메뉴 건너뛰기




Volumn 76, Issue 20, 2002, Pages 10455-10464

Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis

Author keywords

[No Author keywords available]

Indexed keywords

CHLORPROMAZINE; CLATHRIN; GENISTEIN; LIGAND; METHYL BETA CYCLODEXTRIN; NYSTATIN; POTASSIUM; PROTEIN; TRANSFERRIN;

EID: 0036784565     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.76.20.10455-10464.2002     Document Type: Article
Times cited : (272)

References (59)
  • 1
    • 0036118329 scopus 로고    scopus 로고
    • The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains
    • Ahn, A., D. L. Gibbons, and M. Kielian. 2002. The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains. J. Virol. 76: 3267-3275.
    • (2002) J. Virol. , vol.76 , pp. 3267-3275
    • Ahn, A.1    Gibbons, D.L.2    Kielian, M.3
  • 2
    • 0035830901 scopus 로고    scopus 로고
    • Inhibition of clathrin-dependent endocytosis has multiple effects on human rhinovirus serotype 2 cell entry
    • Bayer, N., D. Schober, M. Huttinger, D. Blaas, and R. Fuchs. 2001. Inhibition of clathrin-dependent endocytosis has multiple effects on human rhinovirus serotype 2 cell entry. J. Biol. Chem. 276:3952-3962.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3952-3962
    • Bayer, N.1    Schober, D.2    Huttinger, M.3    Blaas, D.4    Fuchs, R.5
  • 4
    • 15844361829 scopus 로고    scopus 로고
    • The ear of alpha-adaptin interacts with the COOH-terminal domain of the Eps 15 protein
    • Benmerah, A., B. Begue, A. Dautry-Varsat, and N. Cerf-Bensussan. 1996. The ear of alpha-adaptin interacts with the COOH-terminal domain of the Eps 15 protein. J. Biol. Chem. 271:12111-12116.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12111-12116
    • Benmerah, A.1    Begue, B.2    Dautry-Varsat, A.3    Cerf-Bensussan, N.4
  • 5
    • 0029615380 scopus 로고
    • The tyrosine kinase substrate eps15 is constitutively associated with the plasma membrane adaptor AP-2
    • Benmerah, A., J. Gagnon, B. Begue, B. Megarbane, A. Dautry-Varsat, and N. Cerf-Bensussan. 1995. The tyrosine kinase substrate eps15 is constitutively associated with the plasma membrane adaptor AP-2. J. Cell Biol. 131:1831-1838.
    • (1995) J. Cell Biol. , vol.131 , pp. 1831-1838
    • Benmerah, A.1    Gagnon, J.2    Begue, B.3    Megarbane, B.4    Dautry-Varsat, A.5    Cerf-Bensussan, N.6
  • 7
    • 0034602956 scopus 로고    scopus 로고
    • Mapping of Eps15 domains involved in its targeting to clathrin-coated pits
    • Benmerah, A., V. Poupon, N. Cerf-Bensussan, and A. Dautry-Varsat. 2000. Mapping of Eps15 domains involved in its targeting to clathrin-coated pits. J. Biol. Chem. 275:3288-3295.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3288-3295
    • Benmerah, A.1    Poupon, V.2    Cerf-Bensussan, N.3    Dautry-Varsat, A.4
  • 8
    • 0031464218 scopus 로고    scopus 로고
    • An update on non-clathrin coated endocytosis
    • Bishop, N. E. 1997. An update on non-clathrin coated endocytosis. Rev. Med. Virol. 7:199-207.
    • (1997) Rev. Med. Virol. , vol.7 , pp. 199-207
    • Bishop, N.E.1
  • 9
    • 0011913143 scopus 로고
    • Bafilomycins: A class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman, E. J., A. Siebers, and K. Altendorf. 1988. Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc. Natl. Acad. Sci. USA 85:7972-7976.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 11
    • 0029861558 scopus 로고    scopus 로고
    • Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins
    • Bui, M., G. Whittaker, and A. Helenius. 1996. Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins. J. Virol. 70:8391-8401.
    • (1996) J. Virol. , vol.70 , pp. 8391-8401
    • Bui, M.1    Whittaker, G.2    Helenius, A.3
  • 13
    • 0023669065 scopus 로고
    • Inhibition of endocytosis by anti-clathrin antibodies
    • Doxsey, S. J., F. M. Brodsky, G. S. Blank, and A. Helenius. 1987. Inhibition of endocytosis by anti-clathrin antibodies. Cell 50:453-463.
    • (1987) Cell , vol.50 , pp. 453-463
