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Volumn 53, Issue 34, 2014, Pages 5496-5504

The hepatitis B virus core protein intradimer interface modulates capsid assembly and stability

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; GENES; PROTEINS; SULFUR COMPOUNDS; VIRUSES;

EID: 84906857591     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500732b     Document Type: Article
Times cited : (53)

References (46)
  • 1
    • 0019075292 scopus 로고
    • Movement and self-control in protein assemblies. Quasi-equivalence revisited
    • Caspar, D. L. (1980) Movement and self-control in protein assemblies. Quasi-equivalence revisited Biophys. J. 32, 103-138
    • (1980) Biophys. J. , vol.32 , pp. 103-138
    • Caspar, D.L.1
  • 2
    • 78650754124 scopus 로고    scopus 로고
    • Virus assembly, allostery and antivirals
    • Zlotnick, A. and Mukhopadhyay, S. (2011) Virus assembly, allostery and antivirals Trends Microbiol. 19, 14-23
    • (2011) Trends Microbiol. , vol.19 , pp. 14-23
    • Zlotnick, A.1    Mukhopadhyay, S.2
  • 3
    • 73949118464 scopus 로고    scopus 로고
    • Conformational changes in the hepatitis B virus core protein are consistent with a role for allostery in virus assembly
    • Packianathan, C., Katen, S. P., Dann, C. E., III, and Zlotnick, A. (2010) Conformational changes in the hepatitis B virus core protein are consistent with a role for allostery in virus assembly J. Virol. 84, 1607-1615
    • (2010) J. Virol. , vol.84 , pp. 1607-1615
    • Packianathan, C.1    Katen, S.P.2    Dann III, C.E.3    Zlotnick, A.4
  • 4
    • 73649086857 scopus 로고    scopus 로고
    • Dynamic allostery controls coat protein conformer switching during MS2 phage assembly
    • Dykeman, E. C., Stockley, P. G., and Twarock, R. (2010) Dynamic allostery controls coat protein conformer switching during MS2 phage assembly J. Mol. Biol. 395, 916-923
    • (2010) J. Mol. Biol. , vol.395 , pp. 916-923
    • Dykeman, E.C.1    Stockley, P.G.2    Twarock, R.3
  • 5
    • 77952401424 scopus 로고    scopus 로고
    • NMR relaxation studies of an RNA-binding segment of the rous sarcoma virus gag polyprotein in free and bound states: A model for autoinhibition of assembly
    • Taylor, G. M., Ma, L., Vogt, V. M., and Post, C. B. (2010) NMR relaxation studies of an RNA-binding segment of the rous sarcoma virus gag polyprotein in free and bound states: A model for autoinhibition of assembly Biochemistry 49, 4006-4017
    • (2010) Biochemistry , vol.49 , pp. 4006-4017
    • Taylor, G.M.1    Ma, L.2    Vogt, V.M.3    Post, C.B.4
  • 6
    • 3543096838 scopus 로고    scopus 로고
    • Zinc ions trigger conformational change and oligomerization of hepatitis B virus capsid protein
    • Stray, S. J., Ceres, P., and Zlotnick, A. (2004) Zinc ions trigger conformational change and oligomerization of hepatitis B virus capsid protein Biochemistry 43, 9989-9998
    • (2004) Biochemistry , vol.43 , pp. 9989-9998
    • Stray, S.J.1    Ceres, P.2    Zlotnick, A.3
  • 7
    • 73949118464 scopus 로고    scopus 로고
    • Conformational changes in the hepatitis B virus core protein are consistent with a role for allostery in virus assembly
    • Packianathan, C., Katen, S. P., Dann, C. E., III, and Zlotnick, A. (2009) Conformational changes in the hepatitis B virus core protein are consistent with a role for allostery in virus assembly J. Virol. 84, 1607-1615
    • (2009) J. Virol. , vol.84 , pp. 1607-1615
    • Packianathan, C.1    Katen, S.P.2    Dann III, C.E.3    Zlotnick, A.4
  • 9
    • 0028307177 scopus 로고
    • Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy
    • Crowther, R. A., Kiselev, N. A., Bottcher, B., Berriman, J. A., Borisova, G. P., Ose, V., and Pumpens, P. (1994) Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy Cell 77, 943-950
