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Volumn 7, Issue 9, 2011, Pages

Membrane remodeling by the double-barrel scaffolding protein of poxvirus

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; LIPID; PROTEIN D13; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; LIPOSOME;

EID: 80053444781     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002239     Document Type: Article
Times cited : (48)

References (45)
  • 1
    • 31844438075 scopus 로고    scopus 로고
    • Smallpox
    • doi: 10.1016/S0140-6736(06)68143-9
    • Moore ZS, Seward JF, Lane JM, (2006) Smallpox. Lancet 367: 425-435 doi:10.1016/S0140-6736(06)68143-9.
    • (2006) Lancet , vol.367 , pp. 425-435
    • Moore, Z.S.1    Seward, J.F.2    Lane, J.M.3
  • 2
    • 33746577836 scopus 로고    scopus 로고
    • In a nutshell: structure and assembly of the vaccinia virion
    • doi: 10.1016/S0065-3527(06)66002-8
    • Condit RC, Moussatche N, Traktman P, (2006) In a nutshell: structure and assembly of the vaccinia virion. Adv Virus Res 66: 31-124 doi:10.1016/S0065-3527(06)66002-8.
    • (2006) Adv Virus Res , vol.66 , pp. 31-124
    • Condit, R.C.1    Moussatche, N.2    Traktman, P.3
  • 3
    • 79952082581 scopus 로고    scopus 로고
    • Lipid Membranes in Poxvirus Replication
    • doi: 10.3390/v2040972
    • Laliberte JP, Moss B, (2010) Lipid Membranes in Poxvirus Replication. Viruses 2: 972-986 doi:10.3390/v2040972.
    • (2010) Viruses , vol.2 , pp. 972-986
    • Laliberte, J.P.1    Moss, B.2
  • 5
    • 0014315557 scopus 로고
    • Vaccinia as a model for membrane biogenesis
    • Dales S, Mosbach EH, (1968) Vaccinia as a model for membrane biogenesis. Virology 35: 564-583.
    • (1968) Virology , vol.35 , pp. 564-583
    • Dales, S.1    Mosbach, E.H.2
  • 7
    • 67651092300 scopus 로고    scopus 로고
    • Membrane rupture generates single open membrane sheets during vaccinia virus assembly
    • doi: 10.1016/j.chom.2009.05.021
    • Chlanda P, Carbajal MA, Cyrklaff M, Griffiths G, Krijnse-Locker J, (2009) Membrane rupture generates single open membrane sheets during vaccinia virus assembly. Cell Host Microbe 6: 81-90 doi:10.1016/j.chom.2009.05.021.
    • (2009) Cell Host Microbe , vol.6 , pp. 81-90
    • Chlanda, P.1    Carbajal, M.A.2    Cyrklaff, M.3    Griffiths, G.4    Krijnse-Locker, J.5
  • 8
    • 18544365212 scopus 로고    scopus 로고
    • Deep-etch EM reveals that the early poxvirus envelope is a single membrane bilayer stabilized by a geodetic "honeycomb" surface coat
    • doi: 10.1083/jcb.200412169
    • Heuser J, (2005) Deep-etch EM reveals that the early poxvirus envelope is a single membrane bilayer stabilized by a geodetic "honeycomb" surface coat. J of Cell Biol 169: 269-283 doi:10.1083/jcb.200412169.
    • (2005) J of Cell Biol , vol.169 , pp. 269-283
    • Heuser, J.1
  • 9
    • 24944546062 scopus 로고    scopus 로고
    • External scaffold of spherical immature poxvirus particles is made of protein trimers, forming a honeycomb lattice
    • doi: 10.1083/jcb.200504026
    • Szajner P, Weisberg AS, Lebowitz J, Heuser J, Moss B, (2005) External scaffold of spherical immature poxvirus particles is made of protein trimers, forming a honeycomb lattice. J of Cell Biol 170: 971-981 doi:10.1083/jcb.200504026.
    • (2005) J of Cell Biol , vol.170 , pp. 971-981
    • Szajner, P.1    Weisberg, A.S.2    Lebowitz, J.3    Heuser, J.4    Moss, B.5
  • 10
    • 69449094888 scopus 로고    scopus 로고
    • Assembly and disassembly of the capsid-like external scaffold of immature virions during vaccinia virus morphogenesis
    • doi: 10.1128/JVI.00875-09
    • Bisht H, Weisberg AS, Szajner P, Moss B, (2009) Assembly and disassembly of the capsid-like external scaffold of immature virions during vaccinia virus morphogenesis. J Virol 83: 9140-9150 doi:10.1128/JVI.00875-09.
