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Volumn 110, Issue 50, 2013, Pages 20063-20068

Uncoating of common cold virus is preceded by RNA switching as determined by X-ray and cryo-EM analyses of the subviral A-particle

Author keywords

3D cryo EM; Genome uncoating; Picornavirus; X ray analysis

Indexed keywords

GENOMIC RNA; SINGLE STRANDED RNA; VIRUS PROTEIN;

EID: 84890278135     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1312128110     Document Type: Article
Times cited : (49)

References (43)
  • 1
    • 64249159586 scopus 로고    scopus 로고
    • Sequencing and analyses of all known human rhinovirus genomes reveal structure and evolution
    • Palmenberg AC, et al. (2009) Sequencing and analyses of all known human rhinovirus genomes reveal structure and evolution. Science 324(5923):55-59.
    • (2009) Science , vol.324 , Issue.5923 , pp. 55-59
    • Palmenberg, A.C.1
  • 2
    • 36348997665 scopus 로고    scopus 로고
    • Clinical features and complete genome characterization of a distinct human rhinovirus (HRV) genetic cluster, probably representing a previously undetected HRV species, HRV-C, associated with acute respiratory illness in children
    • Lau SK, et al. (2007) Clinical features and complete genome characterization of a distinct human rhinovirus (HRV) genetic cluster, probably representing a previously undetected HRV species, HRV-C, associated with acute respiratory illness in children. J Clin Microbiol 45(11):3655-3664.
    • (2007) J Clin Microbiol , vol.45 , Issue.11 , pp. 3655-3664
    • Lau, S.K.1
  • 3
    • 0031870254 scopus 로고    scopus 로고
    • The poliovirus empty capsid specifically recognizes the poliovirus receptor and undergoes some, but not all, of the transitions associated with cell entry
    • Basavappa R, Gómez-Yafal A, Hogle JM(1998) The poliovirus empty capsid specifically recognizes the poliovirus receptor and undergoes some, but not all, of the transitions associated with cell entry. J Virol 72(9):7551-7556.
    • (1998) J Virol , vol.72 , Issue.9 , pp. 7551-7556
    • Basavappa, R.1    Gómez-Yafal, A.2    Hogle, J.M.3
  • 4
    • 0034725556 scopus 로고    scopus 로고
    • Structure of human rhinovirus serotype 2 (HRV2)
    • Verdaguer N, Blaas D, Fita I (2000) Structure of human rhinovirus serotype 2 (HRV2). J Mol Biol 300(5):1179-1194.
    • (2000) J Mol Biol , vol.300 , Issue.5 , pp. 1179-1194
    • Verdaguer, N.1    Blaas, D.2    Fita, I.3
  • 5
    • 0015319658 scopus 로고
    • Naturally occurring and artificially produced components of three rhinoviruses
    • Korant BD, Lonberg-Holm K, Noble J, Stasny JT (1972) Naturally occurring and artificially produced components of three rhinoviruses. Virology 48(1):71-86.
    • (1972) Virology , vol.48 , Issue.1 , pp. 71-86
    • Korant, B.D.1    Lonberg-Holm, K.2    Noble, J.3    Stasny, J.T.4
  • 6
    • 0028896662 scopus 로고
    • Amino acid substitutions in the poliovirus maturation cleavage site affect assembly and result in accumulation of provirions
    • Ansardi DC, Morrow CD (1995) Amino acid substitutions in the poliovirus maturation cleavage site affect assembly and result in accumulation of provirions. J Virol 69(3):1540-1547.
    • (1995) J Virol , vol.69 , Issue.3 , pp. 1540-1547
    • Ansardi, D.C.1    Morrow, C.D.2
  • 7
    • 0032889247 scopus 로고    scopus 로고
    • Functional coupling between replication and packaging of poliovirus replicon RNA
    • Nugent CI, Johnson KL, Sarnow P, Kirkegaard K (1999) Functional coupling between replication and packaging of poliovirus replicon RNA. J Virol 73(1):427-435.
    • (1999) J Virol , vol.73 , Issue.1 , pp. 427-435
    • Nugent, C.I.1    Johnson, K.L.2    Sarnow, P.3    Kirkegaard, K.4
  • 8
    • 0015867230 scopus 로고
    • Comparison of in vitro and cell-mediated alteration of a human Rhinovirus and its inhibition by sodium dodecyl sulfate
    • Lonberg-Holm K, Noble-Harvey J (1973) Comparison of in vitro and cell-mediated alteration of a human Rhinovirus and its inhibition by sodium dodecyl sulfate. J Virol 12(4):819-826.
    • (1973) J Virol , vol.12 , Issue.4 , pp. 819-826
    • Lonberg-Holm, K.1    Noble-Harvey, J.2
  • 9
    • 0033408492 scopus 로고    scopus 로고
    • Human rhinovirus HRV14 uncoats from early endosomes in the presence of bafilomycin
