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Volumn 269, Issue 2, 2000, Pages 239-247

Cell recognition and entry by rhino- and enteroviruses

Author keywords

[No Author keywords available]

Indexed keywords

INTERCELLULAR ADHESION MOLECULE 1; VIRUS RECEPTOR;

EID: 0034630455     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.2000.0258     Document Type: Article
Times cited : (54)

References (53)
  • 1
    • 0021249482 scopus 로고
    • Many rhinovirus serotypes share the same cellular receptor
    • Abraham G., Colonno R. J. Many rhinovirus serotypes share the same cellular receptor. J. Virol. 51:1984;340-345.
    • (1984) J. Virol. , vol.51 , pp. 340-345
    • Abraham, G.1    Colonno, R.J.2
  • 2
    • 0031958412 scopus 로고    scopus 로고
    • Interaction of poliovirus with its purified receptor and conformational alteration in the virion
    • Arita M., Koike S., Aoki J., Horie H., Nomoto A. Interaction of poliovirus with its purified receptor and conformational alteration in the virion. J. Virol. 72:1998;3578-3586.
    • (1998) J. Virol. , vol.72 , pp. 3578-3586
    • Arita, M.1    Koike, S.2    Aoki, J.3    Horie, H.4    Nomoto, A.5
  • 3
    • 0032516070 scopus 로고    scopus 로고
    • The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand
    • Bella J., Kolatkar P. R., Marlor C. W., Greve J. M., Rossmann M. G. The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand. Proc. Natl. Acad. Sci. USA. 95:1998;4140-4145.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4140-4145
    • Bella, J.1    Kolatkar, P.R.2    Marlor, C.W.3    Greve, J.M.4    Rossmann, M.G.5
  • 6
    • 0028026783 scopus 로고
    • The poliovirus receptor: Identification of domains and amino acid residues critical for virus binding
    • Bernhardt G., Harber J., Zibert A., deCrombrugghe M., Wimmer E. The poliovirus receptor: Identification of domains and amino acid residues critical for virus binding. Virology. 203:1994;344-356.
    • (1994) Virology , vol.203 , pp. 344-356
    • Bernhardt, G.1    Harber, J.2    Zibert, A.3    Decrombrugghe, M.4    Wimmer, E.5
  • 7
    • 0029063466 scopus 로고
    • Kinetics and thermodynamics of virus binding to receptor
    • Casasnovas J. M., Springer T. A. Kinetics and thermodynamics of virus binding to receptor. J. Biol. Chem. 270:1995;13216-13224.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13216-13224
    • Casasnovas, J.M.1    Springer, T.A.2
  • 8
    • 0032516060 scopus 로고    scopus 로고
    • A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1
    • Casasnovas J. M., Stehle T., Liu J., Wang J., Springer T. A. A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1. Proc. Natl. Acad. Sci. USA. 95:1998;4134-4139.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4134-4139
    • Casasnovas, J.M.1    Stehle, T.2    Liu, J.3    Wang, J.4    Springer, T.A.5
  • 9
    • 0030907070 scopus 로고    scopus 로고
    • The molecular structure of cell adhesion molecules
    • Chothia C., Jones E. Y. The molecular structure of cell adhesion molecules. Annu. Rev. Biochem. 66:1997;823-862.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 823-862
    • Chothia, C.1    Jones, E.Y.2
  • 10
    • 0028575393 scopus 로고
    • Soluble receptor-resistant poliovirus mutants identify surface and internal capsid residues that control interaction with the cell receptor
    • Colston E., Racaniello V. R. Soluble receptor-resistant poliovirus mutants identify surface and internal capsid residues that control interaction with the cell receptor. EMBO J. 13:1994;5855-5862.
    • (1994) EMBO J. , vol.13 , pp. 5855-5862
    • Colston, E.1    Racaniello, V.R.2
  • 11
    • 0029844847 scopus 로고    scopus 로고
    • The poliovirus 135S particle is infectious
