메뉴 건너뛰기




Volumn 105, Issue 27, 2008, Pages 9216-9220

High-resolution mass spectrometry of viral assemblies: Molecular composition and stability of dimorphic hepatitis B virus capsids

Author keywords

Atomic force microscopy; Collision induced dissociation; Macromolecular mass spectrometry; Viral structural biology; Virus assembly

Indexed keywords

ACCURACY; ARTICLE; ATOMIC FORCE MICROSCOPY; CONTROLLED STUDY; HEPATITIS B VIRUS; MASS SPECTROMETRY; MOLECULAR BIOLOGY; MOLECULAR WEIGHT; NANOTECHNOLOGY; NONHUMAN; PRIORITY JOURNAL; VIRUS CAPSID; VIRUS MORPHOLOGY; YOUNG MODULUS;

EID: 48249109172     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0800406105     Document Type: Article
Times cited : (188)

References (41)
  • 1
    • 0030740450 scopus 로고    scopus 로고
    • Hepatitis B virus, the vaccine, and the control of primary cancer of the liver
    • Blumberg BS (1997) Hepatitis B virus, the vaccine, and the control of primary cancer of the liver. Proc Natl Acad Sci USA 94:7121-7125.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7121-7125
    • Blumberg, B.S.1
  • 2
    • 0347928672 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus replication by drug-induced depletion of nucleocapsids
    • Deres K, et al. (2003) Inhibition of hepatitis B virus replication by drug-induced depletion of nucleocapsids. Science 299:893-896.
    • (2003) Science , vol.299 , pp. 893-896
    • Deres, K.1
  • 5
    • 26944499478 scopus 로고    scopus 로고
    • Structure, assembly, and antigenicity of hepatitis B virus capsid proteins
    • Steven AC, et al. (2005) Structure, assembly, and antigenicity of hepatitis B virus capsid proteins. Adv Virus Res 64:125-164.
    • (2005) Adv Virus Res , vol.64 , pp. 125-164
    • Steven, A.C.1
  • 6
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Caspar DL, Klug A (1962) Physical principles in the construction of regular viruses. Cold Spring Harb Symp Quant Biol 27:1-24.
    • (1962) Cold Spring Harb Symp Quant Biol , vol.27 , pp. 1-24
    • Caspar, D.L.1    Klug, A.2
  • 7
    • 0028307177 scopus 로고
    • Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy
    • Crowther RA, et al. (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
  • 8
    • 33745207098 scopus 로고    scopus 로고
    • Native hepatitis B virions and capsids visualized by electron cryomicroscopy
    • Dryden KA, et al. (2006) Native hepatitis B virions and capsids visualized by electron cryomicroscopy. Mol Cell 22:843-850.
    • (2006) Mol Cell , vol.22 , pp. 843-850
    • Dryden, K.A.1
  • 9
    • 0029645618 scopus 로고
    • Evolutionary conservation in the hepatitis B virus core structure: Comparison of human and duck cores
    • Kenney JM, von Bonsdorff CH, Nassal M, Fuller SD (1995) Evolutionary conservation in the hepatitis B virus core structure: Comparison of human and duck cores. Structure (London) 3:1009-1019.
    • (1995) Structure (London) , vol.3 , pp. 1009-1019
    • Kenney, J.M.1    von Bonsdorff, C.H.2    Nassal, M.3    Fuller, S.D.4
  • 10
    • 0028953769 scopus 로고
    • Hepatitis core antigen produced in Escherichia coli: Subunit composition, conformational analysis, and in vitro capsid assembly
    • Wingfield PT, Stahl SJ, Williams RW, Steven AC (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
  • 11
    • 0036500146 scopus 로고    scopus 로고
    • The morphogenic linker peptide of HBV capsid protein forms a mobile array on the interior surface
    • Watts NR, et al. (2002) The morphogenic linker peptide of HBV capsid protein forms a mobile array on the interior surface. EMBO J 21:876-884.
    • (2002) EMBO J , vol.21 , pp. 876-884
    • Watts, N.R.1
  • 12
    • 0029950758 scopus 로고    scopus 로고
    • Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein
    • Zlotnick A, et al. (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
  • 13
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Böttcher B, Wynne SA, Crowther RA (1997) Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 386:88-91.
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 14
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway JF, et al. (1997) Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature 386:91-94.
    • (1997) Nature , vol.386 , pp. 91-94
    • Conway, J.F.1
  • 15
    • 0033152857 scopus 로고    scopus 로고
    • The crystal structure of the human hepatitis B virus capsid