    • (1994) Cell , vol.77 , pp. 943-950
    • Crowther, R.A.1    Kiselev, N.A.2    Bottcher, B.3    Berriman, J.A.4    Borisova, G.P.5    Ose, V.6    Pumpens, P.7
  • 10
    • 0025316017 scopus 로고
    • Hepatitis B virus nucleocapsid assembly: Primary structure requirements in the core protein
    • Birnbaum, F. and Nassal, M. (1990) Hepatitis B virus nucleocapsid assembly: Primary structure requirements in the core protein J. Virol. 64, 3319-3330
    • (1990) J. Virol. , vol.64 , pp. 3319-3330
    • Birnbaum, F.1    Nassal, M.2
  • 11
    • 0028953769 scopus 로고
    • Hepatitis core antigen produced in Escherichia coli: Subunit composition, conformational analysis, and in vitro capsid assembly
    • Wingfield, P. T., Stahl, S. J., Williams, R. W., and Steven, A. C. (1995) Hepatitis core antigen produced in Escherichia coli: Subunit composition, conformational analysis, and in vitro capsid assembly Biochemistry 34, 4919-4932
    • (1995) Biochemistry , vol.34 , pp. 4919-4932
    • Wingfield, P.T.1    Stahl, S.J.2    Williams, R.W.3    Steven, A.C.4
  • 12
    • 0029645618 scopus 로고
    • Evolutionary conservation in the hepatitis B virus core structure: Comparison of human and duck cores
    • Kenney, J. M., von Bonsdorff, C. H., Nassal, M., and Fuller, S. D. (1995) Evolutionary conservation in the hepatitis B virus core structure: Comparison of human and duck cores Structure 3, 1009-1019
    • (1995) Structure , vol.3 , pp. 1009-1019
    • Kenney, J.M.1    Von Bonsdorff, C.H.2    Nassal, M.3    Fuller, S.D.4
  • 13
    • 0029950758 scopus 로고    scopus 로고
    • Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein
    • Zlotnick, A., Cheng, N., Conway, J. F., Booy, F. P., Steven, A. C., Stahl, S. J., and Wingfield, P. T. (1996) Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein Biochemistry 35, 7412-7421
    • (1996) Biochemistry , vol.35 , pp. 7412-7421
    • Zlotnick, A.1    Cheng, N.2    Conway, J.F.3    Booy, F.P.4    Steven, A.C.5    Stahl, S.J.6    Wingfield, P.T.7
  • 14
    • 27744467626 scopus 로고    scopus 로고
    • Theoretical aspects of virus capsid assembly
    • Zlotnick, A. (2005) Theoretical aspects of virus capsid assembly J. Mol. Recognit. 18, 479-490
    • (2005) J. Mol. Recognit. , vol.18 , pp. 479-490
    • Zlotnick, A.1
  • 15
    • 33745787907 scopus 로고    scopus 로고
    • Dynamic Pathways for Viral Capsid Assembly
    • Hagan, M. F. and Chandler, D. (2006) Dynamic Pathways for Viral Capsid Assembly Biophys. J. 91, 42-54
    • (2006) Biophys. J. , vol.91 , pp. 42-54
    • Hagan, M.F.1    Chandler, D.2
  • 16
    • 61849163979 scopus 로고    scopus 로고
    • Thermodynamics of Virus Capsid Assembly
    • Katen, S. P. and Zlotnick, A. (2009) Thermodynamics of Virus Capsid Assembly Methods Enzymol. 455, 395-417
    • (2009) Methods Enzymol. , vol.455 , pp. 395-417
    • Katen, S.P.1    Zlotnick, A.2
  • 17
    • 0036786867 scopus 로고    scopus 로고
    • Weak protein-protein interactions are sufficient to drive assembly of hepatitis B virus capsids
    • Ceres, P. and Zlotnick, A. (2002) Weak protein-protein interactions are sufficient to drive assembly of hepatitis B virus capsids Biochemistry 41, 11525-11531
    • (2002) Biochemistry , vol.41 , pp. 11525-11531
    • Ceres, P.1    Zlotnick, A.2
  • 19
    • 0026793044 scopus 로고
    • The structure of hepadnaviral core antigens. Identification of free thiols and determination of the disulfide bonding pattern
    • Zheng, J., Schodel, F., and Peterson, D. (1992) The structure of hepadnaviral core antigens. Identification of free thiols and determination of the disulfide bonding pattern J. Biol. Chem. 267, 9422-9429
    • (1992) J. Biol. Chem. , vol.267 , pp. 9422-9429
    • Zheng, J.1    Schodel, F.2    Peterson, D.3