    • (2009) J Virol , vol.83 , pp. 9140-9150
    • Bisht, H.1    Weisberg, A.S.2    Szajner, P.3    Moss, B.4
  • 11
    • 0014693136 scopus 로고
    • Rifampicin: a specific inhibitor of vaccinia virus assembly
    • Moss B, Rosenblum EN, Katz E, Grimley PM, (1969) Rifampicin: a specific inhibitor of vaccinia virus assembly. Nature 224: 1280-1284.
    • (1969) Nature , vol.224 , pp. 1280-1284
    • Moss, B.1    Rosenblum, E.N.2    Katz, E.3    Grimley, P.M.4
  • 12
    • 35148886674 scopus 로고    scopus 로고
    • The structure of a putative scaffolding protein of immature poxvirus particles as determined by electron microscopy suggests similarity with capsid proteins of large icosahedral DNA viruses
    • doi: 10.1128/JVI.00594-07
    • Hyun J-K, Coulibaly F, Turner AP, Baker EN, Mercer AA, et al. (2007) The structure of a putative scaffolding protein of immature poxvirus particles as determined by electron microscopy suggests similarity with capsid proteins of large icosahedral DNA viruses. J Virol 81: 11075-11083 doi:10.1128/JVI.00594-07.
    • (2007) J Virol , vol.81 , pp. 11075-11083
    • Hyun, J.-K.1    Coulibaly, F.2    Turner, A.P.3    Baker, E.N.4    Mercer, A.A.5
  • 13
    • 0037069358 scopus 로고    scopus 로고
    • The structure and evolution of the major capsid protein of a large, lipid-containing DNA virus
    • doi: 10.1073/pnas.232580699
    • Nandhagopal N, Simpson AA, Gurnon JR, Yan X, Baker TS, et al. (2002) The structure and evolution of the major capsid protein of a large, lipid-containing DNA virus. Proc Natl Acad Sci U S A 99: 14758-14763 doi:10.1073/pnas.232580699.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 14758-14763
    • Nandhagopal, N.1    Simpson, A.A.2    Gurnon, J.R.3    Yan, X.4    Baker, T.S.5
  • 14
    • 33645076499 scopus 로고    scopus 로고
    • Evolutionary genomics of nucleo-cytoplasmic large DNA viruses
    • doi: 10.1016/j.virusres.2006.01.009
    • Iyer LM, Balaji S, Koonin EV, Aravind L, (2006) Evolutionary genomics of nucleo-cytoplasmic large DNA viruses. Virus Res 117: 156-184 doi:10.1016/j.virusres.2006.01.009.
    • (2006) Virus Res , vol.117 , pp. 156-184
    • Iyer, L.M.1    Balaji, S.2    Koonin, E.V.3    Aravind, L.4
  • 15
    • 0033578669 scopus 로고    scopus 로고
    • Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures
    • Benson SD, Bamford JK, Bamford DH, Burnett RM, (1999) Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures. Cell 98: 825-833.
    • (1999) Cell , vol.98 , pp. 825-833
    • Benson, S.D.1    Bamford, J.K.2    Bamford, D.H.3    Burnett, R.M.4
  • 16
    • 52649169247 scopus 로고    scopus 로고
    • Insights into Virus Evolution and Membrane Biogenesis from the Structure of the Marine Lipid-Containing Bacteriophage PM2
    • doi: 10.1016/j.molcel.2008.06.026
    • Abrescia NGA, Grimes JM, Kivelä HM, Assenberg R, Sutton GC, et al. (2008) Insights into Virus Evolution and Membrane Biogenesis from the Structure of the Marine Lipid-Containing Bacteriophage PM2. Mol Cell 31: 749-761 doi:10.1016/j.molcel.2008.06.026.
    • (2008) Mol Cell , vol.31 , pp. 749-761
    • Abrescia, N.G.A.1    Grimes, J.M.2    Kivelä, H.M.3    Assenberg, R.4    Sutton, G.C.5
  • 17
    • 30044450170 scopus 로고    scopus 로고
    • Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses
    • doi: 10.1073/pnas.0506383102
    • Khayat R, Tang L, Larson ET, Lawrence CM, Young M, et al. (2005) Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses. Proc Natl Acad Sci U S A 102: 18944-18949 doi:10.1073/pnas.0506383102.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 18944-18949
    • Khayat, R.1    Tang, L.2    Larson, E.T.3    Lawrence, C.M.4    Young, M.5
  • 18
    • 0023059423 scopus 로고
    • Three-dimensional structure of the adenovirus major coat protein hexon
    • Roberts MM, White JL, Grütter MG, Burnett RM, (1986) Three-dimensional structure of the adenovirus major coat protein hexon. Science 232: 1148-1151.
    • (1986) Science , vol.232 , pp. 1148-1151
    • Roberts, M.M.1    White, J.L.2    Grütter, M.G.3    Burnett, R.M.4
  • 19
    • 27944491964 scopus 로고    scopus 로고
    • What does structure tell us about virus evolution?
