메뉴 건너뛰기




Volumn 334, Issue 1, 2005, Pages 17-27

Maturation of a tetravirus capsid alters the dynamic properties and creates a metastable complex

Author keywords

Capsid; Dynamics; FTIR; Helicoverpa; Mass spectrometry; Metastable; Nudaurelia; Supramolecular; Tetravirus

Indexed keywords

PROTEIN SUBUNIT;

EID: 14644438331     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virol.2005.01.017     Document Type: Article
Times cited : (35)

References (42)
  • 1
    • 0028906644 scopus 로고
    • Assembly of the T = 4 Nudaurelia capensis omega virus capsid protein, post-translational cleavage, and specific encapsidation of its mRNA in a baculovirus expression system
    • D.K. Agrawal, and J.E. Johnson Assembly of the T = 4 Nudaurelia capensis omega virus capsid protein, post-translational cleavage, and specific encapsidation of its mRNA in a baculovirus expression system Virology 207 1995 89 97
    • (1995) Virology , vol.207 , pp. 89-97
    • Agrawal, D.K.1    Johnson, J.E.2
  • 2
    • 0031985001 scopus 로고    scopus 로고
    • Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry
    • B. Bothner, X.F. Dong, L. Bibbs, J.E. Johnson, and G. Siuzdak Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry J. Biol. Chem. 273 2 1998 673 676
    • (1998) J. Biol. Chem. , vol.273 , Issue.2 , pp. 673-676
    • Bothner, B.1    Dong, X.F.2    Bibbs, L.3    Johnson, J.E.4    Siuzdak, G.5
  • 5
    • 0034625320 scopus 로고    scopus 로고
    • Large conformational changes in the maturation of a simple RNA virus, Nudaurelia capensis ω (NωV)
    • M.A. Canady, M. Tihova, T.N. Hanzlik, J.E. Johnson, and M. Yeager Large conformational changes in the maturation of a simple RNA virus, Nudaurelia capensis ω (NωV) J. Mol. Biol. 299 2000 573 584
    • (2000) J. Mol. Biol. , vol.299 , pp. 573-584
    • Canady, M.A.1    Tihova, M.2    Hanzlik, T.N.3    Johnson, J.E.4    Yeager, M.5
  • 6
    • 0035943387 scopus 로고    scopus 로고
    • Analysis of rapid, large-scale protein quaternary structural changes: Time-resolved X-ray solution scattering of Nudaurelia capensis ω (NωV) maturation
    • M.A. Canady, H. Tsuruta, and J.E. Johnson Analysis of rapid, large-scale protein quaternary structural changes: time-resolved X-ray solution scattering of Nudaurelia capensis ω (NωV) maturation J. Mol. Biol. 311 2001 803 814
    • (2001) J. Mol. Biol. , vol.311 , pp. 803-814
    • Canady, M.A.1    Tsuruta, H.2    Johnson, J.E.3
  • 7
    • 0023693897 scopus 로고
    • Structural and conformational changes of beta-lactoglobulin B: An infrared spectroscopic study of the effect of pH and temperature
    • H.L. Casal, U. Kohler, and H.H. Mantsch Structural and conformational changes of beta-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature Biochim. Biophys. Acta 957 1988 11 20
    • (1988) Biochim. Biophys. Acta , vol.957 , pp. 11-20
    • Casal, H.L.1    Kohler, U.2    Mantsch, H.H.3
  • 9
    • 0028773272 scopus 로고
    • Functional implications of quasi-equivalence in a T = 3 icosahedral animal virus established by cryo-electron microscopy and X-ray crystallography
    • R.H. Cheng, V.S. Reddy, N.H. Olsen, A.J. Fisher, T.S. Baker, and J.E. Johnson Functional implications of quasi-equivalence in a T = 3 icosahedral animal virus established by cryo-electron microscopy and X-ray crystallography Structure 2 1994 271 282
    • (1994) Structure , vol.2 , pp. 271-282
    • Cheng, R.H.1    Reddy, V.S.2    Olsen, N.H.3    Fisher, A.J.4    Baker, T.S.5    Johnson, J.E.6
  • 10
    • 0029004044 scopus 로고
    • Probing the solution structure of the DNA-binding protein Max by a combination of proteolysis and mass spectrometry
