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Volumn 6, Issue 4, 2014, Pages 1654-1671

Analysis of determinants in filovirus glycoproteins required for tetherin antagonism

Author keywords

Ebola; Glycoprotein; Lassa; Tetherin

Indexed keywords

TETHERIN PROTEIN; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN; VIRUS PROTEIN; BST2 PROTEIN, HUMAN; GLYCOPROTEIN; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; LEUKOCYTE ANTIGEN;

EID: 84898442087     PISSN: 19994915     EISSN: None     Source Type: Journal    
DOI: 10.3390/v6041654     Document Type: Article
Times cited : (23)

References (58)
  • 1
    • 84866492666 scopus 로고    scopus 로고
    • Intrinsic cellular defenses against human immunodeficiency viruses
    • Blanco-Melo, D.; Venkatesh, S.; Bieniasz, P.D. Intrinsic cellular defenses against human immunodeficiency viruses. Immunity 2012, 37, 399-411.
    • (2012) Immunity , vol.37 , pp. 399-411
    • Blanco-Melo, D.1    Venkatesh, S.2    Bieniasz, P.D.3
  • 2
    • 84870335313 scopus 로고    scopus 로고
    • The restriction factors of human immunodeficiency virus
    • Harris, R.S.; Hultquist, J.F.; Evans, D.T. The restriction factors of human immunodeficiency virus. J. Biol. Chem. 2012, 287, 40875-40883.
    • (2012) J. Biol. Chem. , vol.287 , pp. 40875-40883
    • Harris, R.S.1    Hultquist, J.F.2    Evans, D.T.3
  • 5
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • Neil, S.J.; Zang, T.; Bieniasz, P.D. Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 2008, 451, 425-430.
    • (2008) Nature , vol.451 , pp. 425-430
    • Neil, S.J.1    Zang, T.2    Bieniasz, P.D.3
  • 6
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy, A.M.; Gaddis, N.C.; Choi, J.D.; Malim, M.H. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 2002, 418, 646-650.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 7
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys
    • Stremlau, M.; Owens, C.M.; Perron, M.J.; Kiessling, M.; Autissier, P.; Sodroski, J. The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys. Nature 2004, 427, 848-853.
    • (2004) Nature , vol.427 , pp. 848-853
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3    Kiessling, M.4    Autissier, P.5    Sodroski, J.6
  • 8
    • 79955542915 scopus 로고    scopus 로고
    • A diverse range of gene products are effectors of the type I interferon antiviral response
    • Schoggins, J.W.; Wilson, S.J.; Panis, M.; Murphy, M.Y.; Jones, C.T.; Bieniasz, P.; Rice, C.M. A diverse range of gene products are effectors of the type I interferon antiviral response. Nature 2011, 472, 481-485.
    • (2011) Nature , vol.472 , pp. 481-485
    • Schoggins, J.W.1    Wilson, S.J.2    Panis, M.3    Murphy, M.Y.4    Jones, C.T.5    Bieniasz, P.6    Rice, C.M.7
  • 10
    • 84882883319 scopus 로고    scopus 로고
    • BST-2/tetherin is overexpressed in mammary gland and tumor tissues in MMTV-induced mammary cancer
    • Jones, P.H.; Mahauad-Fernandez, W.D.; Madison, M.N.; Okeoma, C.M. BST-2/tetherin is overexpressed in mammary gland and tumor tissues in MMTV-induced mammary cancer. Virology 2013, 444, 124-139.
    • (2013) Virology , vol.444 , pp. 124-139
    • Jones, P.H.1    Mahauad-Fernandez, W.D.2    Madison, M.N.3    Okeoma, C.M.4
  • 11
    • 84882373580 scopus 로고    scopus 로고
    • The antiviral activities of tetherin
    • Neil, S.J. The antiviral activities of tetherin. Curr. Top. Microbiol. Immunol. 2013, 371, 67-104.
    • (2013) Curr. Top. Microbiol. Immunol. , vol.371 , pp. 67-104
    • Neil, S.J.1
  • 12
    • 81155154291 scopus 로고    scopus 로고
    • C-terminal hydrophobic region in human bone marrow stromal cell antigen 2 (BST-2)/tetherin protein functions as second transmembrane motif
    • Andrew, A.J.; Kao, S.; Strebel, K. C-terminal hydrophobic region in human bone marrow stromal cell antigen 2 (BST-2)/tetherin protein functions as second transmembrane motif. J. Biol. Chem. 2011, 286, 39967-39981.
