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Volumn 102, Issue 11, 2012, Pages 2517-2525

Investigation of Ebola VP40 assembly and oligomerization in live cells using number and brightness analysis

Author keywords

[No Author keywords available]

Indexed keywords

CORE PROTEIN; ENHANCED GREEN FLUORESCENT PROTEIN; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; NUCLEOPROTEIN; NUCLEOPROTEIN VP40, EBOLA VIRUS;

EID: 84861883930     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.04.022     Document Type: Article
Times cited : (63)

References (45)
  • 1
    • 0017581604 scopus 로고
    • Viral haemorrhagic fever in southern Sudan and northern Zaire. Preliminary studies on the aetiological agent
    • E.T. Bowen, and G. Lloyd E.E. Vella Viral haemorrhagic fever in southern Sudan and northern Zaire. Preliminary studies on the aetiological agent Lancet 1 1977 571 573
    • (1977) Lancet , vol.1 , pp. 571-573
    • Bowen, E.T.1    Lloyd, G.2    Vella, E.E.3
  • 2
    • 0022375091 scopus 로고
    • Descriptive analysis of Ebola virus proteins
    • L.H. Elliott, M.P. Kiley, and J.B. McCormick Descriptive analysis of Ebola virus proteins Virology 147 1985 169 176
    • (1985) Virology , vol.147 , pp. 169-176
    • Elliott, L.H.1    Kiley, M.P.2    McCormick, J.B.3
  • 3
    • 0017772897 scopus 로고
    • Isolation and partial characterisation of a new virus causing acute haemorrhagic fever in Zaire
    • K.M. Johnson, and J.V. Lange F.A. Murphy Isolation and partial characterisation of a new virus causing acute haemorrhagic fever in Zaire Lancet 1 1977 569 571
    • (1977) Lancet , vol.1 , pp. 569-571
    • Johnson, K.M.1    Lange, J.V.2    Murphy, F.A.3
  • 4
    • 0032999978 scopus 로고    scopus 로고
    • Clinical virology of Ebola hemorrhagic fever (EHF): Virus, virus antigen, and IgG and IgM antibody findings among EHF patients in Kikwit, Democratic Republic of the Congo, 1995
    • T.G. Ksiazek, and P.E. Rollin C.J. Peters Clinical virology of Ebola hemorrhagic fever (EHF): virus, virus antigen, and IgG and IgM antibody findings among EHF patients in Kikwit, Democratic Republic of the Congo, 1995 J. Infect. Dis. 179 Suppl 1 1999 S177 S187
    • (1999) J. Infect. Dis. , vol.179 , Issue.SUPPL. 1
    • Ksiazek, T.G.1    Rollin, P.E.2    Peters, C.J.3
  • 5
    • 64749097604 scopus 로고    scopus 로고
    • Correlates of protective immunity for Ebola vaccines: Implications for regulatory approval by the animal rule
    • N.J. Sullivan, and J.E. Martin G.J. Nabel Correlates of protective immunity for Ebola vaccines: implications for regulatory approval by the animal rule Nat. Rev. Microbiol. 7 2009 393 400
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 393-400
    • Sullivan, N.J.1    Martin, J.E.2    Nabel, G.J.3
  • 6
    • 4043053773 scopus 로고    scopus 로고
    • Pathogenesis of filoviral haemorrhagic fevers
    • S. Mahanty, and M. Bray Pathogenesis of filoviral haemorrhagic fevers Lancet Infect. Dis. 4 2004 487 498
    • (2004) Lancet Infect. Dis. , vol.4 , pp. 487-498
    • Mahanty, S.1    Bray, M.2
  • 7
    • 60249086364 scopus 로고    scopus 로고
    • No exit: Targeting the budding process to inhibit filovirus replication
    • R.N. Harty No exit: targeting the budding process to inhibit filovirus replication Antiviral Res. 81 2009 189 197
    • (2009) Antiviral Res. , vol.81 , pp. 189-197
    • Harty, R.N.1
  • 8
    • 84355166551 scopus 로고    scopus 로고
    • Identification of an antioxidant small-molecule with broad-spectrum antiviral activity
