메뉴 건너뛰기




Volumn 4, Issue , 2013, Pages

Picornavirus uncoating intermediate captured in atomic detail

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; PROTEIN VP1; PROTEIN VP2; PROTEIN VP3; PROTEIN VP4; VIRUS RNA;

EID: 84885907969     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms2889     Document Type: Article
Times cited : (137)

References (39)
  • 1
    • 34447502257 scopus 로고    scopus 로고
    • Cell entry by enveloped viruses: Redox considerations for HIV and SARS-coronavirus
    • Fenouillet, E., Barbouche, R. & Jones, I. M. Cell entry by enveloped viruses: redox considerations for HIV and SARS-coronavirus. Antioxid. Redox Signal. 9, 1009-1034 (2007).
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 1009-1034
    • Fenouillet, E.1    Barbouche, R.2    Jones, I.M.3
  • 2
    • 84873097195 scopus 로고    scopus 로고
    • The bacteriophage t7 virion undergoes extensive structural remodeling during infection
    • Hu, B., Margolin, W., Molineux, I. J. & Liu, J. The bacteriophage t7 virion undergoes extensive structural remodeling during infection. Science 339, 576-579 (2013).
    • (2013) Science , vol.339 , pp. 576-579
    • Hu, B.1    Margolin, W.2    Molineux, I.J.3    Liu, J.4
  • 3
    • 0004250845 scopus 로고    scopus 로고
    • Wolters Kluwer Health/Lippincott Williams & Wilkins, Philadelphia
    • Fields, B. N., Knipe, D. M. & Howley, P. M. Fields Virology (Wolters Kluwer Health/Lippincott Williams & Wilkins, Philadelphia, 2007).
    • (2007) Fields Virology
    • Fields, B.N.1    Knipe, D.M.2    Howley, P.M.3
  • 4
    • 0028341259 scopus 로고
    • Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature
    • Li, Q., Yafal, A. G., Lee, Y. M., Hogle, J. & Chow, M. Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature. J Virol. 68, 3965-3970 (1994).
    • (1994) J Virol. , vol.68 , pp. 3965-3970
    • Li, Q.1    Yafal, A.G.2    Lee, Y.M.3    Hogle, J.4    Chow, M.5
  • 6
    • 84864123281 scopus 로고    scopus 로고
    • Structural analysis of coxsackievirus A7 reveals conformational changes associated with uncoating
    • Seitsonen, J. J. et al. Structural analysis of coxsackievirus A7 reveals conformational changes associated with uncoating. J. Virol. 86, 7207-7215 (2012).
    • (2012) J. Virol. , vol.86 , pp. 7207-7215
    • Seitsonen, J.J.1
  • 7
    • 78650670078 scopus 로고    scopus 로고
    • Poliovirus RNA is released from the capsid near a twofold symmetry axis
    • Bostina, M., Levy, H., Filman, D. J. & Hogle, J. M. Poliovirus RNA is released from the capsid near a twofold symmetry axis. J. Virol. 85, 776-783 (2011).
    • (2011) J. Virol. , vol.85 , pp. 776-783
    • Bostina, M.1    Levy, H.2    Filman, D.J.3    Hogle, J.M.4
  • 8
    • 0033977270 scopus 로고    scopus 로고
    • Molecular tectonic model of virus structural transitions: The putative cell entry states of poliovirus
    • Belnap, D. M. et al. Molecular tectonic model of virus structural transitions: the putative cell entry states of poliovirus. J. Virol. 74, 1342-1354 (2000).
    • (2000) J. Virol. , vol.74 , pp. 1342-1354
    • Belnap, D.M.1
  • 9
    • 17044373783 scopus 로고    scopus 로고
    • The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes
    • Bubeck, D. et al. The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. J. Virol. 79, 7745-7755 (2005).
    • (2005) J. Virol. , vol.79 , pp. 7745-7755
    • Bubeck, D.1
  • 10
    • 77950852687 scopus 로고    scopus 로고
    • Catching a virus in the act of RNA release: A novel poliovirus uncoating intermediate characterized by cryo-electron microscopy
    • Levy, H. C., Bostina, M., Filman, D. J. & Hogle, J. M. Catching a virus in the act of RNA release: a novel poliovirus uncoating intermediate characterized by cryo-electron microscopy. J. Virol. 84, 4426-4441 (2010).
    • (2010) J. Virol. , vol.84 , pp. 4426-4441
    • Levy, H.C.1    Bostina, M.2    Filman, D.J.3    Hogle, J.M.4
  • 11
    • 0036670673 scopus 로고    scopus 로고
    • The concerted conformational changes during human rhinovirus 2 uncoating
    • Hewat, E. A., Neumann, E. & Blaas, D. The concerted conformational changes during human rhinovirus 2 uncoating. Mol. Cell 10, 317-326 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 317-326
    • Hewat, E.A.1    Neumann, E.2    Blaas, D.3
  • 12
    • 1542287500 scopus 로고    scopus 로고