    • Wynne SA, Crowther RA, Leslie AG (1999) The crystal structure of the human hepatitis B virus capsid. Mol Cell 3:771-780.
    • (1999) Mol Cell , vol.3 , pp. 771-780
    • Wynne, S.A.1    Crowther, R.A.2    Leslie, A.G.3
  • 16
    • 0036786867 scopus 로고    scopus 로고
    • Weak protein-protein interactions are sufficient to drive assembly of hepatitis B virus capsids
    • Ceres P, 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
  • 17
    • 2942662201 scopus 로고    scopus 로고
    • Competing hydrophobic and screened-coulomb interactions in hepatitis B virus capsid assembly
    • Kegel WK, Schoot Pv P (2004) Competing hydrophobic and screened-coulomb interactions in hepatitis B virus capsid assembly. Biophys J 86:3905-3913.
    • (2004) Biophys J , vol.86 , pp. 3905-3913
    • Kegel, W.K.1    Schoot, P.P.2
  • 18
    • 4444243006 scopus 로고    scopus 로고
    • Investigation of intact protein complexes by mass spectrometry
    • Heck AJ, Van Den Heuvel RH (2004) Investigation of intact protein complexes by mass spectrometry. Mass Spectrom Rev 23:368-389.
    • (2004) Mass Spectrom Rev , vol.23 , pp. 368-389
    • Heck, A.J.1    Van Den Heuvel, R.H.2
  • 19
    • 34548215681 scopus 로고    scopus 로고
    • Protein complexes in the gas phase: Technology for structural genomics and proteomics
    • Benesch JL, Ruotolo BT, Simmons DA, Robinson CV (2007) Protein complexes in the gas phase: Technology for structural genomics and proteomics. Chem Rev 107:3544-3567.
    • (2007) Chem Rev , vol.107 , pp. 3544-3567
    • Benesch, J.L.1    Ruotolo, B.T.2    Simmons, D.A.3    Robinson, C.V.4
  • 20
    • 35148816658 scopus 로고    scopus 로고
    • Structural biology of RNA polymerase III: Mass spectrometry elucidates subcomplex architecture
    • Lorenzen K, Vannini A, Cramer P, Heck AJ (2007) Structural biology of RNA polymerase III: Mass spectrometry elucidates subcomplex architecture. Structure (London) 15:1237-1245.
    • (2007) Structure (London) , vol.15 , pp. 1237-1245
    • Lorenzen, K.1    Vannini, A.2    Cramer, P.3    Heck, A.J.4
  • 22
    • 0035793266 scopus 로고    scopus 로고
    • Mass spectrometry of an intact virus
    • Fuerstenau SD, et al. (2001) Mass spectrometry of an intact virus. Angew Chem Int Ed Engl 40:542-544.
    • (2001) Angew Chem Int Ed Engl , vol.40 , pp. 542-544
    • Fuerstenau, S.D.1
  • 23
    • 0034639980 scopus 로고    scopus 로고
    • Electrospray time-of-flight mass spectrometry of the intact MS2 virus capsid
    • Tito MA, Tars K, Valegard K, Hajdu J, Robinson CV (2000) Electrospray time-of-flight mass spectrometry of the intact MS2 virus capsid. J Am Chem Soc 122:3550-3551.
    • (2000) J Am Chem Soc , vol.122 , pp. 3550-3551
    • Tito, M.A.1    Tars, K.2    Valegard, K.3    Hajdu, J.4    Robinson, C.V.5
  • 24
    • 33750696329 scopus 로고    scopus 로고
    • Improving the performance of a quadrupole time-of-flight instrument for macromolecular mass spectrometry
    • van den Heuvel RH, et al. (2006) Improving the performance of a quadrupole time-of-flight instrument for macromolecular mass spectrometry. Anal Chem 78:7473-7483.
    • (2006) Anal Chem , vol.78 , pp. 7473-7483
    • van den Heuvel, R.H.1
  • 25
    • 35148867690 scopus 로고    scopus 로고
    • Optimizing macromolecular tandem mass spectrometry of large non-covalent complexes using heavy collision gases
    • Lorenzen K, Versluis C, van Duijn E, van den Heuvel RHH, Heck AJR (2007) Optimizing macromolecular tandem mass spectrometry of large non-covalent complexes using heavy collision gases. Int J Mass Spectrom 268:198-206.
    • (2007) Int J Mass Spectrom , vol.268 , pp. 198-206
    • Lorenzen, K.1    Versluis, C.2    van Duijn, E.3    van den Heuvel, R.H.H.4    Heck, A.J.R.5
  • 26
    • 33646045893 scopus 로고    scopus 로고
    • Tandem mass spectrometry of intact GroEL-substrate complexes reveals substrate-specific conformational changes in the trans ring
    • van Duijn E, et al. (2006) Tandem mass spectrometry of intact GroEL-substrate complexes reveals substrate-specific conformational changes in the trans ring. J Am Chem Soc 128:4694-4702.
    • (2006) J Am Chem Soc , vol.128 , pp. 4694-4702
    • van Duijn, E.1
  • 27
    • 0033564930 scopus 로고    scopus 로고
    • Pentagon adjacency as a determinant of fullerene stability
    • Albertazzi E, et al. (1999) Pentagon adjacency as a determinant of fullerene stability. Phys Chem Chem Phys 1:2913-2918.
