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Volumn 231, Issue 2, 1997, Pages 281-289

Adaptation of measles virus to polarized epithelial cells: Alterations in virus entry and release

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE COFACTOR PROTEIN;

EID: 0030906793     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1997.8520     Document Type: Article
Times cited : (14)

References (43)
  • 1
    • 0018744621 scopus 로고
    • Purification of measles virus with preservation of infectivity and antigenicity
    • Bellini W. J., Trudgett A., McFarlin D. E. Purification of measles virus with preservation of infectivity and antigenicity. J. Gen. Virol. 43:1979;633-639.
    • (1979) J. Gen. Virol. , vol.43 , pp. 633-639
    • Bellini, W.J.1    Trudgett, A.2    McFarlin, D.E.3
  • 2
    • 84964116705 scopus 로고
    • Propagation of measles in suspension of human and monkey leukocytes
    • Berg R. B., Rosenthal M. S. Propagation of measles in suspension of human and monkey leukocytes. Proc. Soc. Exp. Biol. Med. 106:1961;581-585.
    • (1961) Proc. Soc. Exp. Biol. Med. , vol.106 , pp. 581-585
    • Berg, R.B.1    Rosenthal, M.S.2
  • 3
    • 0029023631 scopus 로고
    • Measles virus entry and release are polarized in epithelial cells
    • Blau D. M., Compans R. W. Measles virus entry and release are polarized in epithelial cells. Virology. 210:1995;91-99.
    • (1995) Virology , vol.210 , pp. 91-99
    • Blau, D.M.1    Compans, R.W.2
  • 4
    • 0030220526 scopus 로고    scopus 로고
    • Polarization of viral entry and release in epithelial cells
    • Blau D. M., Compans R. W. Polarization of viral entry and release in epithelial cells. Semin. Virol. 7:1996;245-253.
    • (1996) Semin. Virol. , vol.7 , pp. 245-253
    • Blau, D.M.1    Compans, R.W.2
  • 6
    • 0023697246 scopus 로고
    • Entry of simian virus 40 is restricted to apical surfaces of polarized epithelial cells
    • Clayson E. T., Compans R. W. Entry of simian virus 40 is restricted to apical surfaces of polarized epithelial cells. Mol. Cell Biol. 8:1988;3391-3396.
    • (1988) Mol. Cell Biol. , vol.8 , pp. 3391-3396
    • Clayson, E.T.1    Compans, R.W.2
  • 7
    • 0027426010 scopus 로고
    • The human CD46 molecule is a receptor for measles virus (Edmonston strain)
    • Dorig E., Marcil A., Chopra A., Richardson C. D. The human CD46 molecule is a receptor for measles virus (Edmonston strain). Cell. 75:1993;295-305.
    • (1993) Cell , vol.75 , pp. 295-305
    • Dorig, E.1    Marcil, A.2    Chopra, A.3    Richardson, C.D.4
  • 9
    • 0021751195 scopus 로고
    • Vesicular stomatitis virus infects and matures only through the basolateral surface of the polarized epithelial cell line, MDCK
    • Fuller S. D., von Bonsdorff C.-H., Simons K. Vesicular stomatitis virus infects and matures only through the basolateral surface of the polarized epithelial cell line, MDCK. Cell. 38:1984;65-77.
    • (1984) Cell , vol.38 , pp. 65-77
    • Fuller, S.D.1    Von Bonsdorff, C.-H.2    Simons, K.3
  • 10
    • 0022135187 scopus 로고
    • Cell surface influenza haemagglutinin can mediate infection by other animal viruses
    • Fuller S. D., von Bonsdorff C.-H., Simons K. Cell surface influenza haemagglutinin can mediate infection by other animal viruses. EMBO J. 4:1985;2475-2485.
    • (1985) EMBO J. , vol.4 , pp. 2475-2485
    • Fuller, S.D.1    Von Bonsdorff, C.-H.2    Simons, K.3
  • 11
    • 0028037919 scopus 로고
    • Measles virus receptor properties are shared by several CD46 isoforms differing in extracellular regions and cytoplasmic tails
    • Gerlier D., Loveland B., Varior-Krishnan G., Thorley B., McKenzie I. F. C., Rabourdin-Combe C. Measles virus receptor properties are shared by several CD46 isoforms differing in extracellular regions and cytoplasmic tails. J. Gen. Virol. 75:1994;2163-2171.