    • Cryoelectron microscopy analysis of the structural changes associated with human rhinovirus type 14 uncoating
    • Hewat, E. A. & Blaas, D. Cryoelectron microscopy analysis of the structural changes associated with human rhinovirus type 14 uncoating. J. Virol. 78, 2935-2942 (2004).
    • (2004) J. Virol. , vol.78 , pp. 2935-2942
    • Hewat, E.A.1    Blaas, D.2
  • 13
    • 84857488318 scopus 로고    scopus 로고
    • Insights into minor group rhinovirus uncoating: The X-ray structure of the HRV2 empty capsid
    • Garriga, D. et al. Insights into minor group rhinovirus uncoating: the X-ray structure of the HRV2 empty capsid. PLoS Pathog. 8, e1002473 (2012).
    • (2012) PLoS Pathog. , vol.8
    • Garriga, D.1
  • 14
    • 84861316194 scopus 로고    scopus 로고
    • A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71
    • Wang, X. et al. A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71. Nat. Struct. Mol. Biol. 19, 424-429 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 424-429
    • Wang, X.1
  • 15
    • 0025273268 scopus 로고
    • Cell-induced conformational change in poliovirus: Externalization of the amino terminus of VP1 is responsible for liposome binding
    • Fricks, C. E. & Hogle, J. M. Cell-induced conformational change in poliovirus: externalization of the amino terminus of VP1 is responsible for liposome binding. J. Virol. 64, 1934-1945 (1990).
    • (1990) J. Virol. , vol.64 , pp. 1934-1945
    • Fricks, C.E.1    Hogle, J.M.2
  • 16
    • 33645997366 scopus 로고    scopus 로고
    • Characterization of early steps in the poliovirus infection process: Receptor-decorated liposomes induce conversion of the virus to membrane-anchored entry-intermediate particles
    • Tuthill, T. J., Bubeck, D., Rowlands, D. J. & Hogle, J. M. Characterization of early steps in the poliovirus infection process: Receptor-decorated liposomes induce conversion of the virus to membrane-anchored entry-intermediate particles. J. Virol. 80, 172-180 (2006).
    • (2006) J. Virol. , vol.80 , pp. 172-180
    • Tuthill, T.J.1    Bubeck, D.2    Rowlands, D.J.3    Hogle, J.M.4
  • 17
    • 0344942597 scopus 로고    scopus 로고
    • Genome delivery and ion channel properties are altered in VP4 mutants of poliovirus
    • Danthi, P., Tosteson, M., Li, Q. H. & Chow, M. Genome delivery and ion channel properties are altered in VP4 mutants of poliovirus. J. Virol. 77, 5266-5274 (2003).
    • (2003) J. Virol. , vol.77 , pp. 5266-5274
    • Danthi, P.1    Tosteson, M.2    Li, Q.H.3    Chow, M.4
  • 19
    • 77951991686 scopus 로고    scopus 로고
    • An emerging recombinant human enterovirus 71 responsible for the 2008 outbreak of hand foot and mouth disease in Fuyang city of China
    • Zhang, Y. et al. An emerging recombinant human enterovirus 71 responsible for the 2008 outbreak of hand foot and mouth disease in Fuyang city of China. Virol. J. 7, 94 (2010).
    • (2010) Virol. J. , vol.7 , pp. 94
    • Zhang, Y.1
  • 20
    • 0022401514 scopus 로고
    • Structure of a human common cold virus and functional relationship to other picornaviruses
    • Rossmann, M. G. et al. Structure of a human common cold virus and functional relationship to other picornaviruses. Nature 317, 145-153 (1985).
    • (1985) Nature , vol.317 , pp. 145-153
    • Rossmann, M.G.1
  • 21
    • 0017685815 scopus 로고
    • Studies on the in vitro uncoating of poliovirus. II. Characteristics of the membrane-modified particle
    • De Sena, J. & Mandel, B. Studies on the in vitro uncoating of poliovirus. II. Characteristics of the membrane-modified particle. Virology 78, 554-566 (1977).
    • (1977) Virology , vol.78 , pp. 554-566
    • De Sena, J.1    Mandel, B.2
  • 22
    • 0000091801 scopus 로고
    • Early interactions between poliovirus and ERK cells: Some observations on the nature and significance of the rejected particles
    • Fenwick, M. L. & Cooper, P. D. Early interactions between poliovirus and ERK cells: some observations on the nature and significance of the rejected particles. Virology 18, 212-223 (1962).
    • (1962) Virology , vol.18 , pp. 212-223
    • Fenwick, M.L.1    Cooper, P.D.2
  • 23
    • 34547112855 scopus 로고    scopus 로고
    • Imaging poliovirus entry in live cells
    • Brandenburg, B. et al. Imaging poliovirus entry in live cells. PLoS Biol. 5, 1543-1555 (2007).
    • (2007) PLoS Biol. , vol.5 , pp. 1543-1555
    • Brandenburg, B.1
  • 24