    • S.L. Cohen, A.R. Ferre-D'Amare, S.K. Burely, and B.T. Chait Probing the solution structure of the DNA-binding protein Max by a combination of proteolysis and mass spectrometry Protein Sci. 6 1995 1088 1099
    • (1995) Protein Sci. , vol.6 , pp. 1088-1099
    • Cohen, S.L.1    Ferre-D'Amare, A.R.2    Burely, S.K.3    Chait, B.T.4
  • 12
    • 0017685815 scopus 로고
    • Studies on the in vitro uncoating of poliovirus: II. Characteristics of the membrane-modified particle
    • J. De Sena, and B. Mandel Studies on the in vitro uncoating of poliovirus: II. Characteristics of the membrane-modified particle Virology 78 1977 554 566
    • (1977) Virology , vol.78 , pp. 554-566
    • De Sena, J.1    Mandel, B.2
  • 13
    • 0023055086 scopus 로고
    • Correlation between sites of limited proteolysis and segmental mobility in thermolysin
    • A. Fontana, G. Fassina, C. Vita, D. Dalzoppo, M. Zamai, and M. Zambonin Correlation between sites of limited proteolysis and segmental mobility in thermolysin Biochemistry 25 1986 1847 1851
    • (1986) Biochemistry , vol.25 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzoppo, D.4    Zamai, M.5    Zambonin, M.6
  • 14
    • 0000091801 scopus 로고
    • Early interactions between poliovirus and ERK cells. Some observation on the nature and significance of the rejected particles
    • M.L. Fenwick, and P.D. Cooper Early interactions between poliovirus and ERK cells. Some observation on the nature and significance of the rejected particles Virology 15 1962 212 223
    • (1962) Virology , vol.15 , pp. 212-223
    • Fenwick, M.L.1    Cooper, P.D.2
  • 15
    • 0025273268 scopus 로고
    • Cell-induced conformational change in poliovirus: Externalization of the amino terminus of VP1 is responsible for liposome binding
    • C.E. Fricks, and J.M. Hogle Cell-induced conformational change in poliovirus: externalization of the amino terminus of VP1 is responsible for liposome binding J. Virol. 64 1990 1934 1945
    • (1990) J. Virol. , vol.64 , pp. 1934-1945
    • Fricks, C.E.1    Hogle, J.M.2
  • 16
    • 1242319463 scopus 로고    scopus 로고
    • The refined structure of Nudaurelia capensis omega virus reveals control elements for a T = 4 capsid maturation
    • C. Helgstrand, S. Munshi, J.E. Johnson, and L. Liljas The refined structure of Nudaurelia capensis omega virus reveals control elements for a T = 4 capsid maturation Virology 318 2004 192 203
    • (2004) Virology , vol.318 , pp. 192-203
    • Helgstrand, C.1    Munshi, S.2    Johnson, J.E.3    Liljas, L.4
  • 17
    • 0036403802 scopus 로고    scopus 로고
    • Poliovirus cell entry: Common structural themes in viral cell entry pathways
    • J.H. Hogle Poliovirus cell entry: common structural themes in viral cell entry pathways Annu. Rev. Microbiol. 56 2002 777 802
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 777-802
    • Hogle, J.H.1
  • 18
    • 0033608952 scopus 로고    scopus 로고
    • An animal virus-derived peptide switches membrane morphology: Possible relevance to nodaviral transfection processes
    • A. Janshoff, D.T. Bong, C. Steinem, J.E. Johnson, and M.R. Ghadiri An animal virus-derived peptide switches membrane morphology: possible relevance to nodaviral transfection processes Biochemistry 38 1999 5328 5336
    • (1999) Biochemistry , vol.38 , pp. 5328-5336
    • Janshoff, A.1    Bong, D.T.2    Steinem, C.3    Johnson, J.E.4    Ghadiri, M.R.5
  • 19
    • 0041324572 scopus 로고    scopus 로고
    • Virus particle dynamics
    • J.E. Johnson Virus particle dynamics Adv. Protein Chem. 64 2003 197 218
    • (2003) Adv. Protein Chem. , vol.64 , pp. 197-218
    • Johnson, J.E.1
  • 20
    • 0000108907 scopus 로고