    • R.G. Panchal, and S.P. Reid S. Bavari Identification of an antioxidant small-molecule with broad-spectrum antiviral activity Antiviral Res. 93 2012 23 29
    • (2012) Antiviral Res. , vol.93 , pp. 23-29
    • Panchal, R.G.1    Reid, S.P.2    Bavari, S.3
  • 9
    • 77951240331 scopus 로고    scopus 로고
    • Antiviral activity of a small-molecule inhibitor of filovirus infection
    • T.K. Warren, and K.L. Warfield S. Bavari Antiviral activity of a small-molecule inhibitor of filovirus infection Antimicrob. Agents Chemother. 54 2010 2152 2159
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 2152-2159
    • Warren, T.K.1    Warfield, K.L.2    Bavari, S.3
  • 10
    • 29144487064 scopus 로고    scopus 로고
    • Filovirus assembly and budding
    • B. Hartlieb, and W. Weissenhorn Filovirus assembly and budding Virology 344 2006 64 70
    • (2006) Virology , vol.344 , pp. 64-70
    • Hartlieb, B.1    Weissenhorn, W.2
  • 11
    • 80052152443 scopus 로고    scopus 로고
    • Intracellular events and cell fate in filovirus infection
    • J. Olejnik, and E. Ryabchikova E. Mühlberger Intracellular events and cell fate in filovirus infection Viruses 3 2011 1501 1531
    • (2011) Viruses , vol.3 , pp. 1501-1531
    • Olejnik, J.1    Ryabchikova, E.2    Mühlberger, E.3
  • 12
    • 0032611382 scopus 로고    scopus 로고
    • The glycoproteins of Marburg and Ebola virus and their potential roles in pathogenesis
    • H. Feldmann, and V.E. Volchkov H.D. Klenk The glycoproteins of Marburg and Ebola virus and their potential roles in pathogenesis Arch. Virol. Suppl. 15 1999 159 169
    • (1999) Arch. Virol. Suppl. , vol.15 , pp. 159-169
    • Feldmann, H.1    Volchkov, V.E.2    Klenk, H.D.3
  • 13
    • 0034663762 scopus 로고    scopus 로고
    • Crystal structure of the matrix protein VP40 from Ebola virus
    • A. Dessen, and V. Volchkov W. Weissenhorn Crystal structure of the matrix protein VP40 from Ebola virus EMBO J. 19 2000 4228 4236
    • (2000) EMBO J. , vol.19 , pp. 4228-4236
    • Dessen, A.1    Volchkov, V.2    Weissenhorn, W.3
  • 14
    • 0035031534 scopus 로고    scopus 로고
    • Ebola virus VP40-induced particle formation and association with the lipid bilayer
    • L.D. Jasenosky, and G. Neumann Y. Kawaoka Ebola virus VP40-induced particle formation and association with the lipid bilayer J. Virol. 75 2001 5205 5214
    • (2001) J. Virol. , vol.75 , pp. 5205-5214
    • Jasenosky, L.D.1    Neumann, G.2    Kawaoka, Y.3
  • 15
    • 23244442927 scopus 로고    scopus 로고
    • Ebola virus VP40 late domains are not essential for viral replication in cell culture
    • G. Neumann, and H. Ebihara Y. Kawaoka Ebola virus VP40 late domains are not essential for viral replication in cell culture J. Virol. 79 2005 10300 10307
    • (2005) J. Virol. , vol.79 , pp. 10300-10307
    • Neumann, G.1    Ebihara, H.2    Kawaoka, Y.3
  • 16
    • 3142710288 scopus 로고    scopus 로고
    • Contribution of ebola virus glycoprotein, nucleoprotein, and VP24 to budding of VP40 virus-like particles
    • J.M. Licata, and R.F. Johnson R.N. Harty Contribution of ebola virus glycoprotein, nucleoprotein, and VP24 to budding of VP40 virus-like particles J. Virol. 78 2004 7344 7351
    • (2004) J. Virol. , vol.78 , pp. 7344-7351
    • Licata, J.M.1    Johnson, R.F.2    Harty, R.N.3
  • 17
  • 18
    • 0346734116 scopus 로고    scopus 로고
    • In vivo oligomerization and raft localization of Ebola virus protein VP40 during vesicular budding
    • R.G. Panchal, and G. Ruthel M.J. Aman In vivo oligomerization and raft localization of Ebola virus protein VP40 during vesicular budding Proc. Natl. Acad. Sci. USA 100 2003 15936 15941