    • 84860295016 scopus 로고    scopus 로고
    • In situ macromolecular crystallography using microbeams
    • Axford, D. et al. In situ macromolecular crystallography using microbeams. Acta Crystallogr. D Biol. Crystallogr. 68, 592-600 (2012).
    • (2012) Acta Crystallogr. D Biol. Crystallogr. , vol.68 , pp. 592-600
    • Axford, D.1
  • 25
    • 84864306558 scopus 로고    scopus 로고
    • A plate-based high-throughput assay for virus stability and vaccine formulation
    • Walter, T. S. et al. A plate-based high-throughput assay for virus stability and vaccine formulation. J. Virol. Methods 185, 166-170 (2012).
    • (2012) J. Virol. Methods , vol.185 , pp. 166-170
    • Walter, T.S.1
  • 28
    • 0141457290 scopus 로고    scopus 로고
    • Evidence for assembly-dependent folding of protein and RNA in an icosahedral virus
    • Lin, T. W., Cavarelli, J. & Johnson, J. E. Evidence for assembly-dependent folding of protein and RNA in an icosahedral virus. Virology 314, 26-33 (2003).
    • (2003) Virology , vol.314 , pp. 26-33
    • Lin, T.W.1    Cavarelli, J.2    Johnson, J.E.3
  • 29
    • 80053948556 scopus 로고    scopus 로고
    • An externalized polypeptide partitions between two distinct sites on genome-released poliovirus particles
    • Lin, J. et al. An externalized polypeptide partitions between two distinct sites on genome-released poliovirus particles. J. Virol. 85, 9974-9983 (2011).
    • (2011) J. Virol. , vol.85 , pp. 9974-9983
    • Lin, J.1
  • 30
    • 84861325747 scopus 로고    scopus 로고
    • Structure of the Fab-labeled "breathing" state of native poliovirus
    • Lin, J. et al. Structure of the Fab-labeled "breathing" state of native poliovirus. J. Virol. 86, 5959-5962 (2012).
    • (2012) J. Virol. , vol.86 , pp. 5959-5962
    • Lin, J.1
  • 31
    • 41949107250 scopus 로고    scopus 로고
    • Recombinant VP4 of human rhinovirus induces permeability in model membranes
    • Davis, M. P. et al. Recombinant VP4 of human rhinovirus induces permeability in model membranes. J. Virol. 82, 4169-4174 (2008).
    • (2008) J. Virol. , vol.82 , pp. 4169-4174
    • Davis, M.P.1
  • 32
    • 84875520601 scopus 로고    scopus 로고
    • RNA transfer from poliovirus 135S particles across membranes is mediated by long umbilical connectors
    • Strauss, M., Levy, H., Bostina, M., Filman, D. J. & Hogle, J. M. RNA transfer from poliovirus 135S particles across membranes is mediated by long umbilical connectors. J. Virol. 87, 3903-3914 (2013).
    • (2013) J. Virol. , vol.87 , pp. 3903-3914
    • Strauss, M.1    Levy, H.2    Bostina, M.3    Filman, D.J.4    Hogle, J.M.5
  • 33
    • 73949155476 scopus 로고    scopus 로고
    • Equine rhinitis A virus and its low pH empty particle: Clues towards an aphthovirus entry mechanism?
    • Tuthill, T. J. et al. Equine rhinitis A virus and its low pH empty particle: clues towards an aphthovirus entry mechanism? PLoS Pathog. 5, e1000620 (2009).
    • (2009) PLoS Pathog. , vol.5
    • Tuthill, T.J.1
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray Diffraction Data Collected in Oscillation Mode
    • Carter, C. W. & Sweet, R. M. Academic Press, New York
    • Otwinowski, Z. & Minor, W. Processing of X-ray Diffraction Data Collected in Oscillation Mode. in Methods in Enzymology Vol. 276 (eds Carter, C. W. & Sweet, R. M.) 307-326 (Academic Press, New York, 1997).
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • Vagin, A. & Teplyakov, A. An approach to multi-copy search in molecular replacement. Acta Crystallogr. D Biol. Crystallogr. 56, 1622-1624 (2000).
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 36
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 38
    • 0000243829 scopus 로고
    • Procheck-a Program to Check the Stereochemical Quality of Protein Structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S. & Thornton, J. M. Procheck-a Program to Check the Stereochemical Quality of Protein Structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 39
    • 0018792428 scopus 로고
    • Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6A
    • Stuart, D. I., Levine, M., Muirhead, H. & Stammers, D. K. Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6A. J. Mol. Biol. 134, 109-142 (1979).
    • (1979) J. Mol. Biol. , vol.134 , pp. 109-142
    • Stuart, D.I.1    Levine, M.2    Muirhead, H.3    Stammers, D.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.