    • doi: 10.1016/j.sbi.2005.10.012
    • Bamford DH, Grimes JM, Stuart DI, (2005) What does structure tell us about virus evolution? Curr Opin Struct Biol 15: 655-663 doi:10.1016/j.sbi.2005.10.012.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 655-663
    • Bamford, D.H.1    Grimes, J.M.2    Stuart, D.I.3
  • 20
    • 9744228738 scopus 로고    scopus 로고
    • Does common architecture reveal a viral lineage spanning all three domains of life?
    • doi: 10.1016/j.molcel.2004.11.016
    • Benson SD, Bamford JKH, Bamford DH, Burnett RM, (2004) Does common architecture reveal a viral lineage spanning all three domains of life? Mol Cell 16: 673-685 doi:10.1016/j.molcel.2004.11.016.
    • (2004) Mol Cell , vol.16 , pp. 673-685
    • Benson, S.D.1    Bamford, J.K.H.2    Bamford, D.H.3    Burnett, R.M.4
  • 21
    • 0035794530 scopus 로고    scopus 로고
    • Structural polymorphism of the major capsid protein of rotavirus
    • doi: 10.1093/emboj/20.7.1498
    • Lepault J, Petitpas I, Erk I, Navaza J, Bigot D, et al. (2001) Structural polymorphism of the major capsid protein of rotavirus. EMBO J 20: 1498-1507 doi:10.1093/emboj/20.7.1498.
    • (2001) EMBO J , vol.20 , pp. 1498-1507
    • Lepault, J.1    Petitpas, I.2    Erk, I.3    Navaza, J.4    Bigot, D.5
  • 22
    • 33847210648 scopus 로고    scopus 로고
    • A dissection of the protein-protein interfaces in icosahedral virus capsids
    • doi: 10.1016/j.jmb.2006.12.054
    • Bahadur RP, Rodier F, Janin J, (2007) A dissection of the protein-protein interfaces in icosahedral virus capsids. J Mol Biol 367: 574-590 doi:10.1016/j.jmb.2006.12.054.
    • (2007) J Mol Biol , vol.367 , pp. 574-590
    • Bahadur, R.P.1    Rodier, F.2    Janin, J.3
  • 23
    • 33846837294 scopus 로고    scopus 로고
    • Amino acid substitutions at multiple sites within the vaccinia virus D13 scaffold protein confer resistance to rifampicin
    • doi: 10.1016/j.virol.2006.09.031
    • Charity JC, Katz E, Moss B, (2007) Amino acid substitutions at multiple sites within the vaccinia virus D13 scaffold protein confer resistance to rifampicin. Virology 359: 227-232 doi:10.1016/j.virol.2006.09.031.
    • (2007) Virology , vol.359 , pp. 227-232
    • Charity, J.C.1    Katz, E.2    Moss, B.3
  • 24
    • 0028115847 scopus 로고
    • Assembly of vaccinia virus: effects of rifampin on the intracellular distribution of viral protein p65
    • Sodeik B, Griffiths G, Ericsson M, Moss B, Doms RW, (1994) Assembly of vaccinia virus: effects of rifampin on the intracellular distribution of viral protein p65. J Virol 68: 1103-1114.
    • (1994) J Virol , vol.68 , pp. 1103-1114
    • Sodeik, B.1    Griffiths, G.2    Ericsson, M.3    Moss, B.4    Doms, R.W.5
  • 27
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes
    • doi: 10.1107/S0907444906019949
    • Minor W, Cymborowski M, Otwinowski Z, Chruszcz M, (2006) HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes. Acta Crystallogr D Biol Crystallogr 62: 859-866 doi:10.1107/S0907444906019949.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 30
    • 36549027357 scopus 로고    scopus 로고
    • Automated structure solution with autoSHARP
    • doi: 10.1385/1-59745-266-1:215
    • Vonrhein C, Blanc E, Roversi P, Bricogne G, (2007) Automated structure solution with autoSHARP. Methods Mol Biol 364: 215 230 doi:10.1385/1-59745-266-1:215.
    • (2007) Methods Mol Biol , vol.364 , pp. 215
    • Vonrhein, C.1    Blanc, E.2    Roversi, P.3    Bricogne, G.4
  • 31
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • doi: 10.1038/nprot.2008.91
    • Langer G, Cohen SX, Lamzin VS, Perrakis A, (2008) Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat Protoc 3: 1171-1179 doi:10.1038/nprot.2008.91.
