메뉴 건너뛰기




Volumn 376, Issue 4, 2008, Pages 1168-1181

RSV Capsid Polymorphism Correlates with Polymerization Efficiency and Envelope Glycoprotein Content: Implications that Nucleation Controls Morphogenesis

Author keywords

capsid assembly; critical concentration; cryo electron tomography; nucleation of assembly; virus maturation

Indexed keywords

CAPSID PROTEIN; ENVELOPE GLYCOPROTEIN; ENVELOPE PROTEIN; FULLERENE; NUCLEOCAPSID PROTEIN; UNCLASSIFIED DRUG; VIRUS RNA;

EID: 39049108146     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.12.003     Document Type: Article
Times cited : (55)

References (53)
  • 1
    • 0003151659 scopus 로고    scopus 로고
    • Retroviral virions and genomes
    • Coffin J.M., Hughes S.H., and Varmus H. (Eds), Cold Spring Harbor Laboratory, Woodbury, NY
    • Vogt V.M. Retroviral virions and genomes. In: Coffin J.M., Hughes S.H., and Varmus H. (Eds). Retroviruses (1997), Cold Spring Harbor Laboratory, Woodbury, NY 27-70
    • (1997) Retroviruses , pp. 27-70
    • Vogt, V.M.1
  • 2
    • 20344368389 scopus 로고    scopus 로고
    • How retroviruses select their genomes
    • D'Souza V., and Summers M.F. How retroviruses select their genomes. Nat. Rev., Microbiol. 3 (2005) 643-655
    • (2005) Nat. Rev., Microbiol. , vol.3 , pp. 643-655
    • D'Souza, V.1    Summers, M.F.2
  • 3
    • 17044440108 scopus 로고    scopus 로고
    • Virus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivity
    • Steven A.C., Heymann J.B., Cheng N., Trus B.L., and Conway J.F. Virus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivity. Curr. Opin. Struct. Biol. 15 (2005) 227-236
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 227-236
    • Steven, A.C.1    Heymann, J.B.2    Cheng, N.3    Trus, B.L.4    Conway, J.F.5
  • 4
    • 0037388765 scopus 로고    scopus 로고
    • Structural organization of authentic, mature HIV-1 virions and cores
    • Briggs J.A., Wilk T., Welker R., Kräusslich H.G., and Fuller S.D. Structural organization of authentic, mature HIV-1 virions and cores. EMBO J. 22 (2003) 1707-1715
    • (2003) EMBO J. , vol.22 , pp. 1707-1715
    • Briggs, J.A.1    Wilk, T.2    Welker, R.3    Kräusslich, H.G.4    Fuller, S.D.5
  • 5
    • 1242274447 scopus 로고    scopus 로고
    • Cryoelectron microscopy of mouse mammary tumor virus
    • Briggs J.A., Watson B.E., Gowen B.E., and Fuller S.D. Cryoelectron microscopy of mouse mammary tumor virus. J. Virol. 78 (2004) 2606-2608
    • (2004) J. Virol. , vol.78 , pp. 2606-2608
    • Briggs, J.A.1    Watson, B.E.2    Gowen, B.E.3    Fuller, S.D.4
  • 7
    • 0001118596 scopus 로고    scopus 로고
    • Synthesis, assembly, and processing of viral proteins
    • Coffin J.M., Hughes S.H., and Varmus H. (Eds), Cold Spring Harbor Laboratory Press, Woodbury, NY
    • Swanstrom R., and Wills J.W. Synthesis, assembly, and processing of viral proteins. In: Coffin J.M., Hughes S.H., and Varmus H. (Eds). Retroviruses (1997), Cold Spring Harbor Laboratory Press, Woodbury, NY 263-334
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.W.2
  • 8
    • 0032560502 scopus 로고    scopus 로고
    • Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: implications for retroviral assembly mechanisms
    • Yeager M., Wilson-Kubalek E.M., Weiner S.G., Brown P.O., and Rein A. Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: implications for retroviral assembly mechanisms. Proc. Natl Acad. Sci. USA 95 (1998) 7299-7304
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7299-7304