  • 20
    • 0024474088 scopus 로고
    • A recombinant hepatitis B core antigen polypeptide with the protamine-like domain deleted self-assembles into capsid particles but fails to bind nucleic acids
    • Gallina, A., Bonelli, F., Zentilin, L., Rindi, G., Muttini, M., and Milanesi, G. (1989) A recombinant hepatitis B core antigen polypeptide with the protamine-like domain deleted self-assembles into capsid particles but fails to bind nucleic acids J. Virol. 63, 4645-4652
    • (1989) J. Virol. , vol.63 , pp. 4645-4652
    • Gallina, A.1    Bonelli, F.2    Zentilin, L.3    Rindi, G.4    Muttini, M.5    Milanesi, G.6
  • 21
    • 84883616701 scopus 로고    scopus 로고
    • 3.5Å cryoEM structure of hepatitis B virus core assembled from full-length core protein
    • Yu, X., Jin, L., Jih, J., Shih, C., and Zhou, Z. H. (2013) 3.5Å cryoEM structure of hepatitis B virus core assembled from full-length core protein PLoS One 8, e69729
    • (2013) PLoS One , vol.8 , pp. 69729
    • Yu, X.1    Jin, L.2    Jih, J.3    Shih, C.4    Zhou, Z.H.5
  • 22
    • 0036242046 scopus 로고    scopus 로고
    • A small molecule inhibits and misdirects assembly of hepatitis B virus capsids
    • Zlotnick, A., Ceres, P., Singh, S., and Johnson, J. M. (2002) A small molecule inhibits and misdirects assembly of hepatitis B virus capsids J. Virol. 76, 4848-4854
    • (2002) J. Virol. , vol.76 , pp. 4848-4854
    • Zlotnick, A.1    Ceres, P.2    Singh, S.3    Johnson, J.M.4
  • 23
    • 77949633781 scopus 로고    scopus 로고
    • Understanding the concentration dependence of viral capsid assembly kinetics: The origin of the lag time and identifying the critical nucleus size
    • Hagan, M. F. and Elrad, O. M. (2010) Understanding the concentration dependence of viral capsid assembly kinetics: The origin of the lag time and identifying the critical nucleus size Biophys. J. 98, 1065-1074
    • (2010) Biophys. J. , vol.98 , pp. 1065-1074
    • Hagan, M.F.1    Elrad, O.M.2
  • 24
    • 0001598395 scopus 로고
    • The isomeric transformation of urea into ammonium cyanate in aqueous solutions
    • Dirnhuber, P. and Schutz, F. (1948) The isomeric transformation of urea into ammonium cyanate in aqueous solutions Biochem. J. 42, 628-632
    • (1948) Biochem. J. , vol.42 , pp. 628-632
    • Dirnhuber, P.1    Schutz, F.2
  • 25
    • 84872128220 scopus 로고    scopus 로고
    • One protein, at least three structures, and many functions
    • Zlotnick, A., Tan, Z., and Selzer, L. (2013) One protein, at least three structures, and many functions Structure 21, 6-8
    • (2013) Structure , vol.21 , pp. 6-8
    • Zlotnick, A.1    Tan, Z.2    Selzer, L.3
  • 26
    • 0031064380 scopus 로고    scopus 로고
    • Probing protein folding and stability using disulfide bonds
    • Darby, N. and Creighton, T. E. (1997) Probing protein folding and stability using disulfide bonds Mol. Biotechnol. 7, 57-77
    • (1997) Mol. Biotechnol. , vol.7 , pp. 57-77
    • Darby, N.1    Creighton, T.E.2
  • 27
    • 0141834247 scopus 로고    scopus 로고
    • Subtype-independent immature secretion and subtype-dependent replication deficiency of a highly frequent, naturally occurring mutation of human hepatitis B virus core antigen
    • Yuan, T. T., Tai, P. C., and Shih, C. (1999) Subtype-independent immature secretion and subtype-dependent replication deficiency of a highly frequent, naturally occurring mutation of human hepatitis B virus core antigen J. Virol. 73, 10122-10128
    • (1999) J. Virol. , vol.73 , pp. 10122-10128
    • Yuan, T.T.1    Tai, P.C.2    Shih, C.3
  • 28
    • 0033064976 scopus 로고    scopus 로고
    • The mechanism of an immature secretion phenotype of a highly frequent naturally occurring missense mutation at codon 97 of human hepatitis B virus core antigen