    • Doxsey, S.J.1    Brodsky, F.M.2    Blank, G.S.3    Helenius, A.4
  • 16
    • 0028930293 scopus 로고
    • Requirement for vacuolar proton-ATPase activity during entry of influenza virus into cells
    • Guinea, R., and L. Carrasco. 1995. Requirement for vacuolar proton-ATPase activity during entry of influenza virus into cells. J. Virol. 69:2306-2312.
    • (1995) J. Virol. , vol.69 , pp. 2306-2312
    • Guinea, R.1    Carrasco, L.2
  • 20
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw, J. E. 2000. Dynamin and its role in membrane fission. Annu. Rev. Cell Dev. Biol. 16:483-519.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 483-519
    • Hinshaw, J.E.1
  • 22
    • 0036017680 scopus 로고    scopus 로고
    • Clathrin-dependent or not: Is it still the question?
    • Johannes, L., and C. Lamaze. 2002. Clathrin-dependent or not: is it still the question? Traffic 3:443-451.
    • (2002) Traffic , vol.3 , pp. 443-451
    • Johannes, L.1    Lamaze, C.2
  • 24
    • 0032559342 scopus 로고    scopus 로고
    • Role of dynamin in the formation of transport vesicles from the trans-Golgi network
    • Jones, S. M., K. E. Howell, J. R. Henley, H. Cao, and M. A. McNiven. 1998. Role of dynamin in the formation of transport vesicles from the trans-Golgi network. Science 279:573-577.
    • (1998) Science , vol.279 , pp. 573-577
    • Jones, S.M.1    Howell, K.E.2    Henley, J.R.3    Cao, H.4    McNiven, M.A.5
  • 25
    • 0020316487 scopus 로고
    • Influence of chlorpromazine on the replication of influenza virus in chick embryo fibroblasts
    • Krizanová, O., F. Ciampor, and P. Verber. 1982. Influence of chlorpromazine on the replication of influenza virus in chick embryo fibroblasts. Acta Virol. 26:209-216.
    • (1982) Acta Virol. , vol.26 , pp. 209-216
    • Krizanová, O.1    Ciampor, F.2    Verber, P.3
  • 26
    • 0035265834 scopus 로고    scopus 로고
    • Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway
    • Lamaze, C., A. Dujeancourt, T. Baba, C. G. Lo, A. Benmerah, and A. Dautry-Varsat. 2001. Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway. Mol. Cell 7:661-671.
    • (2001) Mol. Cell , vol.7 , pp. 661-671
    • Lamaze, C.1    Dujeancourt, A.2    Baba, T.3    Lo, C.G.4    Benmerah, A.5    Dautry-Varsat, A.6
  • 27
    • 0020626609 scopus 로고
    • Depletion of intracellular potassium arrests coated pit formation and receptor-mediated endocytosis in fibroblasts
    • Larkin, J. M., M. S. Brown, J. L. Goldstein, and R. G. Anderson. 1983. Depletion of intracellular potassium arrests coated pit formation and receptor-mediated endocytosis in fibroblasts. Cell 33:273-285.
    • (1983) Cell , vol.33 , pp. 273-285
    • Larkin, J.M.1    Brown, M.S.2    Goldstein, J.L.3    Anderson, R.G.4
  • 28
    • 0023256911 scopus 로고
    • Effect of reduced endocytosis induced by hypotonic shock and potassium depletion on the infection of Hep 2 cells by picornaviruses
    • Madshus, I. H., K. Sandvig, S. Olsnes, and B. van Deurs. 1987. Effect of reduced endocytosis induced by hypotonic shock and potassium depletion on the infection of Hep 2 cells by picornaviruses. J. Cell. Physiol. 131:14-22.
    • (1987) J. Cell. Physiol. , vol.131 , pp. 14-22
    • Madshus, I.H.1    Sandvig, K.2    Olsnes, S.3    Van Deurs, B.4
  • 29
    • 0002186460 scopus 로고    scopus 로고
    • Macropinocytosis
    • M. Marsh (ed.). Oxford University Press, Oxford, United Kingdom
    • Maniak, M. 2001. Macropinocytosis, p. 78-93. In M. Marsh (ed.), Endocytosis. Oxford University Press, Oxford, United Kingdom.
    • (2001) Endocytosis , pp. 78-93
    • Maniak, M.1
  • 30
    • 0019256559 scopus 로고
    • Adsorptive endocytosis of Semliki Forest virus
    • Marsh, M., and A. Helenius. 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
  • 31
    • 0024534779 scopus 로고
    • Virus entry into animal cells
    • Marsh, M., and A. Helenius. 1989. Virus entry into animal cells. Adv. Virus Res. 36:107-151.
    • (1989) Adv. Virus Res. , vol.36 , pp. 107-151
    • Marsh, M.1    Helenius, A.2
  • 32
