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Volumn 7, Issue 6, 2010, Pages 488-499

Entry of bunyaviruses into mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

LYSOSOME ASSOCIATED MEMBRANE PROTEIN; RAB PROTEIN; RAB7 PROTEIN;

EID: 77956536795     PISSN: 19313128     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chom.2010.05.007     Document Type: Article
Times cited : (125)

References (41)
  • 1
    • 33746885822 scopus 로고    scopus 로고
    • Wortmannin delays transfer of human rhinovirus serotype 2 to late endocytic compartments
    • Brabec, M., Blaas, D., and Fuchs, R. (2006). Wortmannin delays transfer of human rhinovirus serotype 2 to late endocytic compartments. Biochem. Biophys. Res. Commun. 348, 741-749.
    • (2006) Biochem. Biophys. Res. Commun. , vol.348 , pp. 741-749
    • Brabec, M.1    Blaas, D.2    Fuchs, R.3
  • 3
    • 67649867917 scopus 로고    scopus 로고
    • Crimean Congo hemorrhagic fever virus infects human monocyte-derived dendritic cells
    • Connolly-Andersen, A. M., Douagi, I., Kraus, A. A., and Mirazimi, A. (2009). Crimean Congo hemorrhagic fever virus infects human monocyte-derived dendritic cells. Virology 390, 157-162.
    • (2009) Virology , vol.390 , pp. 157-162
    • Connolly-Andersen, A.M.1    Douagi, I.2    Kraus, A.A.3    Mirazimi, A.4
  • 4
    • 0023669065 scopus 로고
    • Inhibition of endocytosis by anti-clathrin antibodies
    • Doxsey, S. J., Brodsky, F. M., Blank, G. S., and Helenius, A. (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
  • 5
    • 0018952919 scopus 로고
    • Low temperature selectively inhibits fusion between pinocytic vesicles and lysosomes during heterophagy of 125I-asialofetuin by the perfused rat liver
    • Dunn, W. A., Hubbard, A. L., and Aronson, N. N., Jr. (1980). Low temperature selectively inhibits fusion between pinocytic vesicles and lysosomes during heterophagy of 125I-asialofetuin by the perfused rat liver. J. Biol. Chem. 255, 5971-5978.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5971-5978
    • Dunn, W.A.1    Hubbard, A.L.2    Aronson Jr., N.N.3
  • 6
    • 33751059710 scopus 로고    scopus 로고
    • Development and characterization of a Rift Valley fever virus cell-cell fusion assay using alphavirus replicon vectors
    • Filone, C. M., Heise, M., Doms, R. W., and Bertolotti-Ciarlet, A. (2006). Development and characterization of a Rift Valley fever virus cell-cell fusion assay using alphavirus replicon vectors. Virology 356, 155-164.
    • (2006) Virology , vol.356 , pp. 155-164
    • Filone, C.M.1    Heise, M.2    Doms, R.W.3    Bertolotti-Ciarlet, A.4
  • 7
    • 15444371889 scopus 로고    scopus 로고
    • Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein (beta-penetrenes)
    • Garry, C. E., and Garry, R. F. (2004). Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein (beta-penetrenes). Theor. Biol. Med. Model. 1, 10.
    • (2004) Theor. Biol. Med. Model , vol.1 , pp. 10
    • Garry, C.E.1    Garry, R.F.2
  • 8
    • 70349739362 scopus 로고    scopus 로고
    • Early steps in cell infection by parvoviruses: Host-specific differences in cell receptor binding but similar endosomal trafficking
    • Harbison, C. E., Lyi, S. M., Weichert, W. S., and Parrish, C. R. (2009). Early steps in cell infection by parvoviruses: host-specific differences in cell receptor binding but similar endosomal trafficking. J. Virol. 83, 10504-10514.
    • (2009) J. Virol. , vol.83 , pp. 10504-10514
    • Harbison, C.E.1    Lyi, S.M.2    Weichert, W.S.3    Parrish, C.R.4
  • 9
    • 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. (Pubitemid 10147875)
    • (1980) Journal of Cell Biology , vol.84 , Issue.2 , pp. 404-420
    • Helenius, A.1    Kartenbeck, J.2    Simons, K.3    Fries, E.4
  • 10
    • 35348936658 scopus 로고    scopus 로고
    • A role for Rab5 activity in the biogenesis of endosomal and lysosomal compartments
    • Hirota, Y., Kuronita, T., Fujita, H., and Tanaka, Y. (2007). A role for Rab5 activity in the biogenesis of endosomal and lysosomal compartments. Biochem. Biophys. Res. Commun. 364, 40-47.