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15936-15941
    • Panchal, R.G.1    Ruthel, G.2    Aman, M.J.3
  • 19
    • 0037303193 scopus 로고    scopus 로고
    • Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: Involvement of host proteins TSG101 and VPS-4
    • J.M. Licata, and M. Simpson-Holley R.N. Harty Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: involvement of host proteins TSG101 and VPS-4 J. Virol. 77 2003 1812 1819
    • (2003) J. Virol. , vol.77 , pp. 1812-1819
    • Licata, J.M.1    Simpson-Holley, M.2    Harty, R.N.3
  • 20
    • 80054726390 scopus 로고    scopus 로고
    • Conserved proline-rich region of Ebola virus matrix protein VP40 is essential for plasma membrane targeting and virus-like particle release
    • O. Reynard, and K. Nemirov V.E. Volchkov Conserved proline-rich region of Ebola virus matrix protein VP40 is essential for plasma membrane targeting and virus-like particle release J. Infect. Dis. 204 Suppl 3 2011 S884 S891
    • (2011) J. Infect. Dis. , vol.204 , Issue.SUPPL. 3
    • Reynard, O.1    Nemirov, K.2    Volchkov, V.E.3
  • 21
    • 40149110800 scopus 로고    scopus 로고
    • Ebola virus matrix protein VP40 uses the COPII transport system for its intracellular transport
    • S. Yamayoshi, and T. Noda Y. Kawaoka Ebola virus matrix protein VP40 uses the COPII transport system for its intracellular transport Cell Host Microbe 3 2008 168 177
    • (2008) Cell Host Microbe , vol.3 , pp. 168-177
    • Yamayoshi, S.1    Noda, T.2    Kawaoka, Y.3
  • 22
    • 77953742423 scopus 로고    scopus 로고
    • Oligomerization of Ebola virus VP40 is essential for particle morphogenesis and regulation of viral transcription
    • T. Hoenen, and N. Biedenkopf S. Becker Oligomerization of Ebola virus VP40 is essential for particle morphogenesis and regulation of viral transcription J. Virol. 84 2010 7053 7063
    • (2010) J. Virol. , vol.84 , pp. 7053-7063
    • Hoenen, T.1    Biedenkopf, N.2    Becker, S.3
  • 23
    • 0013025819 scopus 로고    scopus 로고
    • Oligomerization and polymerization of the filovirus matrix protein VP40
    • J. Timmins, and G. Schoehn W. Weissenhorn Oligomerization and polymerization of the filovirus matrix protein VP40 Virology 312 2003 359 368
    • (2003) Virology , vol.312 , pp. 359-368
    • Timmins, J.1    Schoehn, G.2    Weissenhorn, W.3
  • 24
    • 0037389018 scopus 로고    scopus 로고
    • The matrix protein VP40 from Ebola virus octamerizes into pore-like structures with specific RNA binding properties
    • F.X. Gomis-Rüth, and A. Dessen W. Weissenhorn The matrix protein VP40 from Ebola virus octamerizes into pore-like structures with specific RNA binding properties Structure 11 2003 423 433
    • (2003) Structure , vol.11 , pp. 423-433
    • Gomis-Rüth, F.X.1    Dessen, A.2    Weissenhorn, W.3
  • 25
    • 13744259224 scopus 로고    scopus 로고
    • VP40 octamers are essential for Ebola virus replication
    • T. Hoenen, and V. Volchkov W. Weissenhorn VP40 octamers are essential for Ebola virus replication J. Virol. 79 2005 1898 1905
    • (2005) J. Virol. , vol.79 , pp. 1898-1905
    • Hoenen, T.1    Volchkov, V.2    Weissenhorn, W.3
  • 26
    • 20544466388 scopus 로고    scopus 로고
    • An all-atom model of the pore-like structure of hexameric VP40 from Ebola: Structural insights into the monomer-hexamer transition
    • T.L. Nguyen, and G. Schoehn S. Bavari An all-atom model of the pore-like structure of hexameric VP40 from Ebola: structural insights into the monomer-hexamer transition J. Struct. Biol. 151 2005 30 40
    • (2005) J. Struct. Biol. , vol.151 , pp. 30-40