    • The adsorption and early fate of purified poliovirus in HeLA cells
    • W.K. Joklik, and J.E. Darnell The adsorption and early fate of purified poliovirus in HeLA cells Virology 13 1961 439 447
    • (1961) Virology , vol.13 , pp. 439-447
    • Joklik, W.K.1    Darnell, J.E.2
  • 21
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • S. Krimm, and J. Bandekar Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins Adv. Protein Chem. 38 1986 181 364
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 22
    • 0029982559 scopus 로고    scopus 로고
    • Probing protein/protein interactions with mass spectrometry and isotopic labeling: Analysis of the p21/Cdk2 complex
    • R.W. Kriwacki, J. Wu, G. Siuzdak, and P.E. Wright Probing protein/protein interactions with mass spectrometry and isotopic labeling: analysis of the p21/Cdk2 complex J. Am. Chem. Soc. 118 1996 5320 5321
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5320-5321
    • Kriwacki, R.W.1    Wu, J.2    Siuzdak, G.3    Wright, P.E.4
  • 23
    • 2942691397 scopus 로고    scopus 로고
    • Small compounds targeted to subunit interfaces arrest maturation in a nonenveloped, icosahedral animal virus
    • K.K. Lee, J. Tang, D. Taylor, B. Bothner, and J.E. Johnson Small compounds targeted to subunit interfaces arrest maturation in a nonenveloped, icosahedral animal virus J. Virol. 78 2004 7208 7216
    • (2004) J. Virol. , vol.78 , pp. 7208-7216
    • Lee, K.K.1    Tang, J.2    Taylor, D.3    Bothner, B.4    Johnson, J.E.5
  • 25
    • 0028341259 scopus 로고
    • Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature
    • Q. Li, A.G. Yafal, Y.M.-H. Lee, J. Hogle, and M. Chow Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature J. Virol. 68 1994 3965 3970
    • (1994) J. Virol. , vol.68 , pp. 3965-3970
    • Li, Q.1    Yafal, A.G.2    Lee, Y.M.-H.3    Hogle, J.4    Chow, M.5
  • 26
    • 0037764817 scopus 로고    scopus 로고
    • Pseudo-atomic models of swollen CCMV from cryo-electron microscopy data
    • H. Liu, C. Qu, J.E. Johnson, and D.A. Case Pseudo-atomic models of swollen CCMV from cryo-electron microscopy data J. Struct. Biol. 142 2003 356 363
    • (2003) J. Struct. Biol. , vol.142 , pp. 356-363
    • Liu, H.1    Qu, C.2    Johnson, J.E.3    Case, D.A.4
  • 27
    • 0028186730 scopus 로고
    • Use of drug-resistance mutants to identify functional regions in picornavirus capsid proteins
    • A.G. Mosser, D.A. Shepard, and R.R. Rueckert Use of drug-resistance mutants to identify functional regions in picornavirus capsid proteins Arch. Virol., Suppl. 9 1994 111 119
    • (1994) Arch. Virol., Suppl. , vol.9 , pp. 111-119
    • Mosser, A.G.1    Shepard, D.A.2    Rueckert, R.R.3
  • 28
    • 0030576341 scopus 로고    scopus 로고
    • The 2.8 a structure of a T = 4 animal virus and its implications for membrane translocation of RNA
    • S. Munshi, L. Lijas, J. Cavarelli, W. Bomu, B. McKinney, V. Reddy, and J.E. Johnson The 2.8 A structure of a T = 4 animal virus and its implications for membrane translocation of RNA J. Mol. Biol. 261 1996 1 10
    • (1996) J. Mol. Biol. , vol.261 , pp. 1-10
    • Munshi, S.1    Lijas, L.2    Cavarelli, J.3    Bomu, W.4    McKinney, B.5    Reddy, V.6    Johnson, J.E.7
  • 30
    • 0029619776 scopus 로고
    • A novel basis for capsid stabilization by antiviral compounds
    • D.K. Phelps, and C.B. Post A novel basis for capsid stabilization by antiviral compounds J. Mol. Biol. 254 1995 544 551
    • (1995) J. Mol. Biol. , vol.254 , pp. 544-551
    • Phelps, D.K.1    Post, C.B.2
  • 32
    • 0032007554 scopus 로고    scopus 로고
    • Inhibiting virus-capsid assembly by altering the polymerisation pathway