    • (1994) J. Gen. Virol. , vol.75 , pp. 2163-2171
    • Gerlier, D.1    Loveland, B.2    Varior-Krishnan, G.3    Thorley, B.4    McKenzie, I.F.C.5    Rabourdin-Combe, C.6
  • 12
    • 0029037560 scopus 로고
    • Diversity of sites for measles virus binding and for inactivation of complement C3b and C4b on membrane cofactor protein CD46
    • Iwata K., Seya T., Yanagi Y., Pesando J. M., Johnson P. M., Okabe M., Ueda S., Ariga H., Nagasawa S. Diversity of sites for measles virus binding and for inactivation of complement C3b and C4b on membrane cofactor protein CD46. J. Biol. Chem. 270:1995;15148-15152.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15148-15152
    • Iwata, K.1    Seya, T.2    Yanagi, Y.3    Pesando, J.M.4    Johnson, P.M.5    Okabe, M.6    Ueda, S.7    Ariga, H.8    Nagasawa, S.9
  • 13
    • 0023106939 scopus 로고
    • Host cell-mediated variation in H3N2 influenza viruses
    • Katz J. M., Naeve C. W., Webster R. G. Host cell-mediated variation in H3N2 influenza viruses. Virology. 156:1987;386-395.
    • (1987) Virology , vol.156 , pp. 386-395
    • Katz, J.M.1    Naeve, C.W.2    Webster, R.G.3
  • 14
    • 0025060770 scopus 로고
    • Marmoset lymphoblastoid cells as a sensitive host for isolation of measles virus
    • Kobune F., Sakata H., Sugiura A. Marmoset lymphoblastoid cells as a sensitive host for isolation of measles virus. J. Virol. 64:1990;700-705.
    • (1990) J. Virol. , vol.64 , pp. 700-705
    • Kobune, F.1    Sakata, H.2    Sugiura, A.3
  • 15
    • 0028818953 scopus 로고
    • Cell-to-cell contact via measles virus haemagglutinin-CD46 interaction triggers CD46 downregulation
    • Krantic S., Gimenez C., Rabourdin-Combe C. Cell-to-cell contact via measles virus haemagglutinin-CD46 interaction triggers CD46 downregulation. J. Gen. Virol. 76:1995;2793-2800.
    • (1995) J. Gen. Virol. , vol.76 , pp. 2793-2800
    • Krantic, S.1    Gimenez, C.2    Rabourdin-Combe, C.3
  • 16
    • 0025847781 scopus 로고
    • Membrane cofactor protein (MCP or CD46): Newest member of the regulators of complement activation gene cluster
    • Liszewski M. K., Post T. W., Atkinson J. P. Membrane cofactor protein (MCP or CD46): Newest member of the regulators of complement activation gene cluster. Annu. Rev. Immun. 9:1991;431-455.
    • (1991) Annu. Rev. Immun. , vol.9 , pp. 431-455
    • Liszewski, M.K.1    Post, T.W.2    Atkinson, J.P.3
  • 17
    • 0028070628 scopus 로고
    • Binding of measles virus to membrane cofactor protein (CD46): Importance of disulfide bonds and N-glycans for the receptor function
    • Maisner A., Schneider-Schaulies J., Liszewski M. K., Atkinson J. P., Herrler G. Binding of measles virus to membrane cofactor protein (CD46): Importance of disulfide bonds and N-glycans for the receptor function. J. Virol. 68:1994;6299-6304.
    • (1994) J. Virol. , vol.68 , pp. 6299-6304
    • Maisner, A.1    Schneider-Schaulies, J.2    Liszewski, M.K.3    Atkinson, J.P.4    Herrler, G.5
  • 18
    • 0029152104 scopus 로고
    • Membrane cofactor protein with different types of N-glycans can serve as measles virus receptor
    • Maisner A., Herrler G. Membrane cofactor protein with different types of N-glycans can serve as measles virus receptor. Virology. 210:1995;479-481.
    • (1995) Virology , vol.210 , pp. 479-481
    • Maisner, A.1    Herrler, G.2
  • 19
    • 0029946307 scopus 로고    scopus 로고
    • The N-glycan of the SCR 2 region is essential for membrane cofactor protein (CD46) to function as a measles virus receptor
    • Maisner A., Alvarez J., Liszewski M. K., Atkinson D. J., Atkinson J. P., Herrler G. The N-glycan of the SCR 2 region is essential for membrane cofactor protein (CD46) to function as a measles virus receptor. J. Virol. 70:1996a;4973-4977.
