메뉴 건너뛰기




Volumn 110, Issue 1, 1997, Pages 95-103

SFV infection in CHO cells: cell-type specific restrictions to productive virus entry at the cell surface

Author keywords

Membrane fusion; Semliki forest virus; Virus entry

Indexed keywords

ANIMAL CELL; ARTICLE; CELL ORGANELLE; CELL STRAIN BHK; CELL SURFACE; CHO CELL; ENDOCYTOSIS; ENDOSOME; MEMBRANE FUSION; NONHUMAN; PRIORITY JOURNAL; SEMLIKI FOREST ALPHAVIRUS; VESICULAR STOMATITIS VIRUS; VIRION; VIRUS CELL INTERACTION; VIRUS INFECTION;

EID: 0031026138     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (87)

References (55)
  • 2
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G. and Dyer, W. J. (1959). A rapid method of total lipid extraction and purification. Can. J. Biochem. Biophysiol. 37, 911-913.
    • (1959) Can. J. Biochem. Biophysiol. , vol.37 , pp. 911-913
    • Bligh, E.G.1    Dyer, W.J.2
  • 3
    • 50549164858 scopus 로고
    • A rapid and sensitive sub-micro phosphorus determination
    • Böttcher, C. J. F., van Gent, C. M. and Fries, C. (1961). A rapid and sensitive sub-micro phosphorus determination. Anal. Chim. Acta 24, 203-204.
    • (1961) Anal. Chim. Acta , vol.24 , pp. 203-204
    • Böttcher, C.J.F.1    Van Gent, C.M.2    Fries, C.3
  • 4
    • 0022507515 scopus 로고
    • The membrane-associated 'cortex' of animal cells: Its structure and mechanical properties
    • Bray, D., Heath, J. and Moss, D. (1986). The membrane-associated 'cortex' of animal cells: its structure and mechanical properties. J. Cell Sci. Suppl. 4, 71-88.
    • (1986) J. Cell Sci. Suppl. , vol.4 , pp. 71-88
    • Bray, D.1    Heath, J.2    Moss, D.3
  • 5
    • 0027509351 scopus 로고
    • Membrane fusion of Semliki Forest virus in a model system: Correlation between fusion kinetics and structural changes in the envelope glycoprotein
    • Bron, R., Wahlberg, J. M., Garoff, H. and Wilschut, J. (1993). Membrane fusion of Semliki Forest virus in a model system: Correlation between fusion kinetics and structural changes in the envelope glycoprotein. EMBO J. 12, 693-702.
    • (1993) EMBO J. , vol.12 , pp. 693-702
    • Bron, R.1    Wahlberg, J.M.2    Garoff, H.3    Wilschut, J.4
  • 6
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., Hughson, F. M., Skehel, J. J. and Wiley, D. C. (1994). Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371, 37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 7
    • 0028866712 scopus 로고
    • Actin-based motility of vaccinia virus
    • Cudmore, S., Cossart, P., Griffiths, G. and Way, M. (1995). Actin-based motility of vaccinia virus. Nature 378, 636-638.
    • (1995) Nature , vol.378 , pp. 636-638
    • Cudmore, S.1    Cossart, P.2    Griffiths, G.3    Way, M.4
  • 8
    • 0023464728 scopus 로고
    • Two threshold values of low pH block endocytosis at different stages
    • Davoust, J., Gruenberg, J. and Howell, K. E. (1987). Two threshold values of low pH block endocytosis at different stages. EMBO J. 6, 3601-3609.
    • (1987) EMBO J. , vol.6 , pp. 3601-3609
    • Davoust, J.1    Gruenberg, J.2    Howell, K.E.3
  • 9
    • 0021984076 scopus 로고
    • Membrane fusion activity of influenza virus hemagglutinin. The low pH-induced conformational change
    • Doms, R. W., Helenius, A. and White, J. (1985). Membrane fusion activity of influenza virus hemagglutinin. The low pH-induced conformational change. J. Biol. Chem. 260, 2673-2981.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2673-2981
    • Doms, R.W.1    Helenius, A.2    White, J.3
  • 10
    • 0030042764 scopus 로고    scopus 로고
    • Actin filaments facilitate two steps of endocytosis
    • Durrbach, A., Louvard, D. and Coudrier, E. (1996). Actin filaments facilitate two steps of endocytosis. J. Cell Sci. 109, 457-465.
    • (1996) J. Cell Sci. , vol.109 , pp. 457-465
    • Durrbach, A.1    Louvard, D.2    Coudrier, E.3
  • 12
    • 0018483433 scopus 로고
    • Binding of Semliki Forest virus and its isolated glycoprotein to cells
    • Fries, E. and Helenius, A. (1979). Binding of Semliki Forest virus and its isolated glycoprotein to cells. Eur. J. Biochem. 97, 213-220.
    • (1979) Eur. J. Biochem. , vol.97 , pp. 213-220
    • Fries, E.1    Helenius, A.2
  • 13
    • 0024237292 scopus 로고
    • Alphavirus RNA replication on the cytoplasmic surface of endosomes and lysosomes
    • Froshauer, S., Kartenbeck, J. and Helenius, A. (1988). Alphavirus RNA replication on the cytoplasmic surface of endosomes and lysosomes. J. Cell Biol. 107, 2075-2086.
    • (1988) J. Cell Biol. , vol.107 , pp. 2075-2086
    • Froshauer, S.1    Kartenbeck, J.2    Helenius, A.3
  • 14
    • 0022483707 scopus 로고
    • The uncoating and infectivity of the flavivirus West Nile on interaction with cells: Effects of pH and ammonium chloride
    • Gollins, S. W. and Porterfield, J. S. (1986). The uncoating and infectivity of the flavivirus West Nile on interaction with cells: Effects of pH and ammonium chloride. J. Gen. Virol. 67, 1941-1950.
    • (1986) J. Gen. Virol. , vol.67 , pp. 1941-1950
    • Gollins, S.W.1    Porterfield, J.S.2
  • 15
    • 0027469161 scopus 로고
    • Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells
    • Gottlieb, T. A., Ivanov, I. E., Adesnik, M. and Sabatini, D. D. (1993). Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells. J. Cell Biol. 120, 695-710.
    • (1993) J. Cell Biol. , vol.120 , pp. 695-710
    • Gottlieb, T.A.1    Ivanov, I.E.2    Adesnik, M.3    Sabatini, D.D.4
  • 16
    • 0018853517 scopus 로고
    • On the entry of Semliki Forest virus into BHK-21 cells
    • Helenius, A., Kartenbeck, J., Simons, K. and Fries, E. (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
  • 18
    • 0020042010 scopus 로고
    • Effect of lysosomotropic weak bases on Semliki Forest virus penetration into host cells
    • Helenius, A., Marsh, M. and White, J. (1982). Effect of lysosomotropic weak bases on Semliki Forest virus penetration into host cells. J. Gen. Virol. 58, 47-61.
    • (1982) J. Gen. Virol. , vol.58 , pp. 47-61
    • Helenius, A.1    Marsh, M.2    White, J.3
  • 19
    • 0021675842 scopus 로고
    • Semliki Forest virus penetration from endosomes: A morphological study
    • Helenius, A. (1984). Semliki Forest virus penetration from endosomes: a morphological study. Biol. Cell 51, 181-186.
    • (1984) Biol. Cell , vol.51 , pp. 181-186
    • Helenius, A.1
  • 21
    • 0028085551 scopus 로고
    • Inhibition of apical but not basolateral endocytosis of ricin and folate in Caco-2 cells by cytochalasin D.
    • Jackman, M. R., Shurety, W., Ellis, J. A. and Luzio, J. P. (1994). Inhibition of apical but not basolateral endocytosis of ricin and folate in Caco-2 cells by cytochalasin D. J. Cell Sci. 107, 2547-2556.
    • (1994) J. Cell Sci. , vol.107 , pp. 2547-2556
    • Jackman, M.R.1    Shurety, W.2    Ellis, J.A.3    Luzio, J.P.4
  • 22
    • 0027237639 scopus 로고
    • Role of microtubules in transferrin receptor transport from the cell surface to endosomes and the Golgi complex
    • Jin, M. and Snider, M. D. (1993). Role of microtubules in transferrin receptor transport from the cell surface to endosomes and the Golgi complex. J. Biol. Chem. 268, 18390-18397.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18390-18397
    • Jin, M.1    Snider, M.D.2
  • 24
    • 0022273625 scopus 로고
    • pH-induced alterations in the fusogenic spike protein of Semliki Forest Virus
    • Kielian, M. and Helenius, A. (1985). pH-induced alterations in the fusogenic spike protein of Semliki Forest Virus. J. Cell Biol. 101, 2284-2291.
    • (1985) J. Cell Biol. , vol.101 , pp. 2284-2291
    • Kielian, M.1    Helenius, A.2
  • 25
    • 0025373110 scopus 로고
    • Mechanisms of enveloped virus entry into cells
    • Kielian, M. and Jungerwirth, S. (1990). Mechanisms of enveloped virus entry into cells. Mol. Biol. Med. 7, 17-31.
    • (1990) Mol. Biol. Med. , vol.7 , pp. 17-31
    • Kielian, M.1    Jungerwirth, S.2
  • 26
    • 0028152964 scopus 로고
    • Membrane and rotein interactions of a soluble form of the Semliki Forest virus fusion protein
    • Klimjack, M. R., Jeffrey, S. and Kielian, M. (1994). Membrane and rotein interactions of a soluble form of the Semliki Forest virus fusion protein. J. Virol. 68, 6940-6946.
    • (1994) J. Virol. , vol.68 , pp. 6940-6946
    • Klimjack, M.R.1    Jeffrey, S.2    Kielian, M.3
  • 28
    • 0019256559 scopus 로고
    • Adsorptive endocytosis of Semliki Forest virus
    • Marsh, M. and Helenius, A. (1980). Adsorptive endocytosis of Semliki Forest virus. J. Mol. Biol. 142, 439-454.
    • (1980) J. Mol. Biol. , vol.142 , pp. 439-454
    • Marsh, M.1    Helenius, A.2
  • 30
    • 0020724144 scopus 로고
    • Semliki Forest virus penetration occurs from acid prelysosomal vacuoles
    • Marsh, M., Bolzau, E. and Helenius, A. (1983). Semliki Forest virus penetration occurs from acid prelysosomal vacuoles. Cell 32, 931-940.
    • (1983) Cell , vol.32 , pp. 931-940
    • Marsh, M.1    Bolzau, E.2    Helenius, A.3
  • 31
    • 0024534779 scopus 로고
    • Virus entry into animal cells
    • Marsh, M. and Helenius, A. (1989). Virus entry into animal cells. Advan. Virus Res. 36, 107-151.
    • (1989) Advan. Virus Res. , vol.36 , pp. 107-151
    • Marsh, M.1    Helenius, A.2
  • 32
    • 0019814443 scopus 로고
    • Infectious entry pathway of influenza virus in a canine kidney cell line
    • Matlin, K. S., Reggio, H., Helenius, A. and Simons, K. (1981). Infectious entry pathway of influenza virus in a canine kidney cell line. J. Cell Biol. 91, 601-613.
    • (1981) J. Cell Biol. , vol.91 , pp. 601-613
    • Matlin, K.S.1    Reggio, H.2    Helenius, A.3    Simons, K.4
  • 33
    • 0019976569 scopus 로고
    • Pathway of vesicular stomatitis virus entry leading to infection
    • Matlin, K. S., Reggio, H., Helenius, A. and Simons, K. (1982). Pathway of vesicular stomatitis virus entry leading to infection. J. Mol. Biol. 156, 609-631.
    • (1982) J. Mol. Biol. , vol.156 , pp. 609-631
    • Matlin, K.S.1    Reggio, H.2    Helenius, A.3    Simons, K.4
  • 34
    • 0023954154 scopus 로고
    • Human immunodeficiency virus infection of CD4-bearing cells occurs by a pH-independent mechanism
    • McClure, M. O., Marsh, M. and Weiss, R. A. (1988). Human immunodeficiency virus infection of CD4-bearing cells occurs by a pH-independent mechanism. EMBO J. 7, 513-518.
    • (1988) EMBO J. , vol.7 , pp. 513-518
    • McClure, M.O.1    Marsh, M.2    Weiss, R.A.3
  • 36
    • 0025872373 scopus 로고
    • Penetration of CD4 T cells by HIV-1. The CD4 receptor does not internalise with HIV, and CD4-related signal transduction events are not required for entry
    • Orloff, G. M., Orloff, S. L., Kennedy, M. S., Maddon, P. J. and McDougal, J. S. (1991). Penetration of CD4 T cells by HIV-1. The CD4 receptor does not internalise with HIV, and CD4-related signal transduction events are not required for entry. J. Immunol. 146, 2578-2587.
    • (1991) J. Immunol. , vol.146 , pp. 2578-2587
    • Orloff, G.M.1    Orloff, S.L.2    Kennedy, M.S.3    Maddon, P.J.4    McDougal, J.S.5
  • 37
    • 0028824903 scopus 로고
    • The role of CD4 endocytosis in HIV infection
    • Pelchen-Matthews, A., Clapham, P. and Marsh, M. (1995). The role of CD4 endocytosis in HIV infection. J. Virol. 69, 8164-8168.
    • (1995) J. Virol. , vol.69 , pp. 8164-8168
    • Pelchen-Matthews, A.1    Clapham, P.2    Marsh, M.3
  • 38
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson, G. L. (1977). A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem 83, 346-356.
    • (1977) Anal Biochem , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 39
    • 0028092765 scopus 로고
    • Electron microscopic analysis of HIV-host cell interactions
    • Pudney, J. and Song, M. J. (1994). Electron microscopic analysis of HIV-host cell interactions. Tissue & Cell 26, 539-550.
    • (1994) Tissue & Cell , vol.26 , pp. 539-550
    • Pudney, J.1    Song, M.J.2
  • 40
    • 0026567676 scopus 로고
    • Membrane fusion process of Semliki Forest virus. II: Cleavage-dependent reorganization of the spike protein complex controls virus entry
    • Salminen, A., Wahlberg, J. M., Lobigs, M., Liljestrom, P. and Garoff, H. (1992). Membrane fusion process of Semliki Forest virus. II: Cleavage-dependent reorganization of the spike protein complex controls virus entry. J. Cell Biol. 116, 349-357.
    • (1992) J. Cell Biol. , vol.116 , pp. 349-357
    • Salminen, A.1    Wahlberg, J.M.2    Lobigs, M.3    Liljestrom, P.4    Garoff, H.5
  • 41
    • 0023582912 scopus 로고
    • Acidification of the cytosol inhibits endocytosis from coated pits
    • Sandvig, K., Olsnes, S., Petersen, O. W. and van Deurs, B. (1987). Acidification of the cytosol inhibits endocytosis from coated pits. J. Cell. Biol. 105, 679-689.
    • (1987) J. Cell. Biol. , vol.105 , pp. 679-689
    • Sandvig, K.1    Olsnes, S.2    Petersen, O.W.3    Van Deurs, B.4
  • 42
    • 0026013758 scopus 로고
    • Non-viral cellular substrates for human immunodeficiency virus type 1 protease
    • Shoeman, R. L., Kesselmier, C., Mothes, E., Honer, B. and Traub, P. (1991). Non-viral cellular substrates for human immunodeficiency virus type 1 protease. FEBS Lett. 278, 199-203.
    • (1991) FEBS Lett. , vol.278 , pp. 199-203
    • Shoeman, R.L.1    Kesselmier, C.2    Mothes, E.3    Honer, B.4    Traub, P.5
  • 43
    • 0027529843 scopus 로고
    • Cleavage of human and mouse cytoskeletal and sarcomeric proteins by human immunodeficiency virus type 1 protease. Actin, desmin, myosin, and tropomyosin
    • Shoeman, R. L., Sachse, C., Honer, B., Mothes, E., Kaufmann, M. and Traub, P. (1993). Cleavage of human and mouse cytoskeletal and sarcomeric proteins by human immunodeficiency virus type 1 protease. Actin, desmin, myosin, and tropomyosin. Am. J. Pathol. 142, 221-230.
    • (1993) Am. J. Pathol. , vol.142 , pp. 221-230
    • Shoeman, R.L.1    Sachse, C.2    Honer, B.3    Mothes, E.4    Kaufmann, M.5    Traub, P.6
  • 44
    • 0026490846 scopus 로고
    • Role of ribosomes in Semliki Forest virus nucleocapsid uncoating
    • Singh, I. and Helenius, A. (1992). Role of ribosomes in Semliki Forest virus nucleocapsid uncoating. J. Virol. 66, 7049-7058.
    • (1992) J. Virol. , vol.66 , pp. 7049-7058
    • Singh, I.1    Helenius, A.2
  • 45
    • 0025647464 scopus 로고
    • Intermediates in influenza induced membrane fusion
    • Stegmann, T., White, J. M. and Helenius, A. (1990). Intermediates in influenza induced membrane fusion. EMBO J. 9, 4231-4241.
    • (1990) EMBO J. , vol.9 , pp. 4231-4241
    • Stegmann, T.1    White, J.M.2    Helenius, A.3
  • 46
    • 0027434098 scopus 로고
    • Evaluation of membrane fusion assays. Comparison of the octadecylrhodamine dequenching assay with the pyrene excimer assay
    • Stegmann, T., Schoen, P., Bron, R., Wey, J., Bartoldus, I., Nieva, J. L., Ortiz, A. and Wilschut, J. (1993). Evaluation of membrane fusion assays. Comparison of the octadecylrhodamine dequenching assay with the pyrene excimer assay. Biochemistry 32, 11330-11337.
    • (1993) Biochemistry , vol.32 , pp. 11330-11337
    • Stegmann, T.1    Schoen, P.2    Bron, R.3    Wey, J.4    Bartoldus, I.5    Nieva, J.L.6    Ortiz, A.7    Wilschut, J.8
  • 47
    • 0023644926 scopus 로고
    • pH-independent HIV entry into CD4-positive cells via virus envelope fusion to the plasma membrane
    • Stein, B. S., Gowda, S. D., Lifson, J. D., Penhallow, R. C., Bensch, K. G. and Engleman, E. G. (1987). pH-independent HIV entry into CD4-positive cells via virus envelope fusion to the plasma membrane. Cell 49, 659-668.
    • (1987) Cell , vol.49 , pp. 659-668
    • Stein, B.S.1    Gowda, S.D.2    Lifson, J.D.3    Penhallow, R.C.4    Bensch, K.G.5    Engleman, E.G.6
  • 48
    • 0026327505 scopus 로고
    • Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus
    • Tomasselli, A. G., Hui, J. O., Adams, L., Chosay, J., Lowery, D., Greenberg, B., Yem, A., Deibel, M. R., Zurcher, N. H. and Heinrikson, R. L. (1991). Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus. J. Biol. Chem. 266, 14548-14553.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14548-14553
    • Tomasselli, A.G.1    Hui, J.O.2    Adams, L.3    Chosay, J.4    Lowery, D.5    Greenberg, B.6    Yem, A.7    Deibel, M.R.8    Zurcher, N.H.9    Heinrikson, R.L.10
  • 49
    • 0028840159 scopus 로고
    • Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis
    • Vitale, M. L., Seward, E. P. and Trifaro, J. M. (1995). Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis. Neuron 14, 353-363.
    • (1995) Neuron , vol.14 , pp. 353-363
    • Vitale, M.L.1    Seward, E.P.2    Trifaro, J.M.3
  • 50
    • 0026495818 scopus 로고
    • Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein
    • Wahlberg, J. M., Bron, R., Wilschut, J. and Garoff, H. (1992). Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein. J. Virol. 66, 7309-7318.
    • (1992) J. Virol. , vol.66 , pp. 7309-7318
    • Wahlberg, J.M.1    Bron, R.2    Wilschut, J.3    Garoff, H.4
  • 51
    • 0027054277 scopus 로고
    • Identification of a sequence element in the alphavirus core protein which mediates interaction of cores with ribosomes and the disassembly of cores
    • Wengler, G., Wurkner, D. and Wengler, G. (1992). Identification of a sequence element in the alphavirus core protein which mediates interaction of cores with ribosomes and the disassembly of cores. Virology 191, 880-888.
    • (1992) Virology , vol.191 , pp. 880-888
    • Wengler, G.1    Wurkner, D.2    Wengler, G.3
  • 52
    • 0001696895 scopus 로고
    • pH-dependent fusion between the Semliki forest virus membrane and liposomes
    • White, J. and Helenius, A. (1980). pH-dependent fusion between the Semliki forest virus membrane and liposomes. Proc. Nat. Acad. Sci. USA 77, 3273-3277.
    • (1980) Proc. Nat. Acad. Sci. USA , vol.77 , pp. 3273-3277
    • White, J.1    Helenius, A.2
  • 53
    • 0019069749 scopus 로고
    • Fusion of Semliki Forest virus with the plasma membrane can be induced by low pH
    • White, J., Kartenbeck, J. and Helenius, A. (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
  • 54
    • 0020752797 scopus 로고
    • Membrane fusion proteins of enveloped viruses
    • White, J., Kielian, M. and Helenius, A. (1983). Membrane fusion proteins of enveloped viruses. Quart. Rev. Biophys. 16, 151-195.
    • (1983) Quart. Rev. Biophys. , vol.16 , pp. 151-195
    • White, J.1    Kielian, M.2    Helenius, A.3
  • 55
    • 0026492542 scopus 로고
    • Membrane fusion
    • White, J. M. (1992). Membrane fusion. Science 258, 917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.