    • (2011) J. Biol. Chem. , vol.286 , pp. 39967-39981
    • Andrew, A.J.1    Kao, S.2    Strebel, K.3
  • 14
    • 84884795357 scopus 로고    scopus 로고
    • Mechanism of HIV-1 Virion Entrapment by Tetherin
    • Venkatesh, S.; Bieniasz, P.D. Mechanism of HIV-1 Virion Entrapment by Tetherin. PLoS Pathog. 2013, 9, e1003483.
    • (2013) PLoS Pathog. , vol.9
    • Venkatesh, S.1    Bieniasz, P.D.2
  • 15
  • 16
    • 77954055324 scopus 로고    scopus 로고
    • Antagonism of tetherin restriction of HIV-1 release by Vpu involves binding and sequestration of the restriction factor in a perinuclear compartment
    • Dube, M.; Roy, B.B.; Guiot-Guillain, P.; Binette, J.; Mercier, J.; Chiasson, A.; Cohen, E.A. Antagonism of tetherin restriction of HIV-1 release by Vpu involves binding and sequestration of the restriction factor in a perinuclear compartment. PLoS Pathog. 2010, 6, e1000856.
    • (2010) PLoS Pathog. , vol.6
    • Dube, M.1    Roy, B.B.2    Guiot-Guillain, P.3    Binette, J.4    Mercier, J.5    Chiasson, A.6    Cohen, E.A.7
  • 17
    • 71749086904 scopus 로고    scopus 로고
    • HIV-1 accessory protein Vpu internalizes cell-surface BST-2/tetherin through transmembrane interactions leading to lysosomes
    • Iwabu, Y.; Fujita, H.; Kinomoto, M.; Kaneko, K.; Ishizaka, Y.; Tanaka, Y.; Sata, T.; Tokunaga, K. HIV-1 accessory protein Vpu internalizes cell-surface BST-2/tetherin through transmembrane interactions leading to lysosomes. J. Biol. Chem. 2009, 284, 35060-35072.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35060-35072
    • Iwabu, Y.1    Fujita, H.2    Kinomoto, M.3    Kaneko, K.4    Ishizaka, Y.5    Tanaka, Y.6    Sata, T.7    Tokunaga, K.8
  • 18
    • 78649401965 scopus 로고    scopus 로고
    • Determinants of tetherin antagonism in the transmembrane domain of the human immunodeficiency virus type 1 Vpu protein
    • Vigan, R.; Neil, S.J. Determinants of tetherin antagonism in the transmembrane domain of the human immunodeficiency virus type 1 Vpu protein. J. Virol. 2010, 84, 12958-12970.
    • (2010) J. Virol. , vol.84 , pp. 12958-12970
    • Vigan, R.1    Neil, S.J.2
  • 20
    • 84855187526 scopus 로고    scopus 로고
    • HIV-1 Vpu blocks recycling and biosynthetic transport of the intrinsic immunity factor CD317/tetherin to overcome the virion release restriction
    • e00036-11
    • Schmidt, S.; Fritz, J.V.; Bitzegeio, J.; Fackler, O.T.; Keppler, O.T. HIV-1 Vpu blocks recycling and biosynthetic transport of the intrinsic immunity factor CD317/tetherin to overcome the virion release restriction. MBio 2011, 2, e00036-11.
    • (2011) MBio , vol.2
    • Schmidt, S.1    Fritz, J.V.2    Bitzegeio, J.3    Fackler, O.T.4    Keppler, O.T.5
  • 21
    • 80054000378 scopus 로고    scopus 로고
    • Role of the endocytic pathway in the counteraction of BST-2 by human lentiviral pathogens
    • Lau, D.; Kwan, W.; Guatelli, J. Role of the endocytic pathway in the counteraction of BST-2 by human lentiviral pathogens. J. Virol. 2011, 85, 9834-9846.
    • (2011) J. Virol. , vol.85 , pp. 9834-9846
    • Lau, D.1    Kwan, W.2    Guatelli, J.3
  • 22
    • 79952424915 scopus 로고    scopus 로고
    • Differential effects of human immunodeficiency virus type 1 Vpu on the stability of BST-2/tetherin
    • Andrew, A.J.; Miyagi, E.; Strebel, K. Differential effects of human immunodeficiency virus type 1 Vpu on the stability of BST-2/tetherin. J. Virol. 2011, 85, 2611-2619.
