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Volumn 21, Issue 18, 2002, Pages 4754-4762

Atomic model of the papillomavirus capsid

Author keywords

Disulfide bond; Electron microscopy; Papillomavirus; Vaccine design; Virus assembly

Indexed keywords

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL DIFFERENTIATION; COVALENT BOND; CRYSTAL STRUCTURE; DISULFIDE BOND; ELECTRON MICROSCOPY; IMAGE RECONSTRUCTION; IMMUNOGENICITY; MASS SPECTROMETRY; NONHUMAN; PAPILLOMA VIRUS; PRIORITY JOURNAL; VIRUS ASSEMBLY; VIRUS CAPSID; WART VIRUS;

EID: 0037119997     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf494     Document Type: Article
Times cited : (233)

References (33)
  • 1
    • 0026329210 scopus 로고
    • Structures of bovine and human papillomaviruses. Analysis by cryoelectron microscopy and three-dimensional image reconstruction
    • Baker, T.S., Newcomb, W.W., Olson, N.H., Cowsert, L.M., Olson, C. and Brown, J.C. (1991) Structures of bovine and human papillomaviruses. Analysis by cryoelectron microscopy and three-dimensional image reconstruction. Biophys. J., 60, 1445-1456.
    • (1991) Biophys. J , vol.60 , pp. 1445-1456
    • Baker, T.S.1    Newcomb, W.W.2    Olson, N.H.3    Cowsert, L.M.4    Olson, C.5    Brown, J.C.6
  • 3
    • 0032493679 scopus 로고    scopus 로고
    • Two antibodies that neutralize papillomavirus by different mechanisms show distinct binding patterns at 13 A resolution
    • Booy, F.P., Roden, R.B., Greenstone, H.L., Schiller, J.T. and Trus, B.L. (1998) Two antibodies that neutralize papillomavirus by different mechanisms show distinct binding patterns at 13 A resolution. J. Mol. Biol., 281, 95-106.
    • (1998) J. Mol. Biol , vol.281 , pp. 95-106
    • Booy, F.P.1    Roden, R.B.2    Greenstone, H.L.3    Schiller, J.T.4    Trus, B.L.5
  • 4
    • 0029041842 scopus 로고
    • Prevalence of human papillomavirus in cervical cancer: A worldwide perspective
    • International Biological Study on Cervical Cancer (IBSCC) Study Group
    • Bosch, F.X. et al. (1995) Prevalence of human papillomavirus in cervical cancer: a worldwide perspective. International Biological Study on Cervical Cancer (IBSCC) Study Group. J. Natl Cancer Inst., 87, 796-806.
    • (1995) J. Natl Cancer Inst , vol.87 , pp. 796-806
    • Bosch, F.X.1
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D, 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 6
    • 0033696899 scopus 로고    scopus 로고
    • Structure of small virus-like particles assembled from the L1 protein of human papillomavirus 16
    • Chen, X.S., Garcea, R.L., Goldberg, I., Casini, G. and Harrison, S.C. (2000) Structure of small virus-like particles assembled from the L1 protein of human papillomavirus 16. Mol. Cell, 5, 557-567.
    • (2000) Mol. Cell , vol.5 , pp. 557-567
    • Chen, X.S.1    Garcea, R.L.2    Goldberg, I.3    Casini, G.4    Harrison, S.C.5
  • 7
    • 0035896012 scopus 로고    scopus 로고
    • Papillomavirus capsid protein expression in Escherichia coli: Purification and assembly of HPV11 and HPV16 L1
    • Chen, X.S., Casini, G., Harrison, S.C. and Garcea, R.L. (2001) Papillomavirus capsid protein expression in Escherichia coli: purification and assembly of HPV11 and HPV16 L1. J. Mol. Biol., 307, 173-182.
    • (2001) J. Mol. Biol , vol.307 , pp. 173-182
    • Chen, X.S.1    Casini, G.2    Harrison, S.C.3    Garcea, R.L.4
  • 9
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J., McCormack, A. and Yates, J.R. (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom., 5, 1579-1583.