    • 0033538576 scopus 로고    scopus 로고
    • The structural era of endocytosis
    • Marsh, M., and H. T. McMahon. 1999. The structural era of endocytosis. Science 285:215-220.
    • (1999) Science , vol.285 , pp. 215-220
    • Marsh, M.1    McMahon, H.T.2
  • 33
    • 0019814443 scopus 로고
    • Infectious entry pathway of influenza virus in a canine kidney cell line
    • Matlin, K. S., H. Reggio, A. Helenius, and K. Simons. 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
  • 34
    • 0019976569 scopus 로고
    • Pathway of vesicular stomatitis virus leading to infection
    • Matlin, K. S., H. Reggio, A. Helenius, and K. Simons. 1982. Pathway of vesicular stomatitis virus 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
  • 35
    • 0026696312 scopus 로고
    • Epstein-Barr virus enters B cells and epithelial cells by different routes
    • Miller, N., and L. M. Hutt-Fletcher. 1992. Epstein-Barr virus enters B cells and epithelial cells by different routes. J. Virol. 66:3409-3414.
    • (1992) J. Virol. , vol.66 , pp. 3409-3414
    • Miller, N.1    Hutt-Fletcher, L.M.2
  • 39
    • 0033995518 scopus 로고    scopus 로고
    • Role for dynamin in late endosome dynamics and trafficking of the cation-independent mannose 6-phosphate receptor
    • Nicoziani, P., F. Vilhardt, A. Llorente, L. Hilout, P. J. Courtoy, K. Sandvig, and B. van Deurs. 2000. Role for dynamin in late endosome dynamics and trafficking of the cation-independent mannose 6-phosphate receptor. Mol. Biol. Cell 11:481-495.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 481-495
    • Nicoziani, P.1    Vilhardt, F.2    Llorente, A.3    Hilout, L.4    Courtoy, P.J.5    Sandvig, K.6    Van Deurs, B.7
  • 40
    • 0028138521 scopus 로고
    • Regulated internalization of caveolae
    • Parton, R. G., B. Joggerst, and K. Simons. 1994. Regulated internalization of caveolae. J. Cell Biol. 127:1199-1215.
    • (1994) J. Cell Biol. , vol.127 , pp. 1199-1215
    • Parton, R.G.1    Joggerst, B.2    Simons, K.3
  • 41
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular transport pathway to the ER
    • Pelkmans, L., K. J., and A. Helenius. 2001. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular transport pathway to the ER. Nat. Cell Biol. 3:473-483.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 473-483
    • Pelkmans, L.1    Helenius, A.2
  • 42
    • 0033968050 scopus 로고    scopus 로고
    • JC virus enters human glial cells by clathrin-dependent receptor-mediated endocytosis
    • Pho, M. T., A. Ashok, and W. J. Atwood. 2000. JC virus enters human glial cells by clathrin-dependent receptor-mediated endocytosis. J. Virol. 74:2288-2292.
    • (2000) J. Virol. , vol.74 , pp. 2288-2292
    • Pho, M.T.1    Ashok, A.2    Atwood, W.J.3
  • 43
    • 0033767394 scopus 로고    scopus 로고
    • Entry of influenza viruses into cells is inhibited by a highly specific protein kinase C inhibitor
    • Root, C. R., E. G. Wills, L. L. McNair, and G. R. Whittaker. 2000. Entry of influenza viruses into cells is inhibited by a highly specific protein kinase C inhibitor. J. Gen. Virol. 81:2697-2705.
    • (2000) J. Gen. Virol. , vol.81 , pp. 2697-2705
    • Root, C.R.1    Wills, E.G.2    McNair, L.L.3    Whittaker, G.R.4
  • 45
    • 0034142287 scopus 로고    scopus 로고
    • Early stages of influenza virus entry into Mv-1 lung cells: Involvement of dynamin
    • Roy, A.-M. M., J. S. Parker, C. R. Parrish, and G. R. Whittaker. 2000. Early stages of influenza virus entry into Mv-1 lung cells: involvement of dynamin. Virology 267:17-28.
    • (2000) Virology , vol.267 , pp. 17-28
    • Roy, A.-M.M.1    Parker, J.S.2    Parrish, C.R.3    Whittaker, G.R.4
  • 46
    • 0003074218 scopus 로고    scopus 로고
    • Endocytosis in pathogen entry and replication
    • M. Marsh (ed.). Oxford University Press, Oxford, United Kingdom
    • Russell, D. G., and M. Marsh. 2001. Endocytosis in pathogen entry and replication, p. 247-280. In M. Marsh (ed.), Endocytosis. Oxford University Press, Oxford, United Kingdom.