    • (2008) Nat Protoc , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 33
    • 14844321328 scopus 로고    scopus 로고
    • Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT
    • doi: 10.1107/S0907444904016427
    • Blanc E, Roversi P, Vonrhein C, Flensburg C, Lea SM, et al. (2004) Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT. Acta Crystallogr D Biol Crystallogr 60: 2210-2221 doi:10.1107/S0907444904016427.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2210-2221
    • Blanc, E.1    Roversi, P.2    Vonrhein, C.3    Flensburg, C.4    Lea, S.M.5
  • 35
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: a comprehensive Python-based system for macromolecular structure solution
    • doi: 10.1107/S0907444909052925
    • Adams PD, Afonine PV, Bunkóczi G, Chen VB, Davis IW, et al. (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66: 213-221 doi:10.1107/S0907444909052925.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1    Afonine, P.V.2    Bunkóczi, G.3    Chen, V.B.4    Davis, I.W.5
  • 36
    • 5844277742 scopus 로고    scopus 로고
    • Preparation of liposomes that mimic the membrane of endoplasmic reticulum of rat hepatocytes
    • Watanabe J, Asaka Y, Mino K, Kanamura S, (1996) Preparation of liposomes that mimic the membrane of endoplasmic reticulum of rat hepatocytes. J Electron Microsc (Tokyo) 45: 171-176.
    • (1996) J Electron Microsc (Tokyo) , vol.45 , pp. 171-176
    • Watanabe, J.1    Asaka, Y.2    Mino, K.3    Kanamura, S.4
  • 37
    • 0032853933 scopus 로고    scopus 로고
    • Two-dimensional crystallization on lipid layer: A successful approach for membrane proteins
    • doi: 10.1006/jsbi.1999.4155
    • Lévy D, Mosser G, Lambert O, Moeck GS, Bald D, et al. (1999) Two-dimensional crystallization on lipid layer: A successful approach for membrane proteins. J Struct Biol 127: 44-52 doi:10.1006/jsbi.1999.4155.
    • (1999) J Struct Biol , vol.127 , pp. 44-52
    • Lévy, D.1    Mosser, G.2    Lambert, O.3    Moeck, G.S.4    Bald, D.5
  • 38
    • 33845336533 scopus 로고    scopus 로고
    • Bsoft: image processing and molecular modeling for electron microscopy
    • doi: 10.1016/j.jsb.2006.06.006
    • Heymann JB, Belnap DM, (2007) Bsoft: image processing and molecular modeling for electron microscopy. J Struct Biol 157: 3-18 doi:10.1016/j.jsb.2006.06.006.
    • (2007) J Struct Biol , vol.157 , pp. 3-18
    • Heymann, J.B.1    Belnap, D.M.2
  • 39
    • 0029975085 scopus 로고    scopus 로고
    • MRC image processing programs
    • doi: 10.1006/jsbi.1996.0003
    • Crowther RA, Henderson R, Smith JM, (1996) MRC image processing programs. J Struct Biol 116: 9-16 doi:10.1006/jsbi.1996.0003.
    • (1996) J Struct Biol , vol.116 , pp. 9-16
    • Crowther, R.A.1    Henderson, R.2    Smith, J.M.3
  • 40
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • doi: 10.1002/jcc.20084
    • Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, et al. (2004) UCSF Chimera-a visualization system for exploratory research and analysis. Journal Comput Chem 25: 1605-1612 doi:10.1002/jcc.20084.
    • (2004) Journal Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Huang, C.C.3    Couch, G.S.4    Greenblatt, D.M.5
  • 41
    • 0031574325 scopus 로고    scopus 로고
    • Not your average density
    • Kleywegt GJ, Read RJ, (1997) Not your average density. Structure 5: 1557-1569.
    • (1997) Structure , vol.5 , pp. 1557-1569
    • Kleywegt, G.J.1    Read, R.J.2
  • 42
    • 0035783173 scopus 로고    scopus 로고
    • Using situs for flexible and rigid-body fitting of multiresolution single-molecule data
    • doi: 10.1006/jsbi.2000.4350
    • Wriggers W, Birmanns S, (2001) Using situs for flexible and rigid-body fitting of multiresolution single-molecule data. J Struct Biol 133: 193-202 doi:10.1006/jsbi.2000.4350.
    • (2001) J Struct Biol , vol.133 , pp. 193-202
    • Wriggers, W.1    Birmanns, S.2
  • 43
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • doi: 10.1016/j.jmb.2007.05.022
    • Krissinel E, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797 doi:10.1016/j.jmb.2007.05.022.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 44
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • doi: 10.1107/S0907444904026460
    • Krissinel E, Henrick K, (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60: 2256-2268 doi:10.1107/S0907444904026460.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 45
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • doi: 10.1093/nar/gkq399
    • Ashkenazy H, Erez E, Martz E, Pupko T, Ben-Tal N, (2010) ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res 38: W529-33 doi:10.1093/nar/gkq399.
    • (2010) Nucleic Acids Res , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5


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