    • (1996) J. Virol. , vol.70 , pp. 4973-4977
    • Maisner, A.1    Alvarez, J.2    Liszewski, M.K.3    Atkinson, D.J.4    Atkinson, J.P.5    Herrler, G.6
  • 20
    • 0029780812 scopus 로고    scopus 로고
    • Two different cytoplasmic tails direct isoforms of the membrane cofactor protein (CD46) to the basolateral surface of the Madin-Darby canine kidney cells
    • Maisner A., Liszewski M.K., Atkinson J. P., Schwartz-Albiez R., Herrler G. Two different cytoplasmic tails direct isoforms of the membrane cofactor protein (CD46) to the basolateral surface of the Madin-Darby canine kidney cells. J. Biol. Chem. 271:1996b;18853-18858.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18853-18858
    • Maisner, A.1    Liszewski, M.K.2    Atkinson, J.P.3    Schwartz-Albiez, R.4    Herrler, G.5
  • 21
  • 23
    • 0025351119 scopus 로고
    • Nucleotide sequence analyses of the genes encoding the HN, M, NP, P, and L proteins of two host range mutants of Sendai virus
    • Middleton Y., Tashiro M., Thai T., Oh J., Seymour J., Pritzer E., Klenk H.-D., Rott R., Seto J. T. Nucleotide sequence analyses of the genes encoding the HN, M, NP, P, and L proteins of two host range mutants of Sendai virus. Virology. 176:1990;656-657.
    • (1990) Virology , vol.176 , pp. 656-657
    • Middleton, Y.1    Tashiro, M.2    Thai, T.3    Oh, J.4    Seymour, J.5    Pritzer, E.6    Klenk, H.-D.7    Rott, R.8    Seto, J.T.9
  • 25
    • 0027177368 scopus 로고
    • Measles virus haemagglutinin induces down-regulation of gp57/67, a molecule involved in virus binding
    • Naniche D., Wild T. F., Rabourdin-Combe C., Gerlier D. Measles virus haemagglutinin induces down-regulation of gp57/67, a molecule involved in virus binding. J. Gen. Virol. 74:1993b;1073-1079.
    • (1993) J. Gen. Virol. , vol.74 , pp. 1073-1079
    • Naniche, D.1    Wild, T.F.2    Rabourdin-Combe, C.3    Gerlier, D.4
  • 26
    • 0029058399 scopus 로고
    • Functional and structural interactions between measles virus hemagglutinin and CD46
    • Nussbaum O., Broder C. C., Moss B., Stern L. B.-L., Rozenblatt S., Berger E. A. Functional and structural interactions between measles virus hemagglutinin and CD46. J. Virol. 69:1995;3341-3349.
    • (1995) J. Virol. , vol.69 , pp. 3341-3349
    • Nussbaum, O.1    Broder, C.C.2    Moss, B.3    Stern, L.B.-L.4    Rozenblatt, S.5    Berger, E.A.6
  • 27
    • 0025822399 scopus 로고
    • The human immunodeficiency virus envelope protein determines the site of virus release in polarized epithelial cells
    • Owens R. J., Dubay J. W., Hunter E., Compans R. W. The human immunodeficiency virus envelope protein determines the site of virus release in polarized epithelial cells. Proc. Natl. Acad. Sci. USA. 88:1991;3987-3991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3987-3991
    • Owens, R.J.1    Dubay, J.W.2    Hunter, E.3    Compans, R.W.4
  • 28
    • 0021911623 scopus 로고
    • Alterations in the hemagglutinin associated with adaptation of influenza B virus to growth in eggs
    • Robertson J. S., Naeve C. W., Webster R. G., Bootman J. S., Newman R., Schild G. C. Alterations in the hemagglutinin associated with adaptation of influenza B virus to growth in eggs. Virology. 143:1985;166-174.
    • (1985) Virology , vol.143 , pp. 166-174
    • Robertson, J.S.1    Naeve, C.W.2    Webster, R.G.3    Bootman, J.S.4    Newman, R.5    Schild, G.C.6
  • 30
    • 0018853480 scopus 로고
    • Polarized distribution of viral envelope proteins in the plasma membrane of infected epithelial cells
    • Rodriguez-Boulan E., Pendergast M. Polarized distribution of viral envelope proteins in the plasma membrane of infected epithelial cells. Cell. 20:1980;45-54.
    • (1980) Cell , vol.20 , pp. 45-54
    • Rodriguez-Boulan, E.1    Pendergast, M.2
  • 31
    • 0000747079 scopus 로고
    • Asymmetric budding of viruses in epithelial monolayers: A model system for study of epithelial polarity
    • Rodriguez-Boulan E., Sabatini D. D. Asymmetric budding of viruses in epithelial monolayers: A model system for study of epithelial polarity. Proc. Natl. Acad. Sci. USA. 75:1978;5071-5075.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5071-5075
    • Rodriguez-Boulan, E.1    Sabatini, D.D.2
  • 32
    • 0028114493 scopus 로고
    • Entry and release of transmissible gastroenteritis coronavirus are restricted to apical surfaces of polarized epithelial cells
    • Rossen J. W., Bekker C. P., Voorhout W. F., Strous G. J., van der Ende A., Rottier P. J. Entry and release of transmissible gastroenteritis coronavirus are restricted to apical surfaces of polarized epithelial cells. J. Virol. 68:1994;7966-7973.
