메뉴 건너뛰기




Volumn 177, Issue 1, 2012, Pages 145-151

Cryo-EM study of Hepatitis B virus core antigen capsids decorated with antibodies from a human patient

Author keywords

Antibody labeling; Conformational epitopes; Immunodominant epitopes; Molecular modeling; Polyclonal antibodies

Indexed keywords

EPITOPE; HEPATITIS ANTIBODY; HEPATITIS B CORE ANTIGEN; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; POLYCLONAL ANTIBODY; VIRUS CAPSID ANTIGEN;

EID: 84855854230     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2011.10.003     Document Type: Article
Times cited : (10)

References (40)
  • 1
    • 0017678037 scopus 로고
    • New method for localizing proteins in periodic structures: Fab fragment labeling combined with image processing of electron micrographs
    • Aebi U., ten Heggeler B., Onorato L., Kistler J., Showe M.K. New method for localizing proteins in periodic structures: Fab fragment labeling combined with image processing of electron micrographs. Proc. Natl Acad. Sci. USA 1977, 74:5514-5518.
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 5514-5518
    • Aebi, U.1    ten Heggeler, B.2    Onorato, L.3    Kistler, J.4    Showe, M.K.5
  • 3
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    • Baker T.S., Cheng R.H. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 1996, 116:120-130.
    • (1996) J. Struct. Biol. , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 5
    • 0030456414 scopus 로고    scopus 로고
    • Immunoaffinity purification of monoclonal antibodies: in search of an elution buffer of general applicability
    • Ben-David A., Firer M.A. Immunoaffinity purification of monoclonal antibodies: in search of an elution buffer of general applicability. Biotechnol. Tech. 1996, 10:799-802.
    • (1996) Biotechnol. Tech. , vol.10 , pp. 799-802
    • Ben-David, A.1    Firer, M.A.2
  • 6
    • 0027284793 scopus 로고
    • Hybrid hepatitis B virus nucleocapsid bearing an immunodominant region from hepatitis B virus surface antigen
    • Borisova G., Arya B., Dislers A., Borschukova O., Tsibinogin V., et al. Hybrid hepatitis B virus nucleocapsid bearing an immunodominant region from hepatitis B virus surface antigen. J. Virol. 1993, 67:3696-3701.
    • (1993) J. Virol. , vol.67 , pp. 3696-3701
    • Borisova, G.1    Arya, B.2    Dislers, A.3    Borschukova, O.4    Tsibinogin, V.5
  • 7
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Böttcher B., Wynne S.A., Crowther R.A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 1997, 386:88-91.
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 8
    • 0021516232 scopus 로고
    • Specific labeling of protein domains with antibody fragments
    • Buhle E.L., Aebi U. Specific labeling of protein domains with antibody fragments. J. Ultrastruct. Res. 1984, 89:165-178.
    • (1984) J. Ultrastruct. Res. , vol.89 , pp. 165-178
    • Buhle, E.L.1    Aebi, U.2
  • 9
    • 0036310396 scopus 로고    scopus 로고
    • Handedness of the herpes simplex virus capsid and procapsid
    • Cheng N., Trus B.L., Belnap D.M., Newcomb W.W., Brown J.C., et al. Handedness of the herpes simplex virus capsid and procapsid. J. Virol. 2002, 76:7855-7859.
    • (2002) J. Virol. , vol.76 , pp. 7855-7859
    • Cheng, N.1    Trus, B.L.2    Belnap, D.M.3    Newcomb, W.W.4    Brown, J.C.5
  • 10
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway J.F., Cheng N., Zlotnick A., Wingfield P.T., Stahl S.J., et al. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature 1997, 386:91-94.
    • (1997) Nature , vol.386 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingfield, P.T.4    Stahl, S.J.5
  • 11
    • 0037688298 scopus 로고    scopus 로고
    • Characterization of a conformational epitope on hepatitis B virus core antigen and quasi-equivalent variations in antibody binding
    • Conway J.F., Watts N.R., Belnap D.M., Cheng N., Stahl S.J., et al. Characterization of a conformational epitope on hepatitis B virus core antigen and quasi-equivalent variations in antibody binding. J. Virol. 2003, 77:6466-6473.