    • (2011) J. Virol. , vol.85 , pp. 2611-2619
    • Andrew, A.J.1    Miyagi, E.2    Strebel, K.3
  • 23
    • 67749095196 scopus 로고    scopus 로고
    • Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2/Tetherin via a {beta}TrCP-dependent mechanism
    • Douglas, J.L.; Viswanathan, K.; McCarroll, M.N.; Gustin, J.K.; Fruh, K.; Moses, A.V. Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2/Tetherin via a {beta}TrCP-dependent mechanism. J. Virol. 2009, 83, 7931-7947.
    • (2009) J. Virol. , vol.83 , pp. 7931-7947
    • Douglas, J.L.1    Viswanathan, K.2    McCarroll, M.N.3    Gustin, J.K.4    Fruh, K.5    Moses, A.V.6
  • 25
    • 62449106199 scopus 로고    scopus 로고
    • Tetherin-mediated restriction of filovirus budding is antagonized by the Ebola glycoprotein
    • Kaletsky, R.L.; Francica, J.R.; Agrawal-Gamse, C.; Bates, P. Tetherin-mediated restriction of filovirus budding is antagonized by the Ebola glycoprotein. Proc. Natl. Acad. Sci. USA 2009, 106, 2886-2891.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 2886-2891
    • Kaletsky, R.L.1    Francica, J.R.2    Agrawal-Gamse, C.3    Bates, P.4
  • 28
    • 77953736161 scopus 로고    scopus 로고
    • Ebola virus glycoprotein counteracts BST-2/Tetherin restriction in a sequence-independent manner that does not require tetherin surface removal
    • Lopez, L.A.; Yang, S.J.; Hauser, H.; Exline, C.M.; Haworth, K.G.; Oldenburg, J.; Cannon, P.M. Ebola virus glycoprotein counteracts BST-2/Tetherin restriction in a sequence-independent manner that does not require tetherin surface removal. J. Virol. 2010, 84, 7243-7255.
    • (2010) J. Virol. , vol.84 , pp. 7243-7255
    • Lopez, L.A.1    Yang, S.J.2    Hauser, H.3    Exline, C.M.4    Haworth, K.G.5    Oldenburg, J.6    Cannon, P.M.7
  • 29
    • 84884552344 scopus 로고    scopus 로고
    • Expression of HIV-1 Vpu Leads to Loss of the Viral Restriction Factor CD317/Tetherin from Lipid Rafts and Its Enhanced Lysosomal Degradation
    • Rollason, R.; Dunstan, K.; Billcliff, P.G.; Bishop, P.; Gleeson, P.; Wise, H.; Digard, P.; Banting, G. Expression of HIV-1 Vpu Leads to Loss of the Viral Restriction Factor CD317/Tetherin from Lipid Rafts and Its Enhanced Lysosomal Degradation. PLoS One 2013, 8, e75680.
    • (2013) PLoS One , vol.8
    • Rollason, R.1    Dunstan, K.2    Billcliff, P.G.3    Bishop, P.4    Gleeson, P.5    Wise, H.6    Digard, P.7    Banting, G.8
  • 30
    • 60049094369 scopus 로고    scopus 로고
    • Inhibition of Lassa and Marburg virus production by tetherin
    • Sakuma, T.; Noda, T.; Urata, S.; Kawaoka, Y.; Yasuda, J. Inhibition of Lassa and Marburg virus production by tetherin. J. Virol. 2009, 83, 2382-2385.
    • (2009) J. Virol. , vol.83 , pp. 2382-2385
    • Sakuma, T.1    Noda, T.2    Urata, S.3    Kawaoka, Y.4    Yasuda, J.5
  • 31
    • 34247139357 scopus 로고    scopus 로고
    • Role of the transmembrane domain of marburg virus surface protein GP in assembly of the viral envelope
    • Mittler, E.; Kolesnikova, L.; Strecker, T.; Garten, W.; Becker, S. Role of the transmembrane domain of marburg virus surface protein GP in assembly of the viral envelope. J. Virol. 2007, 81, 3942-3948.
    • (2007) J. Virol. , vol.81 , pp. 3942-3948
    • Mittler, E.1    Kolesnikova, L.2    Strecker, T.3    Garten, W.4    Becker, S.5
  • 32
    • 0028246971 scopus 로고
    • Characterization of filoviruses based on differences in structure and antigenicity of the virion glycoprotein
    • Feldmann, H.; Nichol, S.T.; Klenk, H.D.; Peters, C.J.; Sanchez, A. Characterization of filoviruses based on differences in structure and antigenicity of the virion glycoprotein. Virology 1994, 199, 469-473.