    • Bayer N, Prchla E, Schwab M, Blaas D, Fuchs R (1999) Human rhinovirus HRV14 uncoats from early endosomes in the presence of bafilomycin. FEBS Lett 463(1-2):175-178.
    • (1999) FEBS Lett , vol.463 , Issue.1-2 , pp. 175-178
    • Bayer, N.1    Prchla, E.2    Schwab, M.3    Blaas, D.4    Fuchs, R.5
  • 10
    • 0242331746 scopus 로고    scopus 로고
    • Receptor priming of major group human rhinoviruses for uncoating and entry at mild low-pH environments
    • Nurani G, Lindqvist B, Casasnovas JM (2003) Receptor priming of major group human rhinoviruses for uncoating and entry at mild low-pH environments. J Virol 77(22):11985-11991.
    • (2003) J Virol , vol.77 , Issue.22 , pp. 11985-11991
    • Nurani, G.1    Lindqvist, B.2    Casasnovas, J.M.3
  • 11
    • 0023178470 scopus 로고
    • Mechanism of entry of human rhinovirus 2 into HeLa cells
    • Neubauer C, Frasel L, Kuechler E, Blaas D (1987) Mechanism of entry of human rhinovirus 2 into HeLa cells. Virology 158(1):255-258.
    • (1987) Virology , vol.158 , Issue.1 , pp. 255-258
    • Neubauer, C.1    Frasel, L.2    Kuechler, E.3    Blaas, D.4
  • 12
    • 70350312966 scopus 로고    scopus 로고
    • Low pH-triggered beta-propeller switch of the low-density lipoprotein receptor assists rhinovirus infection
    • Konecsni T, et al. (2009) Low pH-triggered beta-propeller switch of the low-density lipoprotein receptor assists rhinovirus infection. J Virol 83(21):10922-10930.
    • (2009) J Virol , vol.83 , Issue.21 , pp. 10922-10930
    • Konecsni, T.1
  • 13
    • 0025273268 scopus 로고
    • Cell-induced conformational change in poliovirus: Externalization of the amino terminus of VP1 is responsible for liposome binding
    • Fricks CE, Hogle JM (1990) Cell-induced conformational change in poliovirus: Externalization of the amino terminus of VP1 is responsible for liposome binding. J Virol 64(5):1934-1945.
    • (1990) J Virol , vol.64 , Issue.5 , pp. 1934-1945
    • Fricks, C.E.1    Hogle, J.M.2
  • 14
    • 79961205983 scopus 로고    scopus 로고
    • Liposomal nanocontainers as models for viral infection: Monitoring viral genomic RNA transfer through lipid membranes
    • Bilek G, et al. (2011) Liposomal nanocontainers as models for viral infection: Monitoring viral genomic RNA transfer through lipid membranes. J Virol 85(16):8368-8375.
    • (2011) J Virol , vol.85 , Issue.16 , pp. 8368-8375
    • Bilek, G.1
  • 15
    • 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 HC, Bostina M, Filman DJ, Hogle JM (2010) Catching a virus in the act of RNA release: A novel poliovirus uncoating intermediate characterized by cryo-electron microscopy. J Virol 84(9):4426-4441.
    • (2010) J Virol , vol.84 , Issue.9 , pp. 4426-4441
    • Levy, H.C.1    Bostina, M.2    Filman, D.J.3    Hogle, J.M.4
  • 16
    • 84857488318 scopus 로고    scopus 로고
    • Insights into minor group rhinovirus uncoating: The X-ray structure of the HRV2 empty capsid
    • Garriga D, et al. (2012) Insights into minor group rhinovirus uncoating: The X-ray structure of the HRV2 empty capsid. PLoS Pathog 8(1):e1002473.
    • (2012) PLoS Pathog , vol.8 , Issue.1
    • Garriga, D.1
  • 17
    • 84861316194 scopus 로고    scopus 로고
    • A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71
    • Wang X, et al. (2012) A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71. Nat Struct Mol Biol 19(4):424-429.
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.4 , pp. 424-429
    • Wang, X.1
  • 18
    • 84862976646 scopus 로고    scopus 로고
    • Characterization of rhinovirus subviral A particles via capillary electrophoresis, electron microscopy and gas-phase electrophoretic mobility molecular analysis: Part I
    • Weiss VU, et al. (2012) Characterization of rhinovirus subviral A particles via capillary electrophoresis, electron microscopy and gas-phase electrophoretic mobility molecular analysis: Part I. Electrophoresis 33(12):1833-1841.
    • (2012) Electrophoresis , vol.33 , Issue.12 , pp. 1833-1841
    • Weiss, V.U.1
  • 19
    • 0037689527 scopus 로고    scopus 로고
    • Structural analysis of human rhinovirus complexed with ICAM-1 reveals the dynamics of receptor-mediated virus uncoating
    • Xing L, Casasnovas JM, Cheng RH (2003) Structural analysis of human rhinovirus complexed with ICAM-1 reveals the dynamics of receptor-mediated virus uncoating. J Virol 77(11):6101-6107.