    • (2003) J. Virol. , vol.77 , pp. 6466-6473
    • Conway, J.F.1    Watts, N.R.2    Belnap, D.M.3    Cheng, N.4    Stahl, S.J.5
  • 12
    • 0032568864 scopus 로고    scopus 로고
    • Hepatitis B virus capsid: localization of the putative immunodominant loop (residues 78 to 83) on the capsid surface, and implications for the distinction between c and e-antigens
    • Conway J.F., Cheng N., Zlotnick A., Stahl S.J., Wingfield P.T., et al. Hepatitis B virus capsid: localization of the putative immunodominant loop (residues 78 to 83) on the capsid surface, and implications for the distinction between c and e-antigens. J. Mol. Biol. 1998, 279:1111-1121.
    • (1998) J. Mol. Biol. , vol.279 , pp. 1111-1121
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Stahl, S.J.4    Wingfield, P.T.5
  • 13
    • 0015242164 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther R.A. Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Philos. Trans. R. Soc. Lond. [Biol.] 1971, 261:221-230.
    • (1971) Philos. Trans. R. Soc. Lond. [Biol.] , vol.261 , pp. 221-230
    • Crowther, R.A.1
  • 14
    • 33745207098 scopus 로고    scopus 로고
    • Native hepatitis B virions and capsids visualized by electron cryomicroscopy
    • Dryden K.A., Wieland S.F., Whitten-Bauer C., Gerin J.L., et al. Native hepatitis B virions and capsids visualized by electron cryomicroscopy. Mol. Cell 2006, 22:843-850.
    • (2006) Mol. Cell , vol.22 , pp. 843-850
    • Dryden, K.A.1    Wieland, S.F.2    Whitten-Bauer, C.3    Gerin, J.L.4
  • 15
    • 14844299785 scopus 로고    scopus 로고
    • Software extensions to UCSF chimera for interactive visualization of large molecular assemblies
    • Goddard T.D., Huang C.C., Ferrin T.E. Software extensions to UCSF chimera for interactive visualization of large molecular assemblies. Structure 2005, 13:473-482.
    • (2005) Structure , vol.13 , pp. 473-482
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 16
    • 28944446740 scopus 로고    scopus 로고
    • Epitope diversity of hepatitis B virus capsids: quasi-equivalent variations in spike epitopes and binding of different antibodies to the same epitope
    • Harris A., Belnap D.M., Watts N.R., Conway J.F., Cheng N., et al. Epitope diversity of hepatitis B virus capsids: quasi-equivalent variations in spike epitopes and binding of different antibodies to the same epitope. J. Mol. Biol. 2006, 355:562-576.
    • (2006) J. Mol. Biol. , vol.355 , pp. 562-576
    • Harris, A.1    Belnap, D.M.2    Watts, N.R.3    Conway, J.F.4    Cheng, N.5
  • 17
    • 0034970430 scopus 로고    scopus 로고
    • Structural studies on antibody interacting with viruses
    • Hewat E., Blaas D. Structural studies on antibody interacting with viruses. Curr. Top. Microbiol. Immunol. 2001, 260:29-44.
    • (2001) Curr. Top. Microbiol. Immunol. , vol.260 , pp. 29-44
    • Hewat, E.1    Blaas, D.2
  • 18
    • 0035783171 scopus 로고    scopus 로고
    • Bsoft: image and molecular processing in electron microscopy
    • Heymann J.B. Bsoft: image and molecular processing in electron microscopy. J. Struct. Biol. 2001, 133:156-169.
    • (2001) J. Struct. Biol. , vol.133 , pp. 156-169
    • Heymann, J.B.1
  • 19
    • 34447648701 scopus 로고    scopus 로고
    • In vitro selection and characterization of DARPins and Fab fragments for the co-crystallization of membrane proteins: the Na(+)-citrate symporter CitS as an example
    • Huber T., Steiner D., Rothlisberger D., Plückthün A. In vitro selection and characterization of DARPins and Fab fragments for the co-crystallization of membrane proteins: the Na(+)-citrate symporter CitS as an example. J. Struct. Biol. 2007, 159:206-221.
    • (2007) J. Struct. Biol. , vol.159 , pp. 206-221
    • Huber, T.1    Steiner, D.2    Rothlisberger, D.3    Plückthün, A.4
  • 20
    • 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., Fuller S.D. Evolutionary conservation in the hepatitis B virus core structure: comparison of human and duck cores. Structure 1995, 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
