinovirus and its inhibition by sodium dodecyl sulfate. J. Virol. 12:819-824.
    • (1973) J. Virol. , vol.12 , pp. 819-824
    • Lonberg-Holm, K.1    Noble-Harvey, J.2
  • 22
    • 0015893652 scopus 로고
    • Antigenic determinants of infective and inactivated human rhinovirus type 2
    • Lonberg-Holm, K., and F. H. Yin. 1973. Antigenic determinants of infective and inactivated human rhinovirus type 2. J. Virol. 12:114-123.
    • (1973) J. Virol. , vol.12 , pp. 114-123
    • Lonberg-Holm, K.1    Yin, F.H.2
  • 23
    • 0021741382 scopus 로고
    • Different pH requirements for entry of the two picornaviruses, human rhinovirus 2 and murine encephalomyocarditis virus
    • Madshus, I., S. Olsnes, and K. Sandvig. 1984. Different pH requirements for entry of the two picornaviruses, human rhinovirus 2 and murine encephalomyocarditis virus. Virology 139:346-357.
    • (1984) Virology , vol.139 , pp. 346-357
    • Madshus, I.1    Olsnes, S.2    Sandvig, K.3
  • 24
    • 0031743610 scopus 로고    scopus 로고
    • Very-low-density lipoprotein receptor fragment shed from HeLa cells inhibits human rhinovirus infection
    • Marlovits, T. C., C. Abrahamsberg, and D. Blaas. 1998. Very-low-density lipoprotein receptor fragment shed from HeLa cells inhibits human rhinovirus infection. J. Virol. 72:10246-10250.
    • (1998) J. Virol. , vol.72 , pp. 10246-10250
    • Marlovits, T.C.1    Abrahamsberg, C.2    Blaas, D.3
  • 25
    • 0032725591 scopus 로고    scopus 로고
    • Functional domains of the very low density lipoprotein receptor: Molecular analysis of ligand binding and acid-dependent ligand dissociation mechanisms
    • Mikhailenko, I., W. Considine, K. M. Argraves, D. Loukinov, B. T. Hyman, and D. K. Strickland. 1999. Functional domains of the very low density lipoprotein receptor: molecular analysis of ligand binding and acid-dependent ligand dissociation mechanisms. J. Cell Sci. 112:3269-3281.
    • (1999) J. Cell Sci. , vol.112 , pp. 3269-3281
    • Mikhailenko, I.1    Considine, W.2    Argraves, K.M.3    Loukinov, D.4    Hyman, B.T.5    Strickland, D.K.6
  • 27
    • 0023178470 scopus 로고
    • Mechanism of entry of human rhinovirus 2 into HeLa cells
    • Neubauer, C., L. Frasel, E. Kuechler, and D. Blaas. 1987. Mechanism of entry of human rhinovirus 2 into HeLa cells. Virology 158:255-258.
    • (1987) Virology , vol.158 , pp. 255-258
    • Neubauer, C.1    Frasel, L.2    Kuechler, E.3    Blaas, D.4
  • 28
    • 0015582051 scopus 로고
    • Interactions of components of human rhinovirus type 2 with HeLa cells
    • Noble, J. N., and K. Lonberg-Holm. 1973. Interactions of components of human rhinovirus type 2 with HeLa cells. Virology 51:270-278.
    • (1973) Virology , vol.51 , pp. 270-278
    • Noble, J.N.1    Lonberg-Holm, K.2
  • 30
    • 0028229815 scopus 로고
    • Uncoating of human rhinovirus serotype 2 from late endosomes
    • Prchla, E., E. Kuechler, D. Blaas, and R. Fuchs. 1994. Uncoating of human rhinovirus serotype 2 from late endosomes. J. Virol. 68:3713-3723.
    • (1994) J. Virol. , vol.68 , pp. 3713-3723
    • Prchla, E.1    Kuechler, E.2    Blaas, D.3    Fuchs, R.4
  • 31
    • 0029154615 scopus 로고
    • Virus-mediated release of endosomal content in vitro: Different behavior of adenovirus and rhinovirus serotype 2
    • Prchla, E., C. Plank, E. Wagner, D. Blaas, and R. Fuchs. 1995. Virus-mediated release of endosomal content in vitro: different behavior of adenovirus and rhinovirus serotype 2. J. Cell Biol. 131:111-123.