    • (1999) Phys Chem Chem Phys , vol.1 , pp. 2913-2918
    • Albertazzi, E.1
  • 28
    • 2442665377 scopus 로고    scopus 로고
    • Bacteriophage capsids: Tough nanoshells with complex elastic properties
    • Ivanovska IL, et al. (2004) Bacteriophage capsids: Tough nanoshells with complex elastic properties. Proc Natl Acad Sci USA 101:7600-7605.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7600-7605
    • Ivanovska, I.L.1
  • 29
    • 34250734534 scopus 로고    scopus 로고
    • Viral capsids: Mechanical characteristics, genome packaging and delivery mechanisms
    • Roos WH, Ivanovska IL, Evilevitch A, Wuite GJ (2007) Viral capsids: Mechanical characteristics, genome packaging and delivery mechanisms. Cell Mol Life Sci 64:1484-1497.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 1484-1497
    • Roos, W.H.1    Ivanovska, I.L.2    Evilevitch, A.3    Wuite, G.J.4
  • 31
    • 33847646319 scopus 로고    scopus 로고
    • Nonlinear finite-element analysis of nanoindentation of viral capsids
    • Gibbons MM, Klug WS (2007) Nonlinear finite-element analysis of nanoindentation of viral capsids. Phys Rev E Stat Nonlin Soft Matter Phys 75:031901.
    • (2007) Phys Rev E Stat Nonlin Soft Matter Phys , vol.75 , pp. 031901
    • Gibbons, M.M.1    Klug, W.S.2
  • 32
    • 0035029535 scopus 로고    scopus 로고
    • The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument
    • Tahallah N, Pinkse M, Maier CS, Heck AJ (2001) The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument. Rapid Commun Mass Spectrom 15:596-601.
    • (2001) Rapid Commun Mass Spectrom , vol.15 , pp. 596-601
    • Tahallah, N.1    Pinkse, M.2    Maier, C.S.3    Heck, A.J.4
  • 33
    • 18244396336 scopus 로고    scopus 로고
    • Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry
    • van Duijn E, et al. (2005) Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry. Nat Methods 2:371-376.
    • (2005) Nat Methods , vol.2 , pp. 371-376
    • van Duijn, E.1
  • 34
    • 33745192792 scopus 로고    scopus 로고
    • Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies
    • Benesch JL, Aquilina JA, Ruotolo BT, Sobott F, Robinson CV (2006) Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies. Chem Biol 13:597-605.
    • (2006) Chem Biol , vol.13 , pp. 597-605
    • Benesch, J.L.1    Aquilina, J.A.2    Ruotolo, B.T.3    Sobott, F.4    Robinson, C.V.5
  • 35
    • 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
  • 36
    • 19844373000 scopus 로고    scopus 로고
    • Control of virus assembly: HK97 "Whiffleball" mutant capsids without pentons
    • Li Y, et al. (2005) Control of virus assembly: HK97 "Whiffleball" mutant capsids without pentons. J Mol Biol 348:167-182.
    • (2005) J Mol Biol , vol.348 , pp. 167-182
    • Li, Y.1
  • 37
    • 33750844822 scopus 로고    scopus 로고
    • A free energy cascade with locks drives assembly and maturation of bacteriophage HK97 capsid
    • Ross PD, et al. (2006) A free energy cascade with locks drives assembly and maturation of bacteriophage HK97 capsid. J Mol Biol 364:512-525.
    • (2006) J Mol Biol , vol.364 , pp. 512-525
    • Ross, P.D.1
  • 38
    • 0033517792 scopus 로고    scopus 로고
    • A theoretical model successfully identifies features of hepatitis B virus capsid assembly
    • Zlotnick A, Johnson JM, Wingfield PW, Stahl SJ, Endres D (1999) A theoretical model successfully identifies features of hepatitis B virus capsid assembly. Biochemistry 38:14644-14652.
    • (1999) Biochemistry , vol.38 , pp. 14644-14652
    • Zlotnick, A.1    Johnson, J.M.2    Wingfield, P.W.3    Stahl, S.J.4    Endres, D.5
  • 39
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • Sobott F, Hernandez H, McCammon MG, Tito MA, Robinson CV (2002) A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies. Anal Chem 74:1402-1407.
    • (2002) Anal Chem , vol.74 , pp. 1402-1407
    • Sobott, F.1    Hernandez, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.5
  • 41
    • 0001155528 scopus 로고    scopus 로고
    • Calibration of rectangular atomic force microscope cantilevers
    • Sader JE, Chon JWM, Mulvaney P (1999) Calibration of rectangular atomic force microscope cantilevers. Rev Sci Instrum 70:3967-3969.
    • (1999) Rev Sci Instrum , vol.70 , pp. 3967-3969
    • Sader, J.E.1    Chon, J.W.M.2    Mulvaney, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.