메뉴 건너뛰기




Volumn 5, Issue 6, 2003, Pages 483-492

Effects of adenovirus-mediated SV5 fusogenic glycoprotein expression on tumor cells

Author keywords

Bystander effect; Cell membrane; Cytotoxicity; Fusogenic protein; Paramyxovirus; SV5; Syncytia; Tumor cell

Indexed keywords

GANCICLOVIR; PROTEIN PRECURSOR; PROTEINASE; THYMIDINE KINASE; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN; VIRUS FUSION PROTEIN;

EID: 1542752193     PISSN: 1099498X     EISSN: None     Source Type: Journal    
DOI: 10.1002/jgm.371     Document Type: Article
Times cited : (10)

References (42)
  • 1
    • 0029006480 scopus 로고
    • Localization of a domain on the paramyxovirus attachment protein required for the promotion of cellular fusion by its homologous fusion protein spike
    • Deng R, Wang Z, Mirza AM, Iorio RM. Localization of a domain on the paramyxovirus attachment protein required for the promotion of cellular fusion by its homologous fusion protein spike. Virology 1995; 209: 457-469.
    • (1995) Virology , vol.209 , pp. 457-469
    • Deng, R.1    Wang, Z.2    Mirza, A.M.3    Iorio, R.M.4
  • 2
    • 0026637939 scopus 로고
    • Biological activity of paramyxovirus fusion proteins: Factors influencing formation of syncytia
    • Horvath CM, Paterson RG, Shaughnessy MA, Wood R, Lamb RA. Biological activity of paramyxovirus fusion proteins: factors influencing formation of syncytia. J Virol 1992; 66: 4564-4569.
    • (1992) J. Virol. , vol.66 , pp. 4564-4569
    • Horvath, C.M.1    Paterson, R.G.2    Shaughnessy, M.A.3    Wood, R.4    Lamb, R.A.5
  • 3
    • 0026525004 scopus 로고
    • Functional interactions between the fusion protein and hemagglutinin-neuraminidase of human parainfluenza viruses
    • Hu X, Ray R, Compans RW. Functional interactions between the fusion protein and hemagglutinin-neuraminidase of human parainfluenza viruses. J Virol 1992; 66: 1528-1534.
    • (1992) J. Virol. , vol.66 , pp. 1528-1534
    • Hu, X.1    Ray, R.2    Compans, R.W.3
  • 4
    • 0026552946 scopus 로고
    • Expression of mumps virus glycoproteins in mammalian cells from cloned cDNAs: Both F and HN proteins are required for cell fusion
    • Tanabayashi K, Takeuchi K, Okazaki K, Hishiyama M, Yamada A. Expression of mumps virus glycoproteins in mammalian cells from cloned cDNAs: both F and HN proteins are required for cell fusion. Virology 1992; 187: 801-804.
    • (1992) Virology , vol.187 , pp. 801-804
    • Tanabayashi, K.1    Takeuchi, K.2    Okazaki, K.3    Hishiyama, M.4    Yamada, A.5
  • 5
    • 0032892508 scopus 로고    scopus 로고
    • Alternative mechanisms of interaction between homotypic and heterotypic parainfluenza virus HN and F proteins
    • Tong S, Compans RW. Alternative mechanisms of interaction between homotypic and heterotypic parainfluenza virus HN and F proteins. J Gen Virol 1999; 80: 107-115.
    • (1999) J. Gen. Virol. , vol.80 , pp. 107-115
    • Tong, S.1    Compans, R.W.2
  • 6
    • 0026058342 scopus 로고
    • Measles virus: Both the hemagglutinin and fusion glycoproteins are required for fusion
    • Wild TF, Malvoisin E, Buckland R. Measles virus: both the hemagglutinin and fusion glycoproteins are required for fusion. J Gen Virol 1991; 72: 439-442.