    • Yuan, T. T., Sahu, G. K., Whitehead, W. E., Greenberg, R., and Shih, C. (1999) The mechanism of an immature secretion phenotype of a highly frequent naturally occurring missense mutation at codon 97 of human hepatitis B virus core antigen J. Virol. 73, 5731-5740
    • (1999) J. Virol. , vol.73 , pp. 5731-5740
    • Yuan, T.T.1    Sahu, G.K.2    Whitehead, W.E.3    Greenberg, R.4    Shih, C.5
  • 29
    • 4143143115 scopus 로고    scopus 로고
    • Hepatitis B Virus Capsid Assembly is Enhanced by Naturally Occurring Mutation F97L
    • Ceres, P., Stray, S. J., and Zlotnick, A. (2004) Hepatitis B Virus Capsid Assembly is Enhanced by Naturally Occurring Mutation F97L J. Virol. 78, 9538-9543
    • (2004) J. Virol. , vol.78 , pp. 9538-9543
    • Ceres, P.1    Stray, S.J.2    Zlotnick, A.3
  • 30
    • 33846285185 scopus 로고    scopus 로고
    • Distinguishing reversible from irreversible virus capsid assembly
    • Zlotnick, A. (2007) Distinguishing reversible from irreversible virus capsid assembly J. Mol. Biol. 366, 14-18
    • (2007) J. Mol. Biol. , vol.366 , pp. 14-18
    • Zlotnick, A.1
  • 31
    • 84874031889 scopus 로고    scopus 로고
    • Phase diagrams map the properties of antiviral agents directed against hepatitis B virus core assembly
    • Li, L., Chirapu, S. R., Finn, M. G., and Zlotnick, A. (2013) Phase diagrams map the properties of antiviral agents directed against hepatitis B virus core assembly Antimicrob. Agents Chemother. 57, 1505-1508
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 1505-1508
    • Li, L.1    Chirapu, S.R.2    Finn, M.G.3    Zlotnick, A.4
  • 32
    • 0037705348 scopus 로고    scopus 로고
    • Observed hysteresis of virus capsid disassembly is implicit in kinetic models of assembly
    • Singh, S. and Zlotnick, A. (2003) Observed hysteresis of virus capsid disassembly is implicit in kinetic models of assembly J. Biol. Chem. 278, 18249-18255
    • (2003) J. Biol. Chem. , vol.278 , pp. 18249-18255
    • Singh, S.1    Zlotnick, A.2
  • 34
    • 0027264123 scopus 로고
    • An intramolecular disulfide bridge between Cys-7 and Cys-61 determines the structure of the secretory core gene product (e antigen) of hepatitis B virus
    • Nassal, M. and Rieger, A. (1993) An intramolecular disulfide bridge between Cys-7 and Cys-61 determines the structure of the secretory core gene product (e antigen) of hepatitis B virus J. Virol. 67, 4307-4315
    • (1993) J. Virol. , vol.67 , pp. 4307-4315
    • Nassal, M.1    Rieger, A.2
  • 35
    • 84904171369 scopus 로고    scopus 로고
    • Assessment of differences in the conformational flexibility of hepatitis B virus core-antigen and e-antigen by hydrogen deuterium exchange-mass spectrometry
    • Bereszczak, J. Z., Watts, N. R., Wingfield, P. T., Steven, A. C., and Heck, A. J. (2014) Assessment of differences in the conformational flexibility of hepatitis B virus core-antigen and e-antigen by hydrogen deuterium exchange-mass spectrometry Protein Sci. 23, 884-896
    • (2014) Protein Sci. , vol.23 , pp. 884-896
    • Bereszczak, J.Z.1    Watts, N.R.2    Wingfield, P.T.3    Steven, A.C.4    Heck, A.J.5
  • 37
    • 0029619776 scopus 로고
    • A novel basis of capsid stabilization by antiviral compounds
    • Phelps, D. K. and Post, C. B. (1995) A novel basis of capsid stabilization by antiviral compounds J. Mol. Biol. 254, 544-551
    • (1995) J. Mol. Biol. , vol.254 , pp. 544-551
    • Phelps, D.K.1    Post, C.B.2
  • 38
    • 0034681288 scopus 로고    scopus 로고
    • Stabilization of poliovirus by capsid-binding antiviral drugs is due to entropic effects
    • Tsang, S. K., Danthi, P., Chow, M., and Hogle, J. M. (2000) Stabilization of poliovirus by capsid-binding antiviral drugs is due to entropic effects J. Mol. Biol. 296, 335-340
    • (2000) J. Mol. Biol. , vol.296 , pp. 335-340
