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Volumn 21, Issue 8, 2013, Pages 1396-1405

The structure of herpesvirus fusion glycoprotein B-bilayer complex reveals the protein-membrane and lateral protein-protein interaction

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN B; LIPOSOME;

EID: 84881477785     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.05.018     Document Type: Article
Times cited : (45)

References (56)
  • 1
    • 78049513712 scopus 로고    scopus 로고
    • Cascade of events governing cell-cell fusion induced by herpes simplex virus glycoproteins gD, gH/gL, and gB
    • D. Atanasiu, W.T. Saw, G.H. Cohen, and R.J. Eisenberg Cascade of events governing cell-cell fusion induced by herpes simplex virus glycoproteins gD, gH/gL, and gB J. Virol. 84 2010 12292 12299
    • (2010) J. Virol. , vol.84 , pp. 12292-12299
    • Atanasiu, D.1    Saw, W.T.2    Cohen, G.H.3    Eisenberg, R.J.4
  • 3
    • 35348938515 scopus 로고    scopus 로고
    • Characterization of EBV gB indicates properties of both class i and class II viral fusion proteins
    • M. Backovic, G.P. Leser, R.A. Lamb, R. Longnecker, and T.S. Jardetzky Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins Virology 368 2007 102 113
    • (2007) Virology , vol.368 , pp. 102-113
    • Backovic, M.1    Leser, G.P.2    Lamb, R.A.3    Longnecker, R.4    Jardetzky, T.S.5
  • 4
    • 62449188223 scopus 로고    scopus 로고
    • Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B
    • M. Backovic, R. Longnecker, and T.S. Jardetzky Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B Proc. Natl. Acad. Sci. USA 106 2009 2880 2885
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 2880-2885
    • Backovic, M.1    Longnecker, R.2    Jardetzky, T.S.3
  • 5
    • 0042890360 scopus 로고    scopus 로고
    • Specific association of glycoprotein B with lipid rafts during herpes simplex virus entry
    • F.C. Bender, J.C. Whitbeck, M. Ponce de Leon, H. Lou, R.J. Eisenberg, and G.H. Cohen Specific association of glycoprotein B with lipid rafts during herpes simplex virus entry J. Virol. 77 2003 9542 9552
    • (2003) J. Virol. , vol.77 , pp. 9542-9552
    • Bender, F.C.1    Whitbeck, J.C.2    Ponce De Leon, M.3    Lou, H.4    Eisenberg, R.J.5    Cohen, G.H.6
  • 7
    • 0023705653 scopus 로고
    • Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion
    • W.H. Cai, B. Gu, and S. Person Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion J. Virol. 62 1988 2596 2604
    • (1988) J. Virol. , vol.62 , pp. 2596-2604
    • Cai, W.H.1    Gu, B.2    Person, S.3
  • 9
  • 10
    • 46449135255 scopus 로고    scopus 로고
    • The hydrophobic insertion mechanism of membrane curvature generation by proteins
    • F. Campelo, H.T. McMahon, and M.M. Kozlov The hydrophobic insertion mechanism of membrane curvature generation by proteins Biophys. J. 95 2008 2325 2339
    • (2008) Biophys. J. , vol.95 , pp. 2325-2339
    • Campelo, F.1    McMahon, H.T.2    Kozlov, M.M.3
  • 13
    • 33746853425 scopus 로고    scopus 로고
    • Eclipse phase of herpes simplex virus type 1 infection: Efficient dynein-mediated capsid transport without the small capsid protein VP26
    • K. Döhner, K. Radtke, S. Schmidt, and B. Sodeik Eclipse phase of herpes simplex virus type 1 infection: Efficient dynein-mediated capsid transport without the small capsid protein VP26 J. Virol. 80 2006 8211 8224
    • (2006) J. Virol. , vol.80 , pp. 8211-8224
    • Döhner, K.1    Radtke, K.2    Schmidt, S.3    Sodeik, B.4
  • 14
    • 0026556674 scopus 로고
    • Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deleted
    • A. Forrester, H. Farrell, G. Wilkinson, J. Kaye, N. Davis-Poynter, and T. Minson Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deleted J. Virol. 66 1992 341 348
    • (1992) J. Virol. , vol.66 , pp. 341-348
    • Forrester, A.1    Farrell, H.2    Wilkinson, G.3    Kaye, J.4    Davis-Poynter, N.5    Minson, T.6
  • 16
    • 77955052751 scopus 로고    scopus 로고
    • Interplay of proteins and lipids in generating membrane curvature
    • T.R. Graham, and M.M. Kozlov Interplay of proteins and lipids in generating membrane curvature Curr. Opin. Cell Biol. 22 2010 430 436
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 430-436
    • Graham, T.R.1    Kozlov, M.M.2
  • 20
    • 44749091723 scopus 로고    scopus 로고
    • Entry of herpesviruses into mammalian cells
    • E.E. Heldwein, and C. Krummenacher Entry of herpesviruses into mammalian cells Cell. Mol. Life Sci. 65 2008 1653 1668
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1653-1668
    • Heldwein, E.E.1    Krummenacher, C.2
  • 23
    • 78049497337 scopus 로고    scopus 로고
    • Reevaluating herpes simplex virus hemifusion
    • J.O. Jackson, and R. Longnecker Reevaluating herpes simplex virus hemifusion J. Virol. 84 2010 11814 11821
    • (2010) J. Virol. , vol.84 , pp. 11814-11821
    • Jackson, J.O.1    Longnecker, R.2
  • 24
    • 0242409119 scopus 로고    scopus 로고
    • The membrane-proximal region of vesicular stomatitis virus glycoprotein G ectodomain is critical for fusion and virus infectivity
    • E. Jeetendra, K. Ghosh, D. Odell, J. Li, H.P. Ghosh, and M.A. Whitt The membrane-proximal region of vesicular stomatitis virus glycoprotein G ectodomain is critical for fusion and virus infectivity J. Virol. 77 2003 12807 12818
    • (2003) J. Virol. , vol.77 , pp. 12807-12818
    • Jeetendra, E.1    Ghosh, K.2    Odell, D.3    Li, J.4    Ghosh, H.P.5    Whitt, M.A.6
  • 25
    • 68949149548 scopus 로고    scopus