    • (1994) J. Virol. , vol.68 , pp. 7966-7973
    • Rossen, J.W.1    Bekker, C.P.2    Voorhout, W.F.3    Strous, G.J.4    Van Der Ende, A.5    Rottier, P.J.6
  • 33
    • 0020770621 scopus 로고
    • Influenza virus hemagglutinin expression is polarized in cells infected with recombinant SV40 viruses carrying cloned hemagglutinin DNA
    • Roth M. G., Compans R. W., Giusti L., Davis A. R., Nayak D. D., Gething M. J., Sambrook J. S. Influenza virus hemagglutinin expression is polarized in cells infected with recombinant SV40 viruses carrying cloned hemagglutinin DNA. Cell. 33:1983a;435-443.
    • (1983) Cell , vol.33 , pp. 435-443
    • Roth, M.G.1    Compans, R.W.2    Giusti, L.3    Davis, A.R.4    Nayak, D.D.5    Gething, M.J.6    Sambrook, J.S.7
  • 34
    • 0020657026 scopus 로고
    • Basolateral maturation of retroviruses in polarized epithelial cells
    • Roth M. G., Srinivas R. V., Compans R. W. Basolateral maturation of retroviruses in polarized epithelial cells. J. Virol. 45:1983b;1065-1073.
    • (1983) J. Virol. , vol.45 , pp. 1065-1073
    • Roth, M.G.1    Srinivas, R.V.2    Compans, R.W.3
  • 37
  • 38
    • 0020413798 scopus 로고
    • Enhanced yields of measles virus from cultured cells
    • Scott J. V., Choppin P. W. Enhanced yields of measles virus from cultured cells. J. Virol. Methods. 5:1982;173-179.
    • (1982) J. Virol. Methods , vol.5 , pp. 173-179
    • Scott, J.V.1    Choppin, P.W.2
  • 40
    • 0025194068 scopus 로고
    • Altered budding site of a pantropic mutant of Sendai virus, F1-R in polarized epithelial cells
    • Tashiro M., Yamakawa M., Tobita K., Seto J. T., Klenk H.-D., Rott R. Altered budding site of a pantropic mutant of Sendai virus, F1-R in polarized epithelial cells. J. Virol. 64:1990a;4672-4677.
    • (1990) J. Virol. , vol.64 , pp. 4672-4677
    • Tashiro, M.1    Yamakawa, M.2    Tobita, K.3    Seto, J.T.4    Klenk, H.-D.5    Rott, R.6
  • 41
    • 0025330794 scopus 로고
    • Organ tropism of Sendai virus in mice: Proteolytic activation of the fusion glycoprotein in mouse organs and budding site at the bronchial epithelium
    • Tashiro M., Yamakawa M., Tobita K., Klenk H.-D., Rott R., Seto J. T. Organ tropism of Sendai virus in mice: Proteolytic activation of the fusion glycoprotein in mouse organs and budding site at the bronchial epithelium. J. Virol. 64:1990b;3627-3634.
    • (1990) J. Virol. , vol.64 , pp. 3627-3634
    • Tashiro, M.1    Yamakawa, M.2    Tobita, K.3    Klenk, H.-D.4    Rott, R.5    Seto, J.T.6
  • 42
    • 0026594699 scopus 로고
    • Budding site of Sendai virus in polarized epithelial cells is one of the determinants for tropism and pathogenicity in mice
    • Tashiro M., Seto J. T., Choosakul S., Yamakawa M., Klenk H.-D., Rott R. Budding site of Sendai virus in polarized epithelial cells is one of the determinants for tropism and pathogenicity in mice. Virology. 187:1992;413-422.
    • (1992) Virology , vol.187 , pp. 413-422
    • Tashiro, M.1    Seto, J.T.2    Choosakul, S.3    Yamakawa, M.4    Klenk, H.-D.5    Rott, R.6
  • 43
    • 0029813302 scopus 로고    scopus 로고
    • Involvement of the mutated M protein in altered budding polarity of a pantropic mutant, F1-R, of Sendai virus
    • Tashiro M., McQueen N. L., Seto J. T., Klenk H.-D., Rott R. Involvement of the mutated M protein in altered budding polarity of a pantropic mutant, F1-R, of Sendai virus. J. Virol. 70:1996;5990-5997.
    • (1996) J. Virol. , vol.70 , pp. 5990-5997
    • Tashiro, M.1    McQueen, N.L.2    Seto, J.T.3    Klenk, H.-D.4    Rott, R.5


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