    • (1994) Virology , vol.199 , pp. 469-473
    • Feldmann, H.1    Nichol, S.T.2    Klenk, H.D.3    Peters, C.J.4    Sanchez, A.5
  • 33
    • 0035940409 scopus 로고    scopus 로고
    • The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P
    • Lenz, O.; ter, M.J.; Klenk, H.D.; Seidah, N.G.; Garten, W. The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P. Proc. Natl. Acad. Sci. USA 2001, 98, 12701-12705.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12701-12705
    • Lenz, O.1    Ter, M.J.2    Klenk, H.D.3    Seidah, N.G.4    Garten, W.5
  • 36
    • 0032949982 scopus 로고    scopus 로고
    • Endoproteolytic processing of the ebola virus envelope glycoprotein: Cleavage is not required for function
    • Wool-Lewis, R.J.; Bates, P. Endoproteolytic processing of the ebola virus envelope glycoprotein: cleavage is not required for function. J. Virol. 1999, 73, 1419-1426.
    • (1999) J. Virol. , vol.73 , pp. 1419-1426
    • Wool-Lewis, R.J.1    Bates, P.2
  • 38
    • 79961195612 scopus 로고    scopus 로고
    • The cytoplasmic domain of Marburg virus GP modulates early steps of viral infection
    • Mittler, E.; Kolesnikova, L.; Hartlieb, B.; Davey, R.; Becker, S. The cytoplasmic domain of Marburg virus GP modulates early steps of viral infection. J. Virol. 2011, 85, 8188-8196.
    • (2011) J. Virol. , vol.85 , pp. 8188-8196
    • Mittler, E.1    Kolesnikova, L.2    Hartlieb, B.3    Davey, R.4    Becker, S.5
  • 39
    • 0032849336 scopus 로고    scopus 로고
    • Mutational analysis of the putative fusion domain of Ebola virus glycoprotein
    • Ito, H.; Watanabe, S.; Sanchez, A.; Whitt, M.A.; Kawaoka, Y. Mutational analysis of the putative fusion domain of Ebola virus glycoprotein. J. Virol. 1999, 73, 8907-8912.
    • (1999) J. Virol. , vol.73 , pp. 8907-8912
    • Ito, H.1    Watanabe, S.2    Sanchez, A.3    Whitt, M.A.4    Kawaoka, Y.5
  • 41
    • 84885405310 scopus 로고    scopus 로고
    • Animal models for Ebola and Marburg virus infections
    • Nakayama, E.; Saijo, M. Animal models for Ebola and Marburg virus infections. Front. Microbiol. 2013, 4, 267.
    • (2013) Front. Microbiol. , vol.4 , pp. 267
    • Nakayama, E.1    Saijo, M.2
  • 42
    • 84871869230 scopus 로고    scopus 로고
    • Host cell factors in filovirus entry: Novel players, new insights
    • Hofmann-Winkler, H.; Kaup, F.; Pöhlmann, S. Host cell factors in filovirus entry: novel players, new insights. Viruses 2012, 4, 3336-3362.
    • (2012) Viruses , vol.4 , pp. 3336-3362
    • Hofmann-Winkler, H.1    Kaup, F.2    Pöhlmann, S.3
  • 43
    • 84859514186 scopus 로고    scopus 로고
    • Filovirus entry into cells-New insights
    • Miller, E.H.; Chandran, K. Filovirus entry into cells-New insights. Curr. Opin. Virol. 2012, 2, 206-214.
    • (2012) Curr. Opin. Virol. , vol.2 , pp. 206-214
    • Miller, E.H.1    Chandran, K.2
  • 44
    • 84860837223 scopus 로고    scopus 로고
    • Anti-tetherin activities of HIV-1 Vpu and Ebola virus glycoprotein do not involve removal of tetherin from lipid rafts
    • Lopez, L.A.; Yang, S.J.; Exline, C.M.; Rengarajan, S.; Haworth, K.G.; Cannon, P.M. Anti-tetherin activities of HIV-1 Vpu and Ebola virus glycoprotein do not involve removal of tetherin from lipid rafts. J. Virol. 2012, 86, 5467-5480.