    • (2007) Biochem. Biophys. Res. Commun. , vol.364 , pp. 40-47
    • Hirota, Y.1    Kuronita, T.2    Fujita, H.3    Tanaka, Y.4
  • 11
    • 0141988384 scopus 로고    scopus 로고
    • Wortmannin alters the intracellular trafficking of the bradykinin B2 receptor: Role of phosphoinositide 3-kinase and Rab5
    • Houle, S., and Marceau, F. (2003). Wortmannin alters the intracellular trafficking of the bradykinin B2 receptor: role of phosphoinositide 3-kinase and Rab5. Biochem. J. 375, 151-158.
    • (2003) Biochem. J. , vol.375 , pp. 151-158
    • Houle, S.1    Marceau, F.2
  • 13
    • 58149390171 scopus 로고    scopus 로고
    • Host cell factors and functions involved in vesicular stomatitis virus entry
    • Johannsdottir, H. K., Mancini, R., Kartenbeck, J., Amato, L., and Helenius, A. (2009). Host cell factors and functions involved in vesicular stomatitis virus entry. J. Virol. 83, 440-453.
    • (2009) J. Virol. , vol.83 , pp. 440-453
    • Johannsdottir, H.K.1    Mancini, R.2    Kartenbeck, J.3    Amato, L.4    Helenius, A.5
  • 14
    • 37049006295 scopus 로고    scopus 로고
    • Proteolysis of the Ebola virus glycoproteins enhances virus binding and infectivity
    • Kaletsky, R. L., Simmons, G., and Bates, P. (2007). Proteolysis of the Ebola virus glycoproteins enhances virus binding and infectivity. J. Virol. 81, 13378-13384.
    • (2007) J. Virol. , vol.81 , pp. 13378-13384
    • Kaletsky, R.L.1    Simmons, G.2    Bates, P.3
  • 15
    • 0347380840 scopus 로고    scopus 로고
    • The ubiquitin-vacuolar protein sorting system is selectively required during entry of influenza virus into host cells
    • Khor, R., McElroy, L. J., and Whittaker, G. R. (2003). The ubiquitin-vacuolar protein sorting system is selectively required during entry of influenza virus into host cells. Traffic 4, 857-868.
    • (2003) Traffic , vol.4 , pp. 857-868
    • Khor, R.1    McElroy, L.J.2    Whittaker, G.R.3
  • 16
    • 0019256559 scopus 로고
    • Adsorptive endocytosis of Semliki Forest virus
    • DOI 10.1016/0022-2836(80)90281-8
    • Marsh, M., and Helenius, A. (1980). Adsorptive endocytosis of Semliki Forest virus. J. Mol. Biol. 142, 439-454. (Pubitemid 11165623)
    • (1980) Journal of Molecular Biology , vol.142 , Issue.3 , pp. 439-454
    • Marsh, M.1    Helenius, A.2
  • 17
    • 0026070664 scopus 로고
    • Transport of incoming influenza virus nucleocapsids into the nucleus
    • Martin, K., and Helenius, A. (1991). Transport of incoming influenza virus nucleocapsids into the nucleus. J. Virol. 65, 232-244.
    • (1991) J. Virol. , vol.65 , pp. 232-244
    • Martin, K.1    Helenius, A.2
  • 19
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma, S., and Poole, B. (1978). Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc. Natl. Acad. Sci. USA 75, 3327-3331.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 20
    • 40649115227 scopus 로고    scopus 로고
    • Insights into bunyavirus architecture from electron cryotomography of Uukuniemi virus
    • Overby, A. K., Pettersson, R. F., Grunewald, K., and Huiskonen, J. T. (2008). Insights into bunyavirus architecture from electron cryotomography of Uukuniemi virus. Proc. Natl. Acad. Sci. USA 105, 2375-2379.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 2375-2379
    • Overby, A.K.1    Pettersson, R.F.2    Grunewald, K.3    Huiskonen, J.T.4
  • 21
    • 0015751136 scopus 로고
    • The ribonucleic acids of Uukuniemi virus, a noncubical tick-borne arbovirus
    • Pettersson, R., and Kaariainen, L. (1973). The ribonucleic acids of Uukuniemi virus, a noncubical tick-borne arbovirus. Virology 56, 608-619.