    • (1994) J. Am. Soc. Mass Spectrom , vol.5 , pp. 1579-1583
    • Eng, J.1    McCormack, A.2    Yates, J.R.3
  • 10
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. (1997) An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph., 15, 132-134.
    • (1997) J. Mol. Graph , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 11
    • 0031856746 scopus 로고    scopus 로고
    • Electrophoresis combined with novel mass spectrometry techniques: Powerful tools for the analysis of proteins and proteomes
    • Figeys, D., Gygi, S.P., Zhang, Y., Watts, J., Gu, M. and Aebersold, R. (1998) Electrophoresis combined with novel mass spectrometry techniques: powerful tools for the analysis of proteins and proteomes. Electrophoresis, 19, 1811-1818.
    • (1998) Electrophoresis , vol.19 , pp. 1811-1818
    • Figeys, D.1    Gygi, S.P.2    Zhang, Y.3    Watts, J.4    Gu, M.5    Aebersold, R.6
  • 12
    • 0034898896 scopus 로고    scopus 로고
    • DNA-induced structural changes in the papillomavirus capsid
    • Fligge, C., Schäfer, F., Selinka, H.C., Sapp, C. and Sapp, M. (2001) DNA-induced structural changes in the papillomavirus capsid. J. Virol., 75, 7727-7731.
    • (2001) J. Virol , vol.75 , pp. 7727-7731
    • Fligge, C.1    Schäfer, F.2    Selinka, H.C.3    Sapp, C.4    Sapp, M.5
  • 13
    • 0023643240 scopus 로고
    • Site-directed mutation affecting polyomavirus capsid self-assembly in vitro
    • Garcea, R.L., Salunke, D.M. and Caspar, D.L. (1987) Site-directed mutation affecting polyomavirus capsid self-assembly in vitro. Nature, 329, 86-87.
    • (1987) Nature , vol.329 , pp. 86-87
    • Garcea, R.L.1    Salunke, D.M.2    Caspar, D.L.3
  • 14
    • 0028300962 scopus 로고
    • Three-dimensional structure of vaccinia virus-produced human papillomavirus type 1 capsids
    • Hagensee, M.E., Olson, N.H., Baker, T.S. and Galloway, D.A. (1994) Three-dimensional structure of vaccinia virus-produced human papillomavirus type 1 capsids. J. Virol., 68, 4503-4505.
    • (1994) J. Virol , vol.68 , pp. 4503-4505
    • Hagensee, M.E.1    Olson, N.H.2    Baker, T.S.3    Galloway, D.A.4
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A, 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 18
    • 0035214437 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time-of-flight mass spectrometric observation of a peptide triplet induced by thermal cleavage of cystine
    • Kim, J.S. and Kim, H.J. (2001) Matrix-assisted laser desorption/ionization time-of-flight mass spectrometric observation of a peptide triplet induced by thermal cleavage of cystine. Rapid Commun. Mass Spectrom., 15, 2296-2300.
    • (2001) Rapid Commun. Mass Spectrom , vol.15 , pp. 2296-2300
    • Kim, J.S.1    Kim, H.J.2
  • 19
    • 0015751746 scopus 로고
    • Thiol solutions-inhibition of autoxidation
    • Kirkpatrick, A. and Maclaren, J.A. (1973) Thiol solutions-inhibition of autoxidation. Anal. Biochem., 56, 137-139.
    • (1973) Anal. Biochem , vol.56 , pp. 137-139
    • Kirkpatrick, A.1    Maclaren, J.A.2
  • 20
    • 0033119386 scopus 로고    scopus 로고
    • Software for handling macromolecular envelopes
    • Kleywegt, G.J. and Jones, T.A. (1999) Software for handling macromolecular envelopes. Acta Crystallogr. D, 55, 941-944.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 941-944
    • Kleywegt, G.J.1    Jones, T.A.2
  • 21
    • 0031574325 scopus 로고    scopus 로고
    • Not your average density
    • Kleywegt, G.J. and Read, R.J. (1997) Not your average density. Structure, 5, 1557-1569.
    • (1997) Structure , vol.5 , pp. 1557-1569
    • Kleywegt, G.J.1    Read, R.J.2