    • (2012) J. Virol. , vol.86 , pp. 5467-5480
    • Lopez, L.A.1    Yang, S.J.2    Exline, C.M.3    Rengarajan, S.4    Haworth, K.G.5    Cannon, P.M.6
  • 46
    • 1342343136 scopus 로고    scopus 로고
    • Codon optimization of the HIV-1 vpu and vif genes stabilizes their mRNA and allows for highly efficient Rev-independent expression
    • Nguyen, K.L.; llano, M.; Akari, H.; Miyagi, E.; Poeschla, E.M.; Strebel, K.; Bour, S. Codon optimization of the HIV-1 vpu and vif genes stabilizes their mRNA and allows for highly efficient Rev-independent expression. Virology 2004, 319, 163-175.
    • (2004) Virology , vol.319 , pp. 163-175
    • Nguyen, K.L.1    Llano, M.2    Akari, H.3    Miyagi, E.4    Poeschla, E.M.5    Strebel, K.6    Bour, S.7
  • 48
    • 33745246612 scopus 로고    scopus 로고
    • The signal peptide of the ebolavirus glycoprotein influences interaction with the cellular lectins DC-SIGN and DC-SIGNR
    • Marzi, A.; Akhavan, A.; Simmons, G.; Gramberg, T.; Hofmann, H.; Bates, P.; Lingappa, V.R.; Pöhlmann, S. The signal peptide of the ebolavirus glycoprotein influences interaction with the cellular lectins DC-SIGN and DC-SIGNR. J. Virol. 2006, 80, 6305-6317.
    • (2006) J. Virol. , vol.80 , pp. 6305-6317
    • Marzi, A.1    Akhavan, A.2    Simmons, G.3    Gramberg, T.4    Hofmann, H.5    Bates, P.6    Lingappa, V.R.7    Pöhlmann, S.8
  • 50
    • 6344261967 scopus 로고    scopus 로고
    • DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of severe acute respiratory syndrome coronavirus
    • Marzi, A.; Gramberg, T.; Simmons, G.; Möller, P.; Rennekamp, A.J.; Krumbiegel, M.; Geier, M.; Eisemann, J.; Turza, N.; Saunier, B.; et al. DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of severe acute respiratory syndrome coronavirus. J. Virol. 2004, 78, 12090-12095.
    • (2004) J. Virol. , vol.78 , pp. 12090-12095
    • Marzi, A.1    Gramberg, T.2    Simmons, G.3    Möller, P.4    Rennekamp, A.J.5    Krumbiegel, M.6    Geier, M.7    Eisemann, J.8    Turza, N.9    Saunier, B.10
  • 52
    • 0028842207 scopus 로고
    • Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes
    • Connor, R.I.; Chen, B.K.; Choe, S.; Landau, N.R. Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes. Virology 1995, 206, 935-944.
    • (1995) Virology , vol.206 , pp. 935-944
    • Connor, R.I.1    Chen, B.K.2    Choe, S.3    Landau, N.R.4
  • 53
    • 0025884056 scopus 로고
    • Efficient selection for high-expression transfectants with a novel eukaryotic vector
    • Niwa, H.; Yamamura, K.; Miyazaki, J. Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 1991, 108, 193-199.
    • (1991) Gene , vol.108 , pp. 193-199
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 54
    • 11244287236 scopus 로고    scopus 로고
    • Production of monoclonal antibodies and development of an antigen capture ELISA directed against the envelope glycoprotein GP of Ebola virus
    • Lucht, A.; Grunow, R.; Otterbein, C.; Moller, P.; Feldmann, H.; Becker, S. Production of monoclonal antibodies and development of an antigen capture ELISA directed against the envelope glycoprotein GP of Ebola virus. Med. Microbiol. Immunol. 2004, 193, 181-187.
    • (2004) Med. Microbiol. Immunol. , vol.193 , pp. 181-187
    • Lucht, A.1    Grunow, R.2    Otterbein, C.3    Moller, P.4    Feldmann, H.5    Becker, S.6
  • 55
    • 78149330589 scopus 로고    scopus 로고
    • Imaging with total internal reflection fluorescence microscopy for the cell biologist
    • Mattheyses, A.L.; Simon, S.M.; Rappoport, J.Z. Imaging with total internal reflection fluorescence microscopy for the cell biologist. J. Cell Sci. 2010, 123, 3621-3628.
    • (2010) J. Cell Sci. , vol.123 , pp. 3621-3628
    • Mattheyses, A.L.1    Simon, S.M.2    Rappoport, J.Z.3
  • 56
    • 84898468478 scopus 로고    scopus 로고
    • version 6.3; Perkin Elmer: Waltham, MA, USA
    • Volocity 3D Image Analysis Software, version 6.3; Perkin Elmer: Waltham, MA, USA, 2014.
    • (2014) Volocity 3D Image Analysis Software


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