    • Yeager, M.1    Wilson-Kubalek, E.M.2    Weiner, S.G.3    Brown, P.O.4    Rein, A.5
  • 10
    • 0031964529 scopus 로고    scopus 로고
    • Genetic determinants of Rous sarcoma virus particle size
    • Krishna N.K., Campbell S., Vogt V.M., and Wills J.W. Genetic determinants of Rous sarcoma virus particle size. J. Virol. 72 (1998) 564-577
    • (1998) J. Virol. , vol.72 , pp. 564-577
    • Krishna, N.K.1    Campbell, S.2    Vogt, V.M.3    Wills, J.W.4
  • 11
    • 27144548783 scopus 로고    scopus 로고
    • The retroviral capsid domain dictates virion size, morphology, and coassembly of gag into virus-like particles
    • Ako-Adjei D., Johnson M.C., and Vogt V.M. The retroviral capsid domain dictates virion size, morphology, and coassembly of gag into virus-like particles. J. Virol. 79 (2005) 13463-13472
    • (2005) J. Virol. , vol.79 , pp. 13463-13472
    • Ako-Adjei, D.1    Johnson, M.C.2    Vogt, V.M.3
  • 12
    • 84881194271 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals conserved and divergent features of gag packing in immature particles of Rous sarcoma virus and human immunodeficiency virus
    • Briggs J.A., Johnson M.C., Simon M.N., Fuller S.D., and Vogt V.M. Cryo-electron microscopy reveals conserved and divergent features of gag packing in immature particles of Rous sarcoma virus and human immunodeficiency virus. J. Mol. Biol. 355 (2006) 157-168
    • (2006) J. Mol. Biol. , vol.355 , pp. 157-168
    • Briggs, J.A.1    Johnson, M.C.2    Simon, M.N.3    Fuller, S.D.4    Vogt, V.M.5
  • 16
    • 0034855639 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells
    • Tang S., Murakami T., Agresta B.E., Campbell S., Freed E.O., and Levin J.G. Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells. J. Virol. 75 (2001) 9357-9366
    • (2001) J. Virol. , vol.75 , pp. 9357-9366
    • Tang, S.1    Murakami, T.2    Agresta, B.E.3    Campbell, S.4    Freed, E.O.5    Levin, J.G.6
  • 17
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • Forshey B.M., von Schwedler U., Sundquist W.I., and Aiken C. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J. Virol. 76 (2002) 5667-5677
    • (2002) J. Virol. , vol.76 , pp. 5667-5677
    • Forshey, B.M.1    von Schwedler, U.2    Sundquist, W.I.3    Aiken, C.4
  • 18
    • 0242409380 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 N-terminal capsid mutants containing cores with abnormally high levels of capsid protein and virtually no reverse transcriptase
    • Tang S., Murakami T., Cheng N., Steven A.C., Freed E.O., and Levin J.G. Human immunodeficiency virus type 1 N-terminal capsid mutants containing cores with abnormally high levels of capsid protein and virtually no reverse transcriptase. J. Virol. 77 (2003) 12592-12602
    • (2003) J. Virol. , vol.77 , pp. 12592-12602
    • Tang, S.1    Murakami, T.2    Cheng, N.3    Steven, A.C.4    Freed, E.O.5    Levin, J.G.6
  • 19
    • 0037404501 scopus 로고    scopus 로고
    • Functional surfaces of the human immunodeficiency virus type 1 capsid protein
    • von Schwedler U.K., Stray K.M., Garrus J.E., and Sundquist W.I. Functional surfaces of the human immunodeficiency virus type 1 capsid protein. J. Virol. 77 (2003) 5439-5450
    • (2003) J. Virol. , vol.77 , pp. 5439-5450
    • von Schwedler, U.K.1    Stray, K.M.2    Garrus, J.E.3    Sundquist, W.I.4
  • 20
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: from cells to molecules
    • Lucic V., Forster F., and Baumeister W. Structural studies by electron tomography: from cells to molecules. Annu. Rev. Biochem. 74 (2005) 833-865