    • Tsang, S.K.1    Danthi, P.2    Chow, M.3    Hogle, J.M.4
  • 39
    • 0035138090 scopus 로고    scopus 로고
    • Molecular dynamics simulations of human rhinovirus and an antiviral compound
    • Speelman, B., Brooks, B. R., and Post, C. B. (2001) Molecular dynamics simulations of human rhinovirus and an antiviral compound Biophys. J. 80, 121-129
    • (2001) Biophys. J. , vol.80 , pp. 121-129
    • Speelman, B.1    Brooks, B.R.2    Post, C.B.3
  • 40
    • 84861836672 scopus 로고    scopus 로고
    • Differential assembly of hepatitis B virus core protein on single- and double-stranded nucleic acid suggest the dsDNA-filled core is spring-loaded
    • Dhason, M. S., Wang, J. C., Hagan, M. F., and Zlotnick, A. (2012) Differential assembly of hepatitis B virus core protein on single- and double-stranded nucleic acid suggest the dsDNA-filled core is spring-loaded Virology 430, 20-29
    • (2012) Virology , vol.430 , pp. 20-29
    • Dhason, M.S.1    Wang, J.C.2    Hagan, M.F.3    Zlotnick, A.4
  • 41
    • 84891552006 scopus 로고    scopus 로고
    • Maturation-associated destabilization of hepatitis B virus nucleocapsid
    • Cui, X., Ludgate, L., Ning, X., and Hu, J. (2013) Maturation-associated destabilization of hepatitis B virus nucleocapsid J. Virol. 87, 11494-11503
    • (2013) J. Virol. , vol.87 , pp. 11494-11503
    • Cui, X.1    Ludgate, L.2    Ning, X.3    Hu, J.4
  • 42
    • 0017618185 scopus 로고
    • Immunochemistry and polypeptide composition of hepatitis B core antigen (HBc Ag)
    • Budkowska, A., Shih, J. W., and Gerin, J. L. (1977) Immunochemistry and polypeptide composition of hepatitis B core antigen (HBc Ag) J. Immunol. 118, 1300-1305
    • (1977) J. Immunol. , vol.118 , pp. 1300-1305
    • Budkowska, A.1    Shih, J.W.2    Gerin, J.L.3
  • 43
    • 0025886356 scopus 로고
    • Differential formation of disulfide linkages in the core antigen of extracellular and intracellular hepatitis B virus core particles
    • Jeng, K. S., Hu, C. P., and Chang, C. M. (1991) Differential formation of disulfide linkages in the core antigen of extracellular and intracellular hepatitis B virus core particles J. Virol. 65, 3924-3927
    • (1991) J. Virol. , vol.65 , pp. 3924-3927
    • Jeng, K.S.1    Hu, C.P.2    Chang, C.M.3
  • 44
    • 0032862596 scopus 로고    scopus 로고
    • Hepatitis B viral core proteins with an N-terminal extension can assemble into core-like particles but cannot be enveloped
    • Hui, E. K., Yi, Y. S., and Lo, S. J. (1999) Hepatitis B viral core proteins with an N-terminal extension can assemble into core-like particles but cannot be enveloped J. Gen. Virol. 80 (Part 10) 2647-2659
    • (1999) J. Gen. Virol. , vol.80 , Issue.PART 10 , pp. 2647-2659
    • Hui, E.K.1    Yi, Y.S.2    Lo, S.J.3
  • 45
    • 0026793651 scopus 로고
    • Conserved cysteines of the hepatitis B virus core protein are not required for assembly of replication-competent core particles nor for their envelopment
    • Nassal, M. (1992) Conserved cysteines of the hepatitis B virus core protein are not required for assembly of replication-competent core particles nor for their envelopment Virology 190, 499-505
    • (1992) Virology , vol.190 , pp. 499-505
    • Nassal, M.1
  • 46
    • 0026787311 scopus 로고
    • Cys residues of the hepatitis B virus capsid protein are not essential for the assembly of viral core particles but can influence their stability
    • Zhou, S. and Standring, D. N. (1992) Cys residues of the hepatitis B virus capsid protein are not essential for the assembly of viral core particles but can influence their stability J. Virol. 66, 5393-5398
    • (1992) J. Virol. , vol.66 , pp. 5393-5398
    • Zhou, S.1    Standring, D.N.2


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