  • 21
    • 46349104643 scopus 로고    scopus 로고
    • Quantification of structures and gold labeling in transmission electron microscopy
    • Lucocq J. Quantification of structures and gold labeling in transmission electron microscopy. Methods Cell Biol. 2008, 88:59-82.
    • (2008) Methods Cell Biol. , vol.88 , pp. 59-82
    • Lucocq, J.1
  • 22
    • 0142151773 scopus 로고    scopus 로고
    • Exploring the biological basis of hepatitis B e antigen in hepatitis B virus infection
    • Milich D., Liang T.J. Exploring the biological basis of hepatitis B e antigen in hepatitis B virus infection. Hepatology 2003, 38:1075-1086.
    • (2003) Hepatology , vol.38 , pp. 1075-1086
    • Milich, D.1    Liang, T.J.2
  • 23
    • 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., Zlotnick A. Conformational changes in the hepatitis B virus core protein are consistent with a role for allostery in virus assembly. J. Virol. 2010, 84:1607-1615.
    • (2010) J. Virol. , vol.84 , pp. 1607-1615
    • Packianathan, C.1    Katen, S.P.2    Dann, C.E.3    Zlotnick, A.4
  • 24
    • 40949135683 scopus 로고    scopus 로고
    • Conventional and immunoelectron microscopy of mitochondria
    • Perkins E.M., McCaffery J.M. Conventional and immunoelectron microscopy of mitochondria. Methods Mol. Biol. 2007, 372:467-483.
    • (2007) Methods Mol. Biol. , vol.372 , pp. 467-483
    • Perkins, E.M.1    McCaffery, J.M.2
  • 26
    • 0029780275 scopus 로고    scopus 로고
    • The silver anniversary of gold: 25 years of the colloidal gold marker system for immunocytochemistry and histochemistry
    • Roth J. The silver anniversary of gold: 25 years of the colloidal gold marker system for immunocytochemistry and histochemistry. Histochem. Cell Biol. 1996, 106:1-8.
    • (1996) Histochem. Cell Biol. , vol.106 , pp. 1-8
    • Roth, J.1
  • 27
    • 0024500103 scopus 로고
    • Antigenic determinants and functional domains in core antigen and e antigen from hepatitis B virus
    • Salfeld J., Pfaff E., Noah M., Schaller H. Antigenic determinants and functional domains in core antigen and e antigen from hepatitis B virus. J. Virol. 1989, 63:798-808.
    • (1989) J. Virol. , vol.63 , pp. 798-808
    • Salfeld, J.1    Pfaff, E.2    Noah, M.3    Schaller, H.4
  • 28
    • 0025872501 scopus 로고
    • Characterisation of a linear binding site for a monoclonal antibody to hepatitis B core antigen
    • Sällberg M., Ruden U., Magnius L.O., Harthus H.P., Noah M., Wahren B. Characterisation of a linear binding site for a monoclonal antibody to hepatitis B core antigen. J. Med. Virol. 1991, 33:248-252.
    • (1991) J. Med. Virol. , vol.33 , pp. 248-252
    • Sällberg, M.1    Ruden, U.2    Magnius, L.O.3    Harthus, H.P.4    Noah, M.5    Wahren, B.6
  • 29
    • 0026556670 scopus 로고
    • The position of heterologous epitopes inserted in hepatitis B virus core particles determines their immunogenicity
    • (erratum appears in J. Virol. 1992 66:3977)
    • Schödel F., Moriarty A.M., Peterson D.L., Zheng J.A., Hughes J.L., et al. The position of heterologous epitopes inserted in hepatitis B virus core particles determines their immunogenicity. J. Virol. 1992, 66:106-114. (erratum appears in J. Virol. 1992 66:3977).
    • (1992) J. Virol. , vol.66 , pp. 106-114
    • Schödel, F.1    Moriarty, A.M.2    Peterson, D.L.3    Zheng, J.A.4    Hughes, J.L.5
  • 30
    • 0041323243 scopus 로고    scopus 로고
    • Structural studies on antibody-virus complexes
    • Academic Press, San Diego, W. Chiu, J.E. Johnson (Eds.)
    • Smith T.J. Structural studies on antibody-virus complexes. Adv. Prot. Chem.: Virus Structure 2003, 409-454. Academic Press, San Diego. W. Chiu, J.E. Johnson (Eds.).
    • (2003) Adv. Prot. Chem.: Virus Structure , pp. 409-454
    • Smith, T.J.1
  • 31
    • 0027306163 scopus 로고
    • Structure of a human rhinovirus-bivalently bound antibody complex: implications for viral neutralization and antibody flexibility