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 833-865
    • Lucic, V.1    Forster, F.2    Baumeister, W.3
  • 25
    • 0034681298 scopus 로고    scopus 로고
    • Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses
    • Campos-Olivas R., Newman J.L., and Summers M.F. Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses. J. Mol. Biol. 296 (2000) 633-649
    • (2000) J. Mol. Biol. , vol.296 , pp. 633-649
    • Campos-Olivas, R.1    Newman, J.L.2    Summers, M.F.3
  • 27
    • 0036307640 scopus 로고    scopus 로고
    • Analysis of Rous sarcoma virus capsid protein variants assembled on lipid monolayers
    • Mayo K., Vana M.L., McDermott J., Huseby D., Leis J., and Barklis E. Analysis of Rous sarcoma virus capsid protein variants assembled on lipid monolayers. J. Mol. Biol. 316 (2002) 667-678
    • (2002) J. Mol. Biol. , vol.316 , pp. 667-678
    • Mayo, K.1    Vana, M.L.2    McDermott, J.3    Huseby, D.4    Leis, J.5    Barklis, E.6
  • 28
    • 0029103178 scopus 로고
    • Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1
    • Campbell S., and Vogt V.M. Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1. J. Virol. 69 (1995) 6487-6497
    • (1995) J. Virol. , vol.69 , pp. 6487-6497
    • Campbell, S.1    Vogt, V.M.2
  • 29
    • 0034751087 scopus 로고    scopus 로고
    • Viral DNA synthesis defects in assembly-competent Rous sarcoma virus CA mutants
    • Cairns T.M., and Craven R.C. Viral DNA synthesis defects in assembly-competent Rous sarcoma virus CA mutants. J. Virol. 75 (2001) 242-250
    • (2001) J. Virol. , vol.75 , pp. 242-250
    • Cairns, T.M.1    Craven, R.C.2
  • 30
    • 0035782860 scopus 로고    scopus 로고
    • The organization of mature Rous sarcoma virus as studied by cryoelectron microscopy
    • Kingston R.L., Olson N.H., and Vogt V.M. The organization of mature Rous sarcoma virus as studied by cryoelectron microscopy. J. Struct. Biol. 136 (2001) 67-80
    • (2001) J. Struct. Biol. , vol.136 , pp. 67-80
    • Kingston, R.L.1    Olson, N.H.2    Vogt, V.M.3
  • 31
    • 23044510524 scopus 로고    scopus 로고
    • A resolution criterion for electron tomography based on cross-validation
    • Cardone G., Grünewald K., and Steven A.C. A resolution criterion for electron tomography based on cross-validation. J. Struct. Biol. 151 (2005) 117-129
    • (2005) J. Struct. Biol. , vol.151 , pp. 117-129
    • Cardone, G.1    Grünewald, K.2    Steven, A.C.3
  • 32
    • 34247185183 scopus 로고    scopus 로고
    • Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells
    • Wright E.R., Schooler J.B., Ding H.J., Kieffer C., Fillmore C., Sundquist W.I., and Jensen G.J. Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells. EMBO J. 26 (2007) 2218-2226
    • (2007) EMBO J. , vol.26 , pp. 2218-2226
    • Wright, E.R.1    Schooler, J.B.2    Ding, H.J.3    Kieffer, C.4    Fillmore, C.5    Sundquist, W.I.6    Jensen, G.J.7
  • 33
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • Li S., Hill C.P., Sundquist W.I., and Finch J.T. Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature 407 (2000) 409-413
    • (2000) Nature , vol.407 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 35
    • 0038376141 scopus 로고    scopus 로고
    • Three-dimensional structure of the M-MuLV CA protein on a lipid monolayer: a general model for retroviral capsid assembly
    • Ganser B.K., Cheng A., Sundquist W.I., and Yeager M. Three-dimensional structure of the M-MuLV CA protein on a lipid monolayer: a general model for retroviral capsid assembly. EMBO J. 22 (2003) 2886-2892