    • (1973) Virology , vol.56 , pp. 608-619
    • Pettersson, R.1    Kaariainen, L.2
  • 22
    • 33846526211 scopus 로고    scopus 로고
    • Mutagenesis of the La Crosse Virus glycoprotein supports a role for Gc (1066-1087) as the fusion peptide
    • Plassmeyer, M. L., Soldan, S. S., Stachelek, K. M., Roth, S. M., Martin-Garcia, J., and Gonzalez-Scarano, F. (2007). Mutagenesis of the La Crosse Virus glycoprotein supports a role for Gc (1066-1087) as the fusion peptide. Virology 358, 273-282.
    • (2007) Virology , vol.358 , pp. 273-282
    • Plassmeyer, M.L.1    Soldan, S.S.2    Stachelek, K.M.3    Roth, S.M.4    Martin-Garcia, J.5    Gonzalez-Scarano, F.6
  • 23
    • 0028229815 scopus 로고
    • Uncoating of human rhinovirus serotype 2 from late endosomes
    • Prchla, E., Kuechler, E., Blaas, D., and Fuchs, R. (1994). Uncoating of human rhinovirus serotype 2 from late endosomes. J. Virol. 68, 3713-3723.
    • (1994) J. Virol. , vol.68 , pp. 3713-3723
    • Prchla, E.1    Kuechler, E.2    Blaas, D.3    Fuchs, R.4
  • 24
    • 67650912077 scopus 로고    scopus 로고
    • A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection
    • 10.1371/journal.ppat.1000465
    • Qian, M., Cai, D., Verhey, K. J., and Tsai, B. (2009). A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection. PLoS Pathog. 5, e1000465. 10.1371/journal.ppat.1000465.
    • (2009) PLoS Pathog. , vol.5
    • Qian, M.1    Cai, D.2    Verhey, K.J.3    Tsai, B.4
  • 25
    • 47749126117 scopus 로고    scopus 로고
    • Lymphocytic choriomeningitis virus uses a novel endocytic pathway for infectious entry via late endosomes
    • Quirin, K., Eschli, B., Scheu, I., Poort, L., Kartenbeck, J., and Helenius, A. (2008). Lymphocytic choriomeningitis virus uses a novel endocytic pathway for infectious entry via late endosomes. Virology 378, 21-33.
    • (2008) Virology , vol.378 , pp. 21-33
    • Quirin, K.1    Eschli, B.2    Scheu, I.3    Poort, L.4    Kartenbeck, J.5    Helenius, A.6
  • 26
    • 0029163526 scopus 로고
    • Homodimeric association of the spike glycoproteins G1 and G2 of Uukuniemi virus
    • Ronka, H., Hilden, P., Von Bonsdorff, C. H., and Kuismanen, E. (1995). Homodimeric association of the spike glycoproteins G1 and G2 of Uukuniemi virus. Virology 211, 241-250.
    • (1995) Virology , vol.211 , pp. 241-250
    • Ronka, H.1    Hilden, P.2    Von Bonsdorff, C.H.3    Kuismanen, E.4
  • 28
    • 0036231098 scopus 로고    scopus 로고
    • Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes
    • Sachse, M., Urbe, S., Oorschot, V., Strous, G. J., and Klumperman, J. (2002). Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes. Mol. Biol. Cell 13, 1313-1328.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 1313-1328
    • Sachse, M.1    Urbe, S.2    Oorschot, V.3    Strous, G.J.4    Klumperman, J.5
  • 30
    • 34948862521 scopus 로고    scopus 로고
    • Bunyaviridae
    • K. D. Fields, ed. Philadelphia: Lippincott Williams & Wilkins
    • Schmaljohn, C., and Nichol, S. (2007). Bunyaviridae. In Virology, K. D. Fields, ed. (Philadelphia: Lippincott Williams & Wilkins), pp. 1741-1788.
    • (2007) Virology , pp. 1741-1788
    • Schmaljohn, C.1    Nichol, S.2
  • 31
    • 0037690744 scopus 로고    scopus 로고
    • Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses
    • Sieczkarski, S. B., and Whittaker, G. R. (2003). Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses. Traffic 4, 333-343.