    • (1991) J. Gen. Virol. , vol.72 , pp. 439-442
    • Wild, T.F.1    Malvoisin, E.2    Buckland, R.3
  • 7
    • 0001561789 scopus 로고
    • Activation cleavage of viral spike proteins by host proteases
    • Wimmer E (ed.). NT: Cold Spring Harbor
    • Klenk HD, Garten W. Activation cleavage of viral spike proteins by host proteases. In Cellular Receptors for Animal Viruses Wimmer E (ed.). NT: Cold Spring Harbor, 1994; 241-280.
    • (1994) Cellular Receptors for Animal Viruses , pp. 241-280
    • Klenk, H.D.1    Garten, W.2
  • 8
    • 0001178028 scopus 로고    scopus 로고
    • Paramyxoviridae: The viruses and their replication
    • Fields BN, Knipe DM, Howley PM (eds). Lippincot-Raven Publishers: Philadelphia
    • Lamb RA, Kolakofsky D. Paramyxoviridae: the viruses and their replication. In Fields Virology, Fields BN, Knipe DM, Howley PM (eds). Lippincot-Raven Publishers: Philadelphia, 1996.
    • (1996) Fields Virology
    • Lamb, R.A.1    Kolakofsky, D.2
  • 9
    • 0034443993 scopus 로고    scopus 로고
    • Common properties of fusion peptides from diverse systems
    • Martin I, Ruysschaert JM. Common properties of fusion peptides from diverse systems.Biosci Reports 2000; 20: 483-500.
    • (2000) Biosci. Reports , vol.20 , pp. 483-500
    • Martin, I.1    Ruysschaert, J.M.2
  • 10
    • 0034440326 scopus 로고    scopus 로고
    • Insights into a structured-based mechanisms of viral membrane fusion
    • LeDuc DL, Shin Y-K. Insights into a structured-based mechanisms of viral membrane fusion. Biosci Reports 2000; 20: 557-570.
    • (2000) Biosci. Reports , vol.20 , pp. 557-570
    • LeDuc, D.L.1    Shin, Y.-K.2
  • 11
    • 0030776258 scopus 로고    scopus 로고
    • Membrane rearrangements in fusion mediated by viral proteins
    • Melikyan GB, Chernomordik LV. Membrane rearrangements in fusion mediated by viral proteins. Trends Microbiol 1997; 5: 349-355.
    • (1997) Trends Microbiol. , vol.5 , pp. 349-355
    • Melikyan, G.B.1    Chernomordik, L.V.2
  • 12
    • 0033591307 scopus 로고    scopus 로고
    • Are the fusion processes involved in birth, life and death of the cell depending on tilted insertion of peptides into membranes?
    • Peuvot J, Schanck A, Lins L, Brasseurs R. Are the fusion processes involved in birth, life and death of the cell depending on tilted insertion of peptides into membranes? J Theor Biol 1999; 198: 173-181.
    • (1999) J. Theor. Biol. , vol.198 , pp. 173-181
    • Peuvot, J.1    Schanck, A.2    Lins, L.3    Brasseurs, R.4
  • 13
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel JJ, Wiley DC. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell 1998; 95: 871-874.
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 14
    • 0027430672 scopus 로고
    • Paramyxovirus fusion: A hypothesis for changes
    • Lamb RA. Paramyxovirus fusion: a hypothesis for changes. Virology 1993; 197: 1-11.
    • (1993) Virology , vol.197 , pp. 1-11
    • Lamb, R.A.1
  • 15
  • 16
    • 0034653696 scopus 로고    scopus 로고
    • Fusogenic membrane glycoproteins as a novel class of genes for the local and immune-mediated control of tumor growth
    • Bateman A, Bullough F, Murphy S, et al. Fusogenic membrane glycoproteins as a novel class of genes for the local and immune-mediated control of tumor growth. Cancer Res 2000; 60: 1492-1497.
    • (2000) Cancer Res. , vol.60 , pp. 1492-1497
    • Bateman, A.1    Bullough, F.2    Murphy, S.3
  • 17
    • 0033692809 scopus 로고    scopus 로고
    • Viral fusogenic membrane glycoprotein expression causes syncytia formation with bioenergetic cell death: Implications for gene therapy
    • Higuchi H, Bronk SF, Bateman A, Harrington K, Vile RG, Gores GJ. Viral fusogenic membrane glycoprotein expression causes syncytia formation with bioenergetic cell death: implications for gene therapy. Cancer Res 2000; 60: 6396-6402.