    • (2003) EMBO J. , vol.22 , pp. 2886-2892
    • Ganser, B.K.1    Cheng, A.2    Sundquist, W.I.3    Yeager, M.4
  • 36
    • 0035123571 scopus 로고    scopus 로고
    • Characterization of Rous sarcoma virus Gag particles assembled in vitro
    • Yu F., Joshi S.M., Ma Y.M., Kingston R.L., Simon M.N., and Vogt V.M. Characterization of Rous sarcoma virus Gag particles assembled in vitro. J. Virol. 75 (2001) 2753-2764
    • (2001) J. Virol. , vol.75 , pp. 2753-2764
    • Yu, F.1    Joshi, S.M.2    Ma, Y.M.3    Kingston, R.L.4    Simon, M.N.5    Vogt, V.M.6
  • 37
    • 18844400837 scopus 로고    scopus 로고
    • Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry
    • Fokine A., Leiman P.G., Shneider M.M., Ahvazi B., Boeshans K.M., Steven A.C., et al. Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry. Proc. Natl Acad. Sci. USA 102 (2005) 7163-7168
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 7163-7168
    • Fokine, A.1    Leiman, P.G.2    Shneider, M.M.3    Ahvazi, B.4    Boeshans, K.M.5    Steven, A.C.6
  • 38
    • 0000956277 scopus 로고
    • Morphogenesis of the T4 head
    • Karam J. (Ed), American Society for Microbiology, Washington, DC
    • Black L.W., Showe M.K., and Steven A.C. Morphogenesis of the T4 head. In: Karam J. (Ed). Molecular Biology of Bacteriophage T4 (1994), American Society for Microbiology, Washington, DC 218-258
    • (1994) Molecular Biology of Bacteriophage T4 , pp. 218-258
    • Black, L.W.1    Showe, M.K.2    Steven, A.C.3
  • 39
    • 0001267296 scopus 로고
    • The shape of the T-even bacteriophage head
    • Moody M.F. The shape of the T-even bacteriophage head. Virology 26 (1965) 567-576
    • (1965) Virology , vol.26 , pp. 567-576
    • Moody, M.F.1
  • 40
    • 0016378040 scopus 로고
    • The transformation of tau particles into T4 heads. II. Transformations of the surface lattice and related observations on form determination
    • Aebi U., Bijlenga R., v.d. Broek R., Eiserling F., Kellenberger C., Kellenberger E., et al. The transformation of tau particles into T4 heads. II. Transformations of the surface lattice and related observations on form determination. J. Supramol. Struct. 2 (1974) 253-275
    • (1974) J. Supramol. Struct. , vol.2 , pp. 253-275
    • Aebi, U.1    Bijlenga, R.2    v.d. Broek, R.3    Eiserling, F.4    Kellenberger, C.5    Kellenberger, E.6
  • 41
    • 0014421280 scopus 로고
    • Studies on the morphopoiesis of the head of phage T-even. V. The formation of polyheads
    • Laemmli U.K., and Eiserling F.A. Studies on the morphopoiesis of the head of phage T-even. V. The formation of polyheads. Mol. Gen. Genet. 101 (1968) 333-345
    • (1968) Mol. Gen. Genet. , vol.101 , pp. 333-345
    • Laemmli, U.K.1    Eiserling, F.A.2
  • 42
    • 0014966072 scopus 로고
    • Studies on the morphopoiesis of the head of bacteriophage T-even. 8. Multilayered polyheads
    • Yanagida M., Boy de la Tour E., Alff-Steinberger C., and Kellenberger E. Studies on the morphopoiesis of the head of bacteriophage T-even. 8. Multilayered polyheads. J. Mol. Biol. 50 (1970) 35-58
    • (1970) J. Mol. Biol. , vol.50 , pp. 35-58
    • Yanagida, M.1    Boy de la Tour, E.2    Alff-Steinberger, C.3    Kellenberger, E.4
  • 43
    • 0017284902 scopus 로고
    • Folding and capsomere morphology of the P23 surface shell of bacteriophage T4 polyheads from mutants in five different head genes