    • (2003) J Virol , vol.77 , Issue.11 , pp. 6101-6107
    • Xing, L.1    Casasnovas, J.M.2    Cheng, R.H.3
  • 20
    • 1542287500 scopus 로고    scopus 로고
    • Cryoelectron microscopy analysis of the structural changes associated with human rhinovirus type 14 uncoating
    • Hewat EA, Blaas D (2004) Cryoelectron microscopy analysis of the structural changes associated with human rhinovirus type 14 uncoating. J Virol 78(6):2935-2942.
    • (2004) J Virol , vol.78 , Issue.6 , pp. 2935-2942
    • Hewat, E.A.1    Blaas, D.2
  • 21
    • 0033977270 scopus 로고    scopus 로고
    • Molecular tectonic model of virus structural transitions: The putative cell entry states of poliovirus
    • Belnap DM, et al. (2000) Molecular tectonic model of virus structural transitions: The putative cell entry states of poliovirus. J Virol 74(3):1342-1354.
    • (2000) J Virol , vol.74 , Issue.3 , pp. 1342-1354
    • Belnap, D.M.1
  • 22
    • 80053948556 scopus 로고    scopus 로고
    • An externalized polypeptide partitions between two distinct sites on genome-released poliovirus particles
    • Lin J, et al. (2011) An externalized polypeptide partitions between two distinct sites on genome-released poliovirus particles. J Virol 85(19):9974-9983.
    • (2011) J Virol , vol.85 , Issue.19 , pp. 9974-9983
    • Lin, J.1
  • 23
    • 84885907969 scopus 로고    scopus 로고
    • Picornavirus uncoating intermediate captured in atomic detail
    • Ren J, et al. (2013) Picornavirus uncoating intermediate captured in atomic detail. Nat Commun 4:1929.
    • (2013) Nat Commun , vol.4 , pp. 1929
    • Ren, J.1
  • 24
    • 0031569393 scopus 로고    scopus 로고
    • The refined structure of human rhinovirus 16 at 2.15 A resolution: Implications for the viral life cycle
    • Hadfield AT, et al. (1997) The refined structure of human rhinovirus 16 at 2.15 A resolution: Implications for the viral life cycle. Structure 5(3):427-441.
    • (1997) Structure , vol.5 , Issue.3 , pp. 427-441
    • Hadfield, A.T.1
  • 25
    • 0030780581 scopus 로고    scopus 로고
    • Dissecting the roles of VP0 cleavage and RNA packaging in picornavirus capsid stabilization: The structure of empty capsids of foot-and-mouth disease virus
    • Curry S, et al. (1997) Dissecting the roles of VP0 cleavage and RNA packaging in picornavirus capsid stabilization: The structure of empty capsids of foot-and-mouth disease virus. J Virol 71(12):9743-9752.
    • (1997) J Virol , vol.71 , Issue.12 , pp. 9743-9752
    • Curry, S.1
  • 26
    • 0016632752 scopus 로고
    • Fractionation of biologically active and inactive populations of human rhinovirus type 2
    • Korant BD, Lonberg-Holm K, Yin FH, Noble-Harvey J (1975) Fractionation of biologically active and inactive populations of human rhinovirus type 2. Virology 63(2):384-394.
    • (1975) Virology , vol.63 , Issue.2 , pp. 384-394
    • Korant, B.D.1    Lonberg-Holm, K.2    Yin, F.H.3    Noble-Harvey, J.4
  • 27
    • 0028152426 scopus 로고
    • Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: Structure of the empty capsid assembly intermediate at 2.9 A resolution
    • Basavappa R, et al. (1994) Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: Structure of the empty capsid assembly intermediate at 2.9 A resolution. Protein Sci 3(10):1651-1669.
    • (1994) Protein Sci , vol.3 , Issue.10 , pp. 1651-1669
    • Basavappa, R.1
  • 28
    • 33749462736 scopus 로고    scopus 로고
    • The structural and functional role of RNA in icosahedral virus assembly
    • Schneemann A (2006) The structural and functional role of RNA in icosahedral virus assembly. Annu Rev Microbiol 60:51-67.
    • (2006) Annu Rev Microbiol , vol.60 , pp. 51-67
    • Schneemann, A.1
  • 29
    • 84861310674 scopus 로고    scopus 로고
    • A 3D framework for understanding enterovirus 71
    • Hogle JM (2012) A 3D framework for understanding enterovirus 71. Nat Struct Mol Biol 19(4):367-368.
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.4 , pp. 367-368
    • Hogle, J.M.1
  • 30
    • 35148838173 scopus 로고    scopus 로고
    • Single particle cryoelectron tomography characterization of the structure and structural variability of poliovirus-receptor-membrane complex at A resolution
    • Bostina M, et al. (2007) Single particle cryoelectron tomography characterization of the structure and structural variability of poliovirus-receptor-membrane complex at A resolution. J Struct Biol 160(2):200-210.