    • Nguyen, T.L.1    Schoehn, G.2    Bavari, S.3
  • 27
    • 35148830331 scopus 로고    scopus 로고
    • Role for amino acids 212KLR214 of Ebola virus VP40 in assembly and budding
    • S.E. McCarthy, and R.F. Johnson R.N. Harty Role for amino acids 212KLR214 of Ebola virus VP40 in assembly and budding J. Virol. 81 2007 11452 11460
    • (2007) J. Virol. , vol.81 , pp. 11452-11460
    • McCarthy, S.E.1    Johnson, R.F.2    Harty, R.N.3
  • 29
    • 36348992573 scopus 로고    scopus 로고
    • Vesicle formation by self-assembly of membrane-bound matrix proteins into a fluidlike budding domain
    • A.V. Shnyrova, and J. Ayllon V.A. Frolov Vesicle formation by self-assembly of membrane-bound matrix proteins into a fluidlike budding domain J. Cell Biol. 179 2007 627 633
    • (2007) J. Cell Biol. , vol.179 , pp. 627-633
    • Shnyrova, A.V.1    Ayllon, J.2    Frolov, V.A.3
  • 30
    • 38149030094 scopus 로고    scopus 로고
    • Determination of particle number and brightness using a laser scanning confocal microscope operating in the analog mode
    • R.B. Dalal, and M.A. Digman E. Gratton Determination of particle number and brightness using a laser scanning confocal microscope operating in the analog mode Microsc. Res. Tech. 71 2008 69 81
    • (2008) Microsc. Res. Tech. , vol.71 , pp. 69-81
    • Dalal, R.B.1    Digman, M.A.2    Gratton, E.3
  • 31
    • 44049105523 scopus 로고    scopus 로고
    • Mapping the number of molecules and brightness in the laser scanning microscope
    • M.A. Digman, and R. Dalal E. Gratton Mapping the number of molecules and brightness in the laser scanning microscope Biophys. J. 94 2008 2320 2332
    • (2008) Biophys. J. , vol.94 , pp. 2320-2332
    • Digman, M.A.1    Dalal, R.2    Gratton, E.3
  • 32
    • 60549110664 scopus 로고    scopus 로고
    • Stoichiometry of molecular complexes at adhesions in living cells
    • M.A. Digman, and P.W. Wiseman E. Gratton Stoichiometry of molecular complexes at adhesions in living cells Proc. Natl. Acad. Sci. USA 106 2009 2170 2175
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 2170-2175
    • Digman, M.A.1    Wiseman, P.W.2    Gratton, E.3
  • 33
    • 79551678673 scopus 로고    scopus 로고
    • Oligomerization state of dynamin 2 in cell membranes using TIRF and number and brightness analysis
    • J.A. Ross, and M.A. Digman D.M. Jameson Oligomerization state of dynamin 2 in cell membranes using TIRF and number and brightness analysis Biophys. J. 100 2011 L15 L17
    • (2011) Biophys. J. , vol.100
    • Ross, J.A.1    Digman, M.A.2    Jameson, D.M.3
  • 34
    • 80054720236 scopus 로고    scopus 로고
    • Unconventional secretion of Ebola virus matrix protein VP40
    • O. Reynard, and S.P. Reid V.E. Volchkov Unconventional secretion of Ebola virus matrix protein VP40 J. Infect. Dis. 204 Suppl 3 2011 S833 S839
    • (2011) J. Infect. Dis. , vol.204 , Issue.SUPPL. 3
    • Reynard, O.1    Reid, S.P.2    Volchkov, V.E.3
  • 35
    • 84893442576 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy, raster image correlation spectroscopy, and number and brightness on a commercial confocal laser scanning microscope with analog detectors (Nikon C1)
    • P.D. Moens, E. Gratton, and I.L. Salvemini Fluorescence correlation spectroscopy, raster image correlation spectroscopy, and number and brightness on a commercial confocal laser scanning microscope with analog detectors (Nikon C1) Microsc. Res. Tech. 74 2010 377 388
    • (2010) Microsc. Res. Tech. , vol.74 , pp. 377-388
    • Moens, P.D.1    Gratton, E.2    Salvemini, I.L.3
  • 36