    • Steven A.C., Aebi U., and Showe M.K. Folding and capsomere morphology of the P23 surface shell of bacteriophage T4 polyheads from mutants in five different head genes. J. Mol. Biol. 102 (1976) 373-400
    • (1976) J. Mol. Biol. , vol.102 , pp. 373-400
    • Steven, A.C.1    Aebi, U.2    Showe, M.K.3
  • 44
    • 18744391391 scopus 로고    scopus 로고
    • Plunder and stowaways: incorporation of cellular proteins by enveloped viruses
    • Cantin R., Methot S., and Tremblay M.J. Plunder and stowaways: incorporation of cellular proteins by enveloped viruses. J. Virol. 79 (2005) 6577-6587
    • (2005) J. Virol. , vol.79 , pp. 6577-6587
    • Cantin, R.1    Methot, S.2    Tremblay, M.J.3
  • 45
    • 33644806492 scopus 로고    scopus 로고
    • The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions
    • Briggs J.A., Grünewald K., Glass B., Forster F., Kräusslich H.G., and Fuller S.D. The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions. Structure 14 (2006) 15-20
    • (2006) Structure , vol.14 , pp. 15-20
    • Briggs, J.A.1    Grünewald, K.2    Glass, B.3    Forster, F.4    Kräusslich, H.G.5    Fuller, S.D.6
  • 47
    • 0347364638 scopus 로고    scopus 로고
    • Electron tomography analysis of envelope glycoprotein trimers on HIV and simian immunodeficiency virus virions
    • Zhu P., Chertova E., Bess Jr. J., Lifson J.D., Arthur L.O., Liu J., et al. Electron tomography analysis of envelope glycoprotein trimers on HIV and simian immunodeficiency virus virions. Proc. Natl Acad. Sci. USA 100 (2003) 15812-15817
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 15812-15817
    • Zhu, P.1    Chertova, E.2    Bess Jr., J.3    Lifson, J.D.4    Arthur, L.O.5    Liu, J.6
  • 48
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde D.N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152 (2005) 36-51
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 49
    • 0032751908 scopus 로고    scopus 로고
    • Tetrairidium, a four-atom cluster, is readily visible as a density label in three-dimensional cryo-EM maps of proteins at 10-25 Å resolution
    • Cheng N., Conway J.F., Watts N.R., Hainfeld J.F., Joshi V., Powell R.D., et al. Tetrairidium, a four-atom cluster, is readily visible as a density label in three-dimensional cryo-EM maps of proteins at 10-25 Å resolution. J. Struct. Biol. 127 (1999) 169-176
    • (1999) J. Struct. Biol. , vol.127 , pp. 169-176
    • Cheng, N.1    Conway, J.F.2    Watts, N.R.3    Hainfeld, J.F.4    Joshi, V.5    Powell, R.D.6
  • 50
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer J.R., Mastronarde D.N., and McIntosh J.R. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116 (1996) 71-76
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 51
    • 33845336533 scopus 로고    scopus 로고
    • Bsoft: image processing and molecular modeling for electron microscopy
    • Heymann J.B., and Belnap D.M. Bsoft: image processing and molecular modeling for electron microscopy. J. Struct. Biol. 157 (2007) 3-18
    • (2007) J. Struct. Biol. , vol.157 , pp. 3-18
    • Heymann, J.B.1    Belnap, D.M.2
  • 52
    • 0344983355 scopus 로고    scopus 로고
    • Applications of a bilateral denoising filter in biological electron microscopy
    • Jiang W., Baker M.L., Wu Q., Bajaj C., and Chiu W. Applications of a bilateral denoising filter in biological electron microscopy. J. Struct. Biol. 144 (2003) 114-122
    • (2003) J. Struct. Biol. , vol.144 , pp. 114-122
    • Jiang, W.1    Baker, M.L.2    Wu, Q.3    Bajaj, C.4    Chiu, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.