    • (2007) J Struct Biol , vol.160 , Issue.2 , pp. 200-210
    • Bostina, M.1
  • 31
    • 22144468063 scopus 로고    scopus 로고
    • Cryo-electron microscopy reconstruction of a poliovirus-receptor-membrane complex
    • Bubeck D, Filman DJ, Hogle JM (2005) Cryo-electron microscopy reconstruction of a poliovirus-receptor-membrane complex. Nat Struct Mol Biol 12(7):615-618.
    • (2005) Nat Struct Mol Biol , vol.12 , Issue.7 , pp. 615-618
    • Bubeck, D.1    Filman, D.J.2    Hogle, J.M.3
  • 32
    • 84876860485 scopus 로고    scopus 로고
    • Viral uncoating is directional: Exit of the genomic RNA in a common cold virus starts with the poly-(A) tail at the 3?-end
    • Harutyunyan S, et al. (2013) Viral uncoating is directional: Exit of the genomic RNA in a common cold virus starts with the poly-(A) tail at the 3?-end. PLoS Pathog 9(4):e1003270.
    • (2013) PLoS Pathog , vol.9 , Issue.4
    • Harutyunyan, S.1
  • 33
    • 0037770209 scopus 로고    scopus 로고
    • A cellular receptor of human rhinovirus type 2, the very-low-density lipoprotein receptor, binds to two neighboring proteins of the viral capsid
    • Neumann E, Moser R, Snyers L, Blaas D, Hewat EA (2003) A cellular receptor of human rhinovirus type 2, the very-low-density lipoprotein receptor, binds to two neighboring proteins of the viral capsid. J Virol 77(15):8504-8511.
    • (2003) J Virol , vol.77 , Issue.15 , pp. 8504-8511
    • Neumann, E.1    Moser, R.2    Snyers, L.3    Blaas, D.4    Hewat, E.A.5
  • 34
    • 34250845791 scopus 로고    scopus 로고
    • Infectious bursal disease virus capsid assembly and maturation by structural rearrangements of a transient molecular switch
    • Luque D, et al. (2007) Infectious bursal disease virus capsid assembly and maturation by structural rearrangements of a transient molecular switch. J Virol 81(13):6869-6878.
    • (2007) J Virol , vol.81 , Issue.13 , pp. 6869-6878
    • Luque, D.1
  • 35
    • 0034517231 scopus 로고    scopus 로고
    • Leginon: An automated system for acquisition of images from vitreous ice specimens
    • Carragher B, et al. (2000) Leginon: An automated system for acquisition of images from vitreous ice specimens. J Struct Biol 132(1):33-45.
    • (2000) J Struct Biol , vol.132 , Issue.1 , pp. 33-45
    • Carragher, B.1
  • 37
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell JA, Grigorieff N (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 142(3):334-347.
    • (2003) J Struct Biol , vol.142 , Issue.3 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 38
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53(Pt 3):240-255.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.PART 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 39
    • 0032128419 scopus 로고    scopus 로고
    • Miscellaneous algorithms for density modification
    • Cowtan K, Main P (1998) Miscellaneous algorithms for density modification. Acta Crystallogr D Biol Crystallogr 54(Pt 4):487-493.
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , Issue.PART 4 , pp. 487-493
    • Cowtan, K.1    Main, P.2
  • 40
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 PART 1 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 41
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera-A visualization system for exploratory research and analysis. J Comput Chem 25(13):1605-1612.
    • (2004) J Comput Chem , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1
  • 42
    • 68149149564 scopus 로고    scopus 로고
    • UROX 2.0: An interactive tool for fitting atomic models into electron-microscopy reconstructions
    • Siebert X, Navaza J (2009) UROX 2.0: An interactive tool for fitting atomic models into electron-microscopy reconstructions. Acta Crystallogr D Biol Crystallogr 65(Pt 7):651-658.
    • (2009) Acta Crystallogr D Biol Crystallogr , vol.65 , Issue.PART 7 , pp. 651-658
    • Siebert, X.1    Navaza, J.2
  • 43
    • 84861325747 scopus 로고    scopus 로고
    • Structure of the Fab-labeled breathing state of native poliovirus
    • Lin J, et al. (2012) Structure of the Fab-labeled breathing state of native poliovirus. J Virol 86(10):5959-5962.
    • (2012) J Virol , vol.86 , Issue.10 , pp. 5959-5962
    • Lin, J.1


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