    • (1995) J. Cell Biol. , vol.131 , pp. 111-123
    • Prchla, E.1    Plank, C.2    Wagner, E.3    Blaas, D.4    Fuchs, R.5
  • 32
    • 0000327130 scopus 로고    scopus 로고
    • Picomaviridae: The viruses and their replication
    • D. M. Knipe, B. N. Fields, and P. M. Howley (ed.). Lippincott-Raven Publishers, Philadelphia, Pa
    • Rueckert, R. R. 1996. Picomaviridae: the viruses and their replication, p. 609-654. In D. M. Knipe, B. N. Fields, and P. M. Howley (ed.), Fields virology, 3rd ed. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , pp. 609-654
    • Rueckert, R.R.1
  • 33
    • 0034802046 scopus 로고    scopus 로고
    • Cellular COPII proteins are involved in production of the vesicles that form the poliovirus replication complex
    • Rust, R. C., L. Landmann, R. Gosert, B. L. Tang, W. Hong, H.-P. Hauri, D. Egger, and K. Bienz. 2001. Cellular COPII proteins are involved in production of the vesicles that form the poliovirus replication complex. J. Virol. 75:9808-9818.
    • (2001) J. Virol. , vol.75 , pp. 9808-9818
    • Rust, R.C.1    Landmann, L.2    Gosert, R.3    Tang, B.L.4    Hong, W.5    Hauri, H.-P.6    Egger, D.7    Bienz, K.8
  • 34
    • 0036166646 scopus 로고    scopus 로고
    • Genetic clustering of all 102 human rhinovirus prototype strains: Serotype 87 is close to human enterovirus 70
    • Savolainen, C., S. Blomqvist, M. N. Mulders, and T. Hovi. 2002. Genetic clustering of all 102 human rhinovirus prototype strains: serotype 87 is close to human enterovirus 70. J. Gen. Virol. 83:333-340.
    • (2002) J. Gen. Virol. , vol.83 , pp. 333-340
    • Savolainen, C.1    Blomqvist, S.2    Mulders, M.N.3    Hovi, T.4
  • 35
    • 0029794678 scopus 로고    scopus 로고
    • Cellular origin and ultrastructure of membranes induced during poliovirus infection
    • Schlegel, A., T. H. Giddings, Jr., M. S. Ladinsky, and K. Kirkegaard. 1996. Cellular origin and ultrastructure of membranes induced during poliovirus infection. J. Virol. 70:6576-6588.
    • (1996) J. Virol. , vol.70 , pp. 6576-6588
    • Schlegel, A.1    Giddings T.H., Jr.2    Ladinsky, M.S.3    Kirkegaard, K.4
  • 36
    • 0031883836 scopus 로고    scopus 로고
    • Major and minor receptor group human rhinoviruses penetrate from endosomes by different mechanisms
    • Schober, D., P. Kronenberger, E. Prchla, D. Blaas, and R. Fuchs. 1998. Major and minor receptor group human rhinoviruses penetrate from endosomes by different mechanisms. J. Virol. 72:1354-1364.
    • (1998) J. Virol. , vol.72 , pp. 1354-1364
    • Schober, D.1    Kronenberger, P.2    Prchla, E.3    Blaas, D.4    Fuchs, R.5
  • 37
    • 0025957484 scopus 로고
    • The major and minor group receptor families contain all but one human rhinovirus serotype
    • Uncapher, C. R., C. M. Dewitt, and R. J. Colonno. 1991. The major and minor group receptor families contain all but one human rhinovirus serotype. Virology 180:814-817.
    • (1991) Virology , vol.180 , pp. 814-817
    • Uncapher, C.R.1    Dewitt, C.M.2    Colonno, R.J.3
  • 38
    • 0019069749 scopus 로고
    • Fusion of Semliki Forest virus with the plasma membrane can be induced by low pH
    • White, J., J. Kartenbeck, and A. Helenius. 1980. Fusion of Semliki Forest virus with the plasma membrane can be induced by low pH. J. Cell Biol. 87:264-272.
    • (1980) J. Cell Biol. , vol.87 , pp. 264-272
    • White, J.1    Kartenbeck, J.2    Helenius, A.3


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