    • (2000) Cancer Res. , vol.60 , pp. 6396-6402
    • Higuchi, H.1    Bronk, S.F.2    Bateman, A.3    Harrington, K.4    Vile, R.G.5    Gores, G.J.6
  • 18
    • 0034926686 scopus 로고    scopus 로고
    • Use of viral fusogenic membrane glycoproteins as novel therapeutic transgene in gliomas
    • Galanis E, Bateman A, Johnson K, et al. Use of viral fusogenic membrane glycoproteins as novel therapeutic transgene in gliomas. Hum Gene Ther 2001; 12: 811-821.
    • (2001) Hum. Gene Ther. , vol.12 , pp. 811-821
    • Galanis, E.1    Bateman, A.2    Johnson, K.3
  • 20
    • 0033959447 scopus 로고    scopus 로고
    • Cancer gene therapy: Hard lessons and new courses
    • Vile RG, Russell SJ, Lemoin NR. Cancer gene therapy: hard lessons and new courses. Gene Ther 2000; 7: 2-8.
    • (2000) Gene Ther. , vol.7 , pp. 2-8
    • Vile, R.G.1    Russell, S.J.2    Lemoin, N.R.3
  • 21
    • 0033106334 scopus 로고    scopus 로고
    • Stractural basis for paramyxovirus-mediated membrane fusion
    • Baker K, Dutch RE, Lamb RA, Jardetzky TS. Stractural basis for paramyxovirus-mediated membrane fusion. Mol Cell 1999; 3: 309-319.
    • (1999) Mol. Cell , vol.3 , pp. 309-319
    • Baker, K.1    Dutch, R.E.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 22
    • 0028690027 scopus 로고
    • Use of recombinant adenovirus for metabolic engineering of mammalian cells
    • Becker TC, Noel RJ, Coats WS, et al. Use of recombinant adenovirus for metabolic engineering of mammalian cells. Methods Cell Biol 1994; 5: 161-189.
    • (1994) Methods Cell Biol. , vol.5 , pp. 161-189
    • Becker, T.C.1    Noel, R.J.2    Coats, W.S.3
  • 23
    • 0023442009 scopus 로고
    • Isolation and characterization of monoclonal antibodies to simian virus 5 and their use in revealing antigenic differences between human, canine and simian isolated
    • Randall RE, Young DF, Goswami KKA, Russell WC. Isolation and characterization of monoclonal antibodies to simian virus 5 and their use in revealing antigenic differences between human, canine and simian isolated. J Gen Virol 1987; 68: 2769-2789.
    • (1987) J. Gen. Virol. , vol.68 , pp. 2769-2789
    • Randall, R.E.1    Young, D.F.2    Goswami, K.K.A.3    Russell, W.C.4
  • 24
    • 0028851288 scopus 로고
    • Temperature dependence of cell-cell fusion induced by the envelope glycoprotein of human immunodeficiency virus type I
    • Frey S, Marsh M, Gunther S, et al. Temperature dependence of cell-cell fusion induced by the envelope glycoprotein of human immunodeficiency virus type I. J Virol 1995; 69: 1462-1472.
    • (1995) J. Virol. , vol.69 , pp. 1462-1472
    • Frey, S.1    Marsh, M.2    Gunther, S.3
  • 25
    • 0029762913 scopus 로고    scopus 로고
    • Improving stractural integrity of cryosections for immunogold labeling
    • Liou W, Geuze HJ, Slot JW. Improving stractural integrity of cryosections for immunogold labeling. Histochem Cell Biol 1996; 106: 41-58.