    • Smith T.J., Olson N.H., Cheng R.H., Chase E.S., Baker T.S. Structure of a human rhinovirus-bivalently bound antibody complex: implications for viral neutralization and antibody flexibility. Proc. Natl Acad. Sci. USA 1993, 90:7015-7018.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7015-7018
    • Smith, T.J.1    Olson, N.H.2    Cheng, R.H.3    Chase, E.S.4    Baker, T.S.5
  • 32
    • 77649336166 scopus 로고    scopus 로고
    • Generation and characterization of a chimeric rabbit/human Fab for co-crystallization of HIV-1 Rev
    • Stahl S.J., Watts N.R., Rader C., DiMattia M.A., Mage R.G., et al. Generation and characterization of a chimeric rabbit/human Fab for co-crystallization of HIV-1 Rev. J. Mol. Biol. 2010, 397:697-708.
    • (2010) J. Mol. Biol. , vol.397 , pp. 697-708
    • Stahl, S.J.1    Watts, N.R.2    Rader, C.3    DiMattia, M.A.4    Mage, R.G.5
  • 33
    • 26944499478 scopus 로고    scopus 로고
    • Structure, assembly, and antigenicity of hepatitis B virus capsid proteins
    • Steven A.C., Conway J.F., Cheng N., Watts N.R., Belnap D.M., et al. Structure, assembly, and antigenicity of hepatitis B virus capsid proteins. Adv. Virus Res. 2005, 64:125-164.
    • (2005) Adv. Virus Res. , vol.64 , pp. 125-164
    • Steven, A.C.1    Conway, J.F.2    Cheng, N.3    Watts, N.R.4    Belnap, D.M.5
  • 34
    • 0026490068 scopus 로고
    • Distinct monoclonal antibodies separately label the hexons or the pentons of herpes simplex virus capsid
    • Trus B.L., Newcomb W.W., Booy F.P., Brown J.C., Steven A.C. Distinct monoclonal antibodies separately label the hexons or the pentons of herpes simplex virus capsid. Proc. Natl Acad. Sci. USA 1992, 89:11508-11512.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 11508-11512
    • Trus, B.L.1    Newcomb, W.W.2    Booy, F.P.3    Brown, J.C.4    Steven, A.C.5
  • 36
    • 0027121512 scopus 로고
    • Identification of a Fab interaction footprint site on an icosahedral virus by cryoelectron microscopy and X-ray crystallography
    • Wang G.J., Porta C., Chen Z.G., Baker T.S., Johnson J.E. Identification of a Fab interaction footprint site on an icosahedral virus by cryoelectron microscopy and X-ray crystallography. Nature 1992, 355:275-278.
    • (1992) Nature , vol.355 , pp. 275-278
    • Wang, G.J.1    Porta, C.2    Chen, Z.G.3    Baker, T.S.4    Johnson, J.E.5
  • 37
    • 44349168170 scopus 로고    scopus 로고
    • Non-canonical binding of an antibody resembling a naive B cell receptor immunoglobulin to hepatitis B virus capsids
    • Watts N.R., Cardone G., Vethanayagam J.G., Cheng N., Hultgren C., et al. Non-canonical binding of an antibody resembling a naive B cell receptor immunoglobulin to hepatitis B virus capsids. J. Mol. Biol. 2008, 379:1119-1129.
    • (2008) J. Mol. Biol. , vol.379 , pp. 1119-1129
    • Watts, N.R.1    Cardone, G.2    Vethanayagam, J.G.3    Cheng, N.4    Hultgren, C.5
  • 38
    • 70449337697 scopus 로고    scopus 로고
    • Use of hepadnavirus core proteins as vaccine platforms
    • Whitacre D.C., Lee B.O., Milich D.R. Use of hepadnavirus core proteins as vaccine platforms. Expert Rev. Vaccines 2009, 8:1565-1573.
    • (2009) Expert Rev. Vaccines , vol.8 , pp. 1565-1573
    • Whitacre, D.C.1    Lee, B.O.2    Milich, D.R.3
  • 39
    • 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., Steven A.C. Hepatitis core antigen produced in Escherichia coli: subunit composition, conformational analysis, and in vitro capsid assembly. Biochemistry 1995, 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
  • 40
    • 0033152857 scopus 로고    scopus 로고
    • The crystal structure of the human hepatitis B virus capsid
    • Wynne S.A., Crowther R.A., Leslie A.G. The crystal structure of the human hepatitis B virus capsid. Mol. Cell 1999, 3:771-780.
    • (1999) Mol. Cell , vol.3 , pp. 771-780
    • Wynne, S.A.1    Crowther, R.A.2    Leslie, A.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.