    • (2003) Traffic , vol.4 , pp. 333-343
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 32
    • 60649099762 scopus 로고    scopus 로고
    • Microtubuledependent and microtubule-independent steps in Crimean-Congo hemorrhagic fever virus replication cycle
    • Simon, M., Johansson, C., Lundkvist, A., and Mirazimi, A. (2009a). Microtubuledependent and microtubule-independent steps in Crimean-Congo hemorrhagic fever virus replication cycle. Virology 385, 313-332.
    • (2009) Virology , vol.385 , pp. 313-332
    • Simon, M.1    Johansson, C.2    Lundkvist, A.3    Mirazimi, A.4
  • 33
    • 59849116492 scopus 로고    scopus 로고
    • Crimean-Congo hemorrhagic fever virus entry and replication is clathrin-, pH-and cholesterol-dependent
    • Simon, M., Johansson, C., and Mirazimi, A. (2009b). Crimean-Congo hemorrhagic fever virus entry and replication is clathrin-, pH-and cholesterol-dependent. J. Gen. Virol. 90, 210-215.
    • (2009) J. Gen. Virol. , vol.90 , pp. 210-215
    • Simon, M.1    Johansson, C.2    Mirazimi, A.3
  • 36
    • 0016839826 scopus 로고
    • Surface structure of Uukuniemi virus
    • von Bonsdorff, C. H., and Pettersson, R. (1975). Surface structure of Uukuniemi virus. J. Virol. 16, 1296-1307.
    • (1975) J. Virol. , vol.16 , pp. 1296-1307
    • Von Bonsdorff, C.H.1    Pettersson, R.2
  • 37
    • 58149265437 scopus 로고    scopus 로고
    • Dissecting the cell entry pathway of dengue virus by single-particle tracking in living cells
    • 10.1371/journal.ppat.1000244
    • van der Schaar, H. M., Rust, M. J., Chen, C., van der Ende-Metselaar, H., Wilschut, J., Zhuang, X., and Smit, J. M. (2008). Dissecting the cell entry pathway of dengue virus by single-particle tracking in living cells. PLoS Pathog. 4, e1000244. 10.1371/journal.ppat.1000244.
    • (2008) PLoS Pathog. , vol.4
    • Van Der Schaar, H.M.1    Rust, M.J.2    Chen, C.3    Van Der Ende-Metselaar, H.4    Wilschut, J.5    Zhuang, X.6    Smit, J.M.7
  • 38
    • 34447311691 scopus 로고    scopus 로고
    • Rapid membrane fusion of individual virus particles with supported lipid bilayers
    • Wessels, L., Elting, M. W., Scimeca, D., and Weninger, K. (2007). Rapid membrane fusion of individual virus particles with supported lipid bilayers. Biophys. J. 93, 526-538.
    • (2007) Biophys. J. , vol.93 , pp. 526-538
    • Wessels, L.1    Elting, M.W.2    Scimeca, D.3    Weninger, K.4
  • 39
    • 0019870337 scopus 로고
    • Cell fusion by Semliki Forest, influenza, and vesicular stomatitis viruses
    • White, J., Matlin, K., and Helenius, A. (1981). Cell fusion by Semliki Forest, influenza, and vesicular stomatitis viruses. J. Cell Biol. 89, 674-679.
    • (1981) J. Cell. Biol. , vol.89 , pp. 674-679
    • White, J.1    Matlin, K.2    Helenius, A.3
  • 40
    • 10644245814 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system facilitates the transfer of murine coronavirus from endosome to cytoplasm during virus entry
    • Yu, G. Y., and Lai, M. M. (2005). The ubiquitin-proteasome system facilitates the transfer of murine coronavirus from endosome to cytoplasm during virus entry. J. Virol. 79, 644-648.
    • (2005) J. Virol. , vol.79 , pp. 644-648
    • Yu, G.Y.1    Lai, M.M.2
  • 41
    • 67249150119 scopus 로고    scopus 로고
    • Rab7: Roles in membrane trafficking and disease
    • Zhang, M., Chen, L., Wang, S., and Wang, T. (2009). Rab7: roles in membrane trafficking and disease. Biosci. Rep. 29, 193-209.
    • (2009) Biosci. Rep. , vol.29 , pp. 193-209
    • Zhang, M.1    Chen, L.2    Wang, S.3    Wang, T.4


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