    • Curry S., Chow M., Hogle J. M. The poliovirus 135S particle is infectious. J. Virol. 70:1996;7125-7131.
    • (1996) J. Virol. , vol.70 , pp. 7125-7131
    • Curry, S.1    Chow, M.2    Hogle, J.M.3
  • 12
    • 0031008581 scopus 로고    scopus 로고
    • Cold-adapted poliovirus mutants bypass a postentry replication block
    • Dove A. W., Racaniello V. R. Cold-adapted poliovirus mutants bypass a postentry replication block. J. Virol. 71:1997;4728-4735.
    • (1997) J. Virol. , vol.71 , pp. 4728-4735
    • Dove, A.W.1    Racaniello, V.R.2
  • 13
    • 0022632902 scopus 로고
    • The prevention of rhinovirus and poliovirus uncoating by WIN 51711: A new antiviral drug
    • Fox M. P., Otto M. J., McKinlay M. A. The prevention of rhinovirus and poliovirus uncoating by WIN 51711: A new antiviral drug. Antimicrob. Agents Chemother. 30:1986;110-116.
    • (1986) Antimicrob. Agents Chemother. , vol.30 , pp. 110-116
    • Fox, M.P.1    Otto, M.J.2    McKinlay, M.A.3
  • 14
    • 0025815410 scopus 로고
    • Mutational analysis of the cellular receptor for poliovirus
    • Freistadt M. S., Racaniello V. R. Mutational analysis of the cellular receptor for poliovirus. J. Virol. 65:1991;3873-3876.
    • (1991) J. Virol. , vol.65 , pp. 3873-3876
    • Freistadt, M.S.1    Racaniello, V.R.2
  • 15
    • 0025273268 scopus 로고
    • Cell-induced conformational change in poliovirus: Externalization of the amino terminus of VP1 is responsible for liposome binding
    • Fricks C. E., Hogle J. M. Cell-induced conformational change in poliovirus: Externalization of the amino terminus of VP1 is responsible for liposome binding. J. Virol. 64:1990;1934-1945.
    • (1990) J. Virol. , vol.64 , pp. 1934-1945
    • Fricks, C.E.1    Hogle, J.M.2
  • 18
    • 0029563111 scopus 로고
    • Canyon rim residues, including antigenic determinants, modulate serotype-specific binding of polioviruses to mutants of the poliovirus receptor
    • Harber J., Bernhardt G., Lu H. H., Sgro J. Y., Wimmer E. Canyon rim residues, including antigenic determinants, modulate serotype-specific binding of polioviruses to mutants of the poliovirus receptor. Virology. 214:1995;559-570.
    • (1995) Virology , vol.214 , pp. 559-570
    • Harber, J.1    Bernhardt, G.2    Lu, H.H.3    Sgro, J.Y.4    Wimmer, E.5
  • 21
    • 0022409872 scopus 로고
    • Three-dimensional structure of poliovirus at 2.9 Å resolution
    • Hogle J. M., Chow M., Filman D. J. Three-dimensional structure of poliovirus at 2.9 Å resolution. Science. 229:1985;1358-1365.
    • (1985) Science , vol.229 , pp. 1358-1365
    • Hogle, J.M.1    Chow, M.2    Filman, D.J.3
  • 22
    • 0027473611 scopus 로고
    • Formation of rhinovirus-soluble ICAM-1 complexes and conformational changes in the virion
    • Hoover-Litty H., Greve J. M. Formation of rhinovirus-soluble ICAM-1 complexes and conformational changes in the virion. J. Virol. 67:1993;390-397.
    • (1993) J. Virol. , vol.67 , pp. 390-397
    • Hoover-Litty, H.1    Greve, J.M.2
  • 24
    • 0025882083 scopus 로고
    • Functional domains of the poliovirus receptor
    • Koike S., Ise I., Nomoto A. Functional domains of the poliovirus receptor. Proc. Natl. Acad. Sci. USA. 88:1991;4104-4108.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4104-4108
    • Koike, S.1    Ise, I.2    Nomoto, A.3
  • 26
    • 0033571522 scopus 로고    scopus 로고
    • Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor
    • Kolatkar P. R., Bella J., Olson N. H., Bator C. M., Baker T. S., Rossmann M. G. Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor. EMBO J. 18:1999;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
  • 27
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong P. D., Wyatt R., Robinson J., Sweet R. W., Sodroski J., Hendrickson W. A. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature (London). 393:1998;648-659.