    • (1996) Histochem. Cell Biol. , vol.106 , pp. 41-58
    • Liou, W.1    Geuze, H.J.2    Slot, J.W.3
  • 26
    • 0002478233 scopus 로고    scopus 로고
    • Immunolabeling of ultrathin cryosections: Application in immunology
    • Herzenberg LA, Weir D, Blackwell C (eds). Blackwell Science: Cambridge, MA
    • Raposo G, Kleijmeer MJ, Posthuma G, Slot JW, Geuze HJ. Immunolabeling of ultrathin cryosections: application in immunology. In Handbook of Experimental Immunology, vol. 4, Herzenberg LA, Weir D, Blackwell C (eds). Blackwell Science: Cambridge, MA, 1997; 1-11.
    • (1997) Handbook of Experimental Immunology , vol.4 , pp. 1-11
    • Raposo, G.1    Kleijmeer, M.J.2    Posthuma, G.3    Slot, J.W.4    Geuze, H.J.5
  • 27
    • 0028074962 scopus 로고
    • Replicating vectors for gene therapy of cancer: Risks, limitations and prospects
    • Russell SJ. Replicating vectors for gene therapy of cancer: risks, limitations and prospects. Eur J Cancer 1994; 30A: 1165-1171.
    • (1994) Eur. J. Cancer , vol.30 A , pp. 1165-1171
    • Russell, S.J.1
  • 28
    • 0034445297 scopus 로고    scopus 로고
    • Virus membrane fusion proteins: Biological machines that undergo a metamorphosis
    • Dutch RE, Jardetzky TS, Lamb RA. Virus membrane fusion proteins: biological machines that undergo a metamorphosis. Biosci Reports 2000; 20: 597-612.
    • (2000) Biosci. Reports , vol.20 , pp. 597-612
    • Dutch, R.E.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 29
    • 0035695874 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1-mediated syncytium formation is compatible with adenovirus replication and facilitates efficient dispersion of viral gene products and de novo synthesized viras particles
    • Li H, Haviv YS, Derdeyn CA, et al. Human immunodeficiency virus type 1-mediated syncytium formation is compatible with adenovirus replication and facilitates efficient dispersion of viral gene products and de novo synthesized viras particles. Hum Gene Ther 2001; 12: 2155-2165.
    • (2001) Hum. Gene Ther. , vol.12 , pp. 2155-2165
    • Li, H.1    Haviv, Y.S.2    Derdeyn, C.A.3
  • 30
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble GW, Danieli T, White JM. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell 1994; 76: 383-391.
    • (1994) Cell , vol.76 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 31
    • 0034442294 scopus 로고    scopus 로고
    • Mechanisms of initiation of membrane fusion: Role of lipids
    • Kinnunen PKJ, Holopainen JM. Mechanisms of initiation of membrane fusion: role of lipids. Biosci Reports 2000; 20: 465-482.
    • (2000) Biosci. Reports , vol.20 , pp. 465-482
    • Kinnunen, P.K.J.1    Holopainen, J.M.2
  • 32
    • 0031795752 scopus 로고    scopus 로고
    • Lipid polymorphism and protein lipid interactions
    • Epand RM. Lipid polymorphism and protein lipid interactions. Biochim Biophys Acta 1998; 1376: 353-368.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 353-368
    • Epand, R.M.1
  • 33
    • 0035942298 scopus 로고    scopus 로고
    • Sensitivity of single membrane-spanning R-helical peptides to hydrophobic mismatch with a lipid bilayer: Effects on backbone structure, orientation and extent of membrane incorporation
    • Kraijtzer JAW, Liskamp RMJ, de Kruijff B, Killian A. Sensitivity of single membrane-spanning R-helical peptides to hydrophobic mismatch with a lipid bilayer: effects on backbone structure, orientation and extent of membrane incorporation.Biochemistry 2001; 40: 5000-5010.
    • (2001) Biochemistry , vol.40 , pp. 5000-5010
    • Kraijtzer, J.A.W.1    Liskamp, R.M.J.2    de Kruijff, B.3    Killian, A.4
  • 34
    • 0034164025 scopus 로고    scopus 로고
    • Interactions of peptides with liposomes: Pore formation and fusion
    • Nir S, Nieva JL. Interactions of peptides with liposomes: pore formation and fusion, Prog Lipid Res 2000; 39: 181-206.