  • 22
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0031936604 scopus 로고    scopus 로고
    • Intercapsomeric disulfide bonds in papillomavirus assembly and disassembly
    • Li, M., Beard, P., Estes, P.A., Lyon, M.K. and Garcea, R.L. (1998) Intercapsomeric disulfide bonds in papillomavirus assembly and disassembly. J. Virol., 72, 2160-2167.
    • (1998) J. Virol , vol.72 , pp. 2160-2167
    • Li, M.1    Beard, P.2    Estes, P.A.3    Lyon, M.K.4    Garcea, R.L.5
  • 25
    • 0030815133 scopus 로고    scopus 로고
    • Raster 3D photorealistic molecular graphics
    • Merritt, E.A. and Bacon, D.J. (1997) Raster 3D photorealistic molecular graphics. Methods Enzymol., 277, 505-524.
    • (1997) Methods Enzymol , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 26
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins, 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 27
    • 0034767957 scopus 로고    scopus 로고
    • Cancer burden in the year 2000. The global picture
    • Parkin, D.M., Bray, F.I. and Devesa, S.S. (2000) Cancer burden in the year 2000. The global picture. Eur. J. Cancer, 37, S4-S66.
    • (2000) Eur. J. Cancer , vol.37 , pp. S4-S66
    • Parkin, D.M.1    Bray, F.I.2    Devesa, S.S.3
  • 28
    • 0029112188 scopus 로고
    • Organization of the major and minor capsid proteins in human papillomavirus type 33 virus-like particles
    • Sapp, M., Volpers, C., Müller, M. and Streeck, R.E. (1995) Organization of the major and minor capsid proteins in human papillomavirus type 33 virus-like particles. J. Gen. Virol., 76, 2407-2412.
    • (1995) J. Gen. Virol , vol.76 , pp. 2407-2412
    • Sapp, M.1    Volpers, C.2    Müller, M.3    Streeck, R.E.4
  • 29
    • 0031777693 scopus 로고    scopus 로고
    • Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines
    • Sapp, M., Fligge, C., Petzak, I., Harris, J.R. and Streeck, R.E. (1998) Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines. J. Virol., 72, 6186-6189.
    • (1998) J. Virol , vol.72 , pp. 6186-6189
    • Sapp, M.1    Fligge, C.2    Petzak, I.3    Harris, J.R.4    Streeck, R.E.5
  • 30
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. and Mann, M. (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem., 68, 850-858.
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 31
    • 0028303852 scopus 로고
    • Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment
    • Stehle, T., Yan, Y., Benjamin, T.L. and Harrison, S.C. (1994) Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment. Nature, 369, 160-163.
    • (1994) Nature , vol.369 , pp. 160-163
    • Stehle, T.1    Yan, Y.2    Benjamin, T.L.3    Harrison, S.C.4
  • 32
    • 0030584124 scopus 로고    scopus 로고
    • The structure of simian virus 40 refined at 3.1 A resolution
    • Stehle, T., Gamblin, S.J., Yan, Y. and Harrison, S.C. (1996) The structure of simian virus 40 refined at 3.1 A resolution. Structure, 4, 165-182.
    • (1996) Structure , vol.4 , pp. 165-182
    • Stehle, T.1    Gamblin, S.J.2    Yan, Y.3    Harrison, S.C.4
  • 33
    • 0030931283 scopus 로고    scopus 로고
    • Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 Å resolution
    • Trus, B.L., Roden, R.B., Greenstone, H.L., Vrhel, M., Schiller, J.T. and Booy, F.P. (1997) Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 Å resolution. Nat. Struct. Biol., 4, 413-420.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 413-420
    • Trus, B.L.1    Roden, R.B.2    Greenstone, H.L.3    Vrhel, M.4    Schiller, J.T.5    Booy, F.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.