    • 78049412062 scopus 로고    scopus 로고
    • Raster image correlation spectroscopy in live cells
    • M.J. Rossow, and J.M. Sasaki E. Gratton Raster image correlation spectroscopy in live cells Nat. Protoc. 5 2010 1761 1774
    • (2010) Nat. Protoc. , vol.5 , pp. 1761-1774
    • Rossow, M.J.1    Sasaki, J.M.2    Gratton, E.3
  • 37
    • 0034672008 scopus 로고    scopus 로고
    • Membrane association induces a conformational change in the Ebola virus matrix protein
    • S. Scianimanico, and G. Schoehn W. Weissenhorn Membrane association induces a conformational change in the Ebola virus matrix protein EMBO J. 19 2000 6732 6741
    • (2000) EMBO J. , vol.19 , pp. 6732-6741
    • Scianimanico, S.1    Schoehn, G.2    Weissenhorn, W.3
  • 38
    • 41649110901 scopus 로고    scopus 로고
    • Paxillin dynamics measured during adhesion assembly and disassembly by correlation spectroscopy
    • M.A. Digman, and C.M. Brown E. Gratton Paxillin dynamics measured during adhesion assembly and disassembly by correlation spectroscopy Biophys. J. 94 2008 2819 2831
    • (2008) Biophys. J. , vol.94 , pp. 2819-2831
    • Digman, M.A.1    Brown, C.M.2    Gratton, E.3
  • 39
    • 0034733392 scopus 로고    scopus 로고
    • Structural characterization and membrane binding properties of the matrix protein VP40 of Ebola virus
    • R.W.H. Ruigrok, and G. Schoehn W. Weissenhorn Structural characterization and membrane binding properties of the matrix protein VP40 of Ebola virus J. Mol. Biol. 300 2000 103 112
    • (2000) J. Mol. Biol. , vol.300 , pp. 103-112
    • Ruigrok, R.W.H.1    Schoehn, G.2    Weissenhorn, W.3
  • 40
    • 33947167287 scopus 로고    scopus 로고
    • Budding of Marburgvirus is associated with filopodia
    • L. Kolesnikova, and A.B. Bohil S. Becker Budding of Marburgvirus is associated with filopodia Cell. Microbiol. 9 2007 939 951
    • (2007) Cell. Microbiol. , vol.9 , pp. 939-951
    • Kolesnikova, L.1    Bohil, A.B.2    Becker, S.3
  • 41
    • 66349103875 scopus 로고    scopus 로고
    • Simulations of membrane tubulation by lattices of amphiphysin N-BAR domains
    • Y. Yin, A. Arkhipov, and K. Schulten Simulations of membrane tubulation by lattices of amphiphysin N-BAR domains Structure 17 2009 882 892
    • (2009) Structure , vol.17 , pp. 882-892
    • Yin, Y.1    Arkhipov, A.2    Schulten, K.3
  • 42
    • 73649128296 scopus 로고    scopus 로고
    • Molecular basis of the potent membrane-remodeling activity of the epsin 1 N-terminal homology domain
    • Y. Yoon, and J. Tong W. Cho Molecular basis of the potent membrane-remodeling activity of the epsin 1 N-terminal homology domain J. Biol. Chem. 285 2010 531 540
    • (2010) J. Biol. Chem. , vol.285 , pp. 531-540
    • Yoon, Y.1    Tong, J.2    Cho, W.3
  • 43
    • 79953323443 scopus 로고    scopus 로고
    • Live-cell visualization of dynamics of HIV budding site interactions with an ESCRT component
    • V. Baumgärtel, and S. Ivanchenko D.C. Lamb Live-cell visualization of dynamics of HIV budding site interactions with an ESCRT component Nat. Cell Biol. 13 2011 469 474
    • (2011) Nat. Cell Biol. , vol.13 , pp. 469-474
    • Baumgärtel, V.1    Ivanchenko, S.2    Lamb, D.C.3
  • 45
    • 79953296191 scopus 로고    scopus 로고
    • Dynamics of ESCRT protein recruitment during retroviral assembly
    • N. Jouvenet, and M. Zhadina S.M. Simon Dynamics of ESCRT protein recruitment during retroviral assembly Nat. Cell Biol. 13 2011 394 401
    • (2011) Nat. Cell Biol. , vol.13 , pp. 394-401
    • Jouvenet, N.1    Zhadina, M.2    Simon, S.M.3


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