    • P.E. Prevelige Jr. Inhibiting virus-capsid assembly by altering the polymerisation pathway Trends Biotechnol. 16 1998 61 65
    • (1998) Trends Biotechnol. , vol.16 , pp. 61-65
    • Prevelige Jr., P.E.1
  • 35
    • 0033989157 scopus 로고    scopus 로고
    • Illuminating folding intermediates
    • C.P. Schultz Illuminating folding intermediates Nat. Struct. Biol. 7 2000 7 10
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 7-10
    • Schultz, C.P.1
  • 36
    • 0036776532 scopus 로고    scopus 로고
    • Large-scale, pH-dependent, quaternary structure changes in an RNA virus capsid are reversible in the absence of subunit autoproteolysis
    • D. Taylor, N.K. Krishna, M.A. Candy, A. Scheenmann, and J.E. Johnson Large-scale, pH-dependent, quaternary structure changes in an RNA virus capsid are reversible in the absence of subunit autoproteolysis J. Virol. 76 2002 9972 9980
    • (2002) J. Virol. , vol.76 , pp. 9972-9980
    • Taylor, D.1    Krishna, N.K.2    Candy, M.A.3    Scheenmann, A.4    Johnson, J.E.5
  • 37
    • 0344099412 scopus 로고    scopus 로고
    • Correlation of chemical reactivity of Nudaurelia capensis omega virus with a pH-induced conformational change
    • D. Taylor, Q. Wang, B. Bothner, P. Natarajan, M.G. Finn, and J.E. Johnson Correlation of chemical reactivity of Nudaurelia capensis omega virus with a pH-induced conformational change Chem. Commun. (Cambridge) 22 2003 2770 2771
    • (2003) Chem. Commun. (Cambridge) , vol.22 , pp. 2770-2771
    • Taylor, D.1    Wang, Q.2    Bothner, B.3    Natarajan, P.4    Finn, M.G.5    Johnson, J.E.6
  • 38
    • 0027364215 scopus 로고
    • Inhibition of viral capsid assembly by 1,1′-bi(4- anilinonaphthalene-5-sulfonic acid)
    • C.M. Teschke, J. King, and P.E. Prevelige Jr. Inhibition of viral capsid assembly by 1,1′-bi(4-anilinonaphthalene-5-sulfonic acid) Biochemistry 32 1993 10658 10665
    • (1993) Biochemistry , vol.32 , pp. 10658-10665
    • Teschke, C.M.1    King, J.2    Prevelige Jr., P.E.3
  • 39
    • 0023042762 scopus 로고
    • Role of the N-terminal part of the coat protein in the assembly of cowpea chlorotic mottle virus. A 500 MHz proton nuclear magnetic resonance study and structural calculations
    • G. Vriend, B.J. Verduin, and M.A. Hemminga Role of the N-terminal part of the coat protein in the assembly of cowpea chlorotic mottle virus. A 500 MHz proton nuclear magnetic resonance study and structural calculations J. Mol. Biol. 191 1986 453 460
    • (1986) J. Mol. Biol. , vol.191 , pp. 453-460
    • Vriend, G.1    Verduin, B.J.2    Hemminga, M.A.3
  • 40
    • 0035558423 scopus 로고    scopus 로고
    • Structural dynamics, an intrinsic property of viral capsids
    • J. Witz, and F. Brown Structural dynamics, an intrinsic property of viral capsids Arch. Virol. 146 2001 2263 2274
    • (2001) Arch. Virol. , vol.146 , pp. 2263-2274
    • Witz, J.1    Brown, F.2
  • 41
    • 0036242046 scopus 로고    scopus 로고
    • A small molecule inhibits and misdirects assembly of hepatitis B virus capsids
    • A.P. Zlotnick, P. Ceres, S. Singh, and J.M. Johnson A small molecule inhibits and misdirects assembly of hepatitis B virus capsids J. Virol. 76 2002 4848 4854
    • (2002) J. Virol. , vol.76 , pp. 4848-4854
    • Zlotnick, A.P.1    Ceres, P.2    Singh, S.3    Johnson, J.M.4
  • 42
    • 0034834580 scopus 로고    scopus 로고
    • Preparation and characterization of purified amyloid fibrils
    • J. Zurdo, J.I. Guijarro, and C.M. Dobson Preparation and characterization of purified amyloid fibrils J. Am. Chem. Soc. 123 2001 8141 8142
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8141-8142
    • Zurdo, J.1    Guijarro, J.I.2    Dobson, C.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.