    • (2000) Prog. Lipid Res. , vol.39 , pp. 181-206
    • Nir, S.1    Nieva, J.L.2
  • 35
    • 0034673978 scopus 로고    scopus 로고
    • Visualization of highly ordered striated domains induced by transmembrane peptides in supported phosphatidylcholine bilayers
    • Rinia A, Kik RA, Demel RA, et al. Visualization of highly ordered striated domains induced by transmembrane peptides in supported phosphatidylcholine bilayers. Biochemistry 2000; 39 5852-5858.
    • (2000) Biochemistry , vol.39 , pp. 5852-5858
    • Rinia, A.1    Kik, R.A.2    Demel, R.A.3
  • 36
    • 13344282745 scopus 로고
    • Human immunodeficiency viras 1 envelope-initiated G2-phase programed cell death
    • Kolesnitchenko V, Wahl LM, Tian H, et al. Human immunodeficiency viras 1 envelope-initiated G2-phase programed cell death. Proc Natl Acad Sci U S A 1995; 92: 11 889-11 893.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 11889-11893
    • Kolesnitchenko, V.1    Wahl, L.M.2    Tian, H.3
  • 37
    • 0023248494 scopus 로고
    • Comparison of the relative roles of the F and HN surface glycoproteins of the paramyxovirus Simian virus 5 in inducing protective immunity
    • Paterson RG, Lamb RA, Moss B, Murphy BR. Comparison of the relative roles of the F and HN surface glycoproteins of the paramyxovirus Simian virus 5 in inducing protective immunity. J Virol 1987; 61 1972-1977.
    • (1987) J. Virol. , vol.61 , pp. 1972-1977
    • Paterson, R.G.1    Lamb, R.A.2    Moss, B.3    Murphy, B.R.4
  • 38
    • 0030909584 scopus 로고    scopus 로고
    • Comparative analysis of expression of the protein convertases furin, PACE4, PC1 and PC2, in human lung tumours
    • Mbaky M, Sirois F, Yao J, Seidah NG, Chretien M. Comparative analysis of expression of the protein convertases furin, PACE4, PC1 and PC2, in human lung tumours. Br J Cancer 1997; 75: 1509-1514.
    • (1997) Br. J. Cancer , vol.75 , pp. 1509-1514
    • Mbaky, M.1    Sirois, F.2    Yao, J.3    Seidah, N.G.4    Chretien, M.5
  • 40
    • 0023520009 scopus 로고
    • Fur gene expression as a discriminating marker for small cell and nonsmall cell lung carcinomas
    • Schalke JA, Roebroek JM, Oomen PPCA, et al. Fur gene expression as a discriminating marker for small cell and nonsmall cell lung carcinomas. J Clin Invest 1987; 80: 1545-1549.
    • (1987) J. Clin. Invest. , vol.80 , pp. 1545-1549
    • Schalke, J.A.1    Roebroek, J.M.2    Oomen, P.P.C.A.3
  • 41
    • 0029917238 scopus 로고    scopus 로고
    • Targeting of retroviral vectors through protease-substrate interactions
    • Nilson BH, Morling FJ, Cosset FL, Russell SJ. Targeting of retroviral vectors through protease-substrate interactions. Gene Ther 1996; 3: 280-286.
    • (1996) Gene Ther. , vol.3 , pp. 280-286
    • Nilson, B.H.1    Morling, F.J.2    Cosset, F.L.3    Russell, S.J.4
  • 42
    • 0032846999 scopus 로고    scopus 로고
    • Selective transduction of protease-rich tumors by matrix-metalloproteinase-targeted retroviral vectors
    • Peng KW, Vile R, Cosset FL, Russell SJ. Selective transduction of protease-rich tumors by matrix-metalloproteinase-targeted retroviral vectors. Gene Ther 1999; 6: 1552-1557.
    • (1999) Gene Ther. , vol.6 , pp. 1552-1557
    • Peng, K.W.1    Vile, R.2    Cosset, F.L.3    Russell, S.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.