    • (1998) Nature (London) , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 29
    • 0028341259 scopus 로고
    • Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature
    • Li Q., Yafal A. G., Lee Y. M., Hogle J., Chow M. Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature. J. Virol. 68:1994;3965-3970.
    • (1994) J. Virol. , vol.68 , pp. 3965-3970
    • Li, Q.1    Yafal, A.G.2    Lee, Y.M.3    Hogle, J.4    Chow, M.5
  • 30
    • 0030780583 scopus 로고    scopus 로고
    • Allele-specific adaptations to poliovirus VP1 B-C loop variants to mutant cell receptors
    • Liao S., Racaniello V. Allele-specific adaptations to poliovirus VP1 B-C loop variants to mutant cell receptors. J. Virol. 71:1997;9770-9777.
    • (1997) J. Virol. , vol.71 , pp. 9770-9777
    • Liao, S.1    Racaniello, V.2
  • 31
    • 0025887767 scopus 로고
    • Identification of monoclonal antibody epitopes and critical residues for rhinovirus binding in domain 1 of intercellular adhesion molecule-1
    • McClelland A., deBear J., Yost S. C., Meyer A. M., Marlor C. W., Greve J. M. Identification of monoclonal antibody epitopes and critical residues for rhinovirus binding in domain 1 of intercellular adhesion molecule-1. Proc. Natl. Acad. Sci. USA. 88:1991;7993-7997.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7993-7997
    • McClelland, A.1    Debear, J.2    Yost, S.C.3    Meyer, A.M.4    Marlor, C.W.5    Greve, J.M.6
  • 32
    • 0024519677 scopus 로고
    • Cellular receptors for poliovirus: Molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily
    • Mendelsohn C. L., Wimmer E., Racaniello V. R. Cellular receptors for poliovirus: Molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily. Cell. 56:1989;855-865.
    • (1989) Cell , vol.56 , pp. 855-865
    • Mendelsohn, C.L.1    Wimmer, E.2    Racaniello, V.R.3
  • 33
    • 0028214691 scopus 로고
    • Homolog-scanning mutagenesis reveals poliovirus receptor residues important for virus binding and replication
    • Morrison M. E., He Y.-J., Wien M. W., Hogle J. M., Racaniello V. R. Homolog-scanning mutagenesis reveals poliovirus receptor residues important for virus binding and replication. J. Virol. 68:1994;2578-2588.
    • (1994) J. Virol. , vol.68 , pp. 2578-2588
    • Morrison, M.E.1    He, Y.-J.2    Wien, M.W.3    Hogle, J.M.4    Racaniello, V.R.5
  • 35
    • 0024475524 scopus 로고
    • Magnification calibration and the determination of spherical virus diameters using cryo-microscopy
    • Olson N. H., Baker T. S. Magnification calibration and the determination of spherical virus diameters using cryo-microscopy. Ultramicroscopy. 30:1989;281-298.
    • (1989) Ultramicroscopy , vol.30 , pp. 281-298
    • Olson, N.H.1    Baker, T.S.2
  • 37
    • 0000371262 scopus 로고
    • Sequence alignments of picornaviral capsid proteins
    • B. L. Semler, & E. Ehrenfeld. Washington: Am. Soc. Microbiol.
    • Palmenberg A. C. Sequence alignments of picornaviral capsid proteins. Semler B. L., Ehrenfeld E. Molecular Aspects of Picornavirus Infection and Detection. 1989;211-241 Am. Soc. Microbiol. Washington.
    • (1989) Molecular Aspects of Picornavirus Infection and Detection , pp. 211-241
    • Palmenberg, A.C.1
  • 38
    • 0002414459 scopus 로고
    • Molecular targets for antiviral therapy of the common cold
    • Pevear D. C., Diana G. D., McKinlay M. A. Molecular targets for antiviral therapy of the common cold. Semin. Virol. 3:1992;41-55.
    • (1992) Semin. Virol. , vol.3 , pp. 41-55
    • Pevear, D.C.1    Diana, G.D.2    McKinlay, M.A.3
  • 40
    • 0025789993 scopus 로고
    • Human-murine chimeras of ICAM-1 identify amino acid residues critical for rhinovirus and antibody binding
    • Register R. B., Uncapher C. R., Naylor A. M., Lineberger D. W., Colonno R. J. Human-murine chimeras of ICAM-1 identify amino acid residues critical for rhinovirus and antibody binding. J. Virol. 65:1991;6589-6596.
    • (1991) J. Virol. , vol.65 , pp. 6589-6596
    • Register, R.B.1    Uncapher, C.R.2    Naylor, A.M.3    Lineberger, D.W.4    Colonno, R.J.5
  • 41
    • 0028032395 scopus 로고
    • Viral cell recognition and entry
    • Rossmann M. G. Viral cell recognition and entry. Protein Sci. 3:1994;1712-1725.
    • (1994) Protein Sci. , vol.3 , pp. 1712-1725
    • Rossmann, M.G.1
  • 42
    • 0033780164 scopus 로고    scopus 로고
    • Fitting of atomic models into electron microscopy maps
    • Rossmann M. G. Fitting of atomic models into electron microscopy maps. Acta Crystallogr. D. 2000.
    • (2000) Acta Crystallogr. D
    • Rossmann, M.G.1
  • 44
    • 0001952393 scopus 로고
    • Picornaviridae and their replication
    • B. N. Fields, & D. M. Knipe. New York: Raven Press
    • Rueckert R. R. Picornaviridae and their replication. Fields B. N., Knipe D. M. Virology. 1990;507-548 Raven Press, New York.
    • (1990) Virology , pp. 507-548
    • Rueckert, R.R.1
  • 45
    • 0000327130 scopus 로고    scopus 로고
    • Picornaviridae: The viruses and their replication
    • B. N. Fields, D. M. Knipe, & P. M. Howley. New York: Lippincott-Raven Press
    • Rueckert R. R. Picornaviridae: The viruses and their replication. Fields B. N., Knipe D. M., Howley P. M. Virology. 1996;609-654 Lippincott-Raven Press, New York.
    • (1996) Virology , pp. 609-654
    • Rueckert, R.R.1
  • 46
    • 0025870093 scopus 로고
    • Poliovirus can enter and infect mammalian cells by way of an intercellular adhesion molecule 1 pathway
    • Selinka H.-C., Zibert A., Wimmer E. Poliovirus can enter and infect mammalian cells by way of an intercellular adhesion molecule 1 pathway. Proc. Natl. Acad. Sci. USA. 88:1991;3598-3602.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3598-3602
    • Selinka, H.-C.1    Zibert, A.2    Wimmer, E.3
  • 47
    • 0021971892 scopus 로고
    • Evidence for at least two dominant neutralization antigens on human rhinovirus 14
    • Sherry B., Rueckert R. Evidence for at least two dominant neutralization antigens on human rhinovirus 14. J. Virol. 53:1985;137-143.
    • (1985) J. Virol. , vol.53 , pp. 137-143
    • Sherry, B.1    Rueckert, R.2
  • 48
    • 0029743275 scopus 로고    scopus 로고
    • Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon
    • Smith T. J., Chase E. S., Schmidt T. J., Olson N. H., Baker T. S. Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon. Nature (London). 383:1996;350-354.
    • (1996) Nature (London) , vol.383 , pp. 350-354
    • Smith, T.J.1    Chase, E.S.2    Schmidt, T.J.3    Olson, N.H.4    Baker, T.S.5
  • 49
    • 0025269047 scopus 로고
    • The arrangement of the immunoglobulin-like domains of the ICAM-1 and the binding site of LFA-1 and rhinovirus
    • Staunton D. E., Dustin M. L., Erickson H. P., Springer T. A. The arrangement of the immunoglobulin-like domains of the ICAM-1 and the binding site of LFA-1 and rhinovirus. Cell. 61:1990;243-254.
    • (1990) Cell , vol.61 , pp. 243-254
    • Staunton, D.E.1    Dustin, M.L.2    Erickson, H.P.3    Springer, T.A.4
  • 51
    • 0025957484 scopus 로고
    • The major and minor group receptor families contain all but one human rhinovirus serotype
    • Uncapher C. R., DeWitt C. M., Colonno R. J. The major and minor group receptor families contain all but one human rhinovirus serotype. Virology. 180:1991;814-817.
    • (1991) Virology , vol.180 , pp. 814-817
    • Uncapher, C.R.1    Dewitt, C.M.2    Colonno, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.