    • (2001) Endocytosis , pp. 247-280
    • Russell, D.G.1    Marsh, M.2
  • 48
    • 0033593321 scopus 로고    scopus 로고
    • Influenza viruses select ordered lipid domains during budding from the plasma membrane
    • Scheiffele, P., A. Rietveld, T. Wilk, and K. Simons. 1999. Influenza viruses select ordered lipid domains during budding from the plasma membrane. J. Biol. Chem. 274:2038-2044.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2038-2044
    • Scheiffele, P.1    Rietveld, A.2    Wilk, T.3    Simons, K.4
  • 49
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele, P., M. G. Roth, and K. Simons. 1997. Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO J. 16:5501-5508.
    • (1997) EMBO J. , vol.16 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 51
    • 0034898592 scopus 로고    scopus 로고
    • Caveolae as portals of entry for microbes
    • Shin, J. S., and S. N. Abraham. 2001. Caveolae as portals of entry for microbes. Microbes Infect. 3:755-761.
    • (2001) Microbes Infect. , vol.3 , pp. 755-761
    • Shin, J.S.1    Abraham, S.N.2
  • 52
    • 0036298810 scopus 로고    scopus 로고
    • Dissecting virus entry via endocytosis
    • First published 28 March 2002; 10.1099/vir.0.18346-0
    • Sieczkarski, S. B., and G. R. Whittaker, 2002. Dissecting virus entry via endocytosis. J. Gen. Virol. 83:1535-1545. (First published 28 March 2002; 10.1099/vir.0.18346-0.)
    • (2002) J. Gen. Virol. , vol.83 , pp. 1535-1545
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 54
    • 0033492265 scopus 로고    scopus 로고
    • Endocytic mechanisms responsible for uptake of GPI-linked diphtheria toxin receptor
    • Skretting, G., M. L. Torgersen, B. van Deurs, and K. Sandvig. 1999. Endocytic mechanisms responsible for uptake of GPI-linked diphtheria toxin receptor. J. Cell Sci. 112:3899-3909.
    • (1999) J. Cell Sci. , vol.112 , pp. 3899-3909
    • Skretting, G.1    Torgersen, M.L.2    Van Deurs, B.3    Sandvig, K.4
  • 55
    • 0029826531 scopus 로고    scopus 로고
    • Eps15 is a component of clathrin-coated pits and vesicles and is located at the rim of coated pits
    • Tebar, F., T. Sorkina, A. Sorkin, M. Ericsson, and T. Kirchhausen. 1996. Eps15 is a component of clathrin-coated pits and vesicles and is located at the rim of coated pits. J. Biol. Chem. 271:28727-28730.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28727-28730
    • Tebar, F.1    Sorkina, T.2    Sorkin, A.3    Ericsson, M.4    Kirchhausen, T.5
  • 56
    • 0026628752 scopus 로고
    • High-affinity laminin receptor is a receptor for Sindbis virus in mammalian cells
    • Wang, K. S., R. J. Kuhn, E. G. Strauss, S. Ou, and J. H. Strauss. 1992. High-affinity laminin receptor is a receptor for Sindbis virus in mammalian cells. J. Virol. 66:4992-5001.
    • (1992) J. Virol. , vol.66 , pp. 4992-5001
    • Wang, K.S.1    Kuhn, R.J.2    Strauss, E.G.3    Ou, S.4    Strauss, J.H.5
  • 57
    • 0027520440 scopus 로고
    • Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation
    • Wang, L. H., K. G. Rothberg, and R. G. Anderson. 1993. Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation. J. Cell Biol. 123:1107-1117.
    • (1993) J. Cell Biol. , vol.123 , pp. 1107-1117
    • Wang, L.H.1    Rothberg, K.G.2    Anderson, R.G.3
  • 58
    • 0020338520 scopus 로고
    • Membrane fusion activity of influenza virus
    • White, J., J. Kartenbeck, and A. Helenius. 1982. Membrane fusion activity of influenza virus. EMBO J. 1:217-222.
    • (1982) EMBO J. , vol.1 , pp. 217-222
    • White, J.1    Kartenbeck, J.2    Helenius, A.3
  • 59
    • 0028961386 scopus 로고
    • Hyperphosphorylation of mutant influenza virus matrix (MI) protein causes its retention in the nucleus
    • Whittaker, G., I. Kemler, and A. Helenius. 1995. Hyperphosphorylation of mutant influenza virus matrix (MI) protein causes its retention in the nucleus. J. Virol. 69:439-445.
    • (1995) J. Virol. , vol.69 , pp. 439-445
    • Whittaker, G.1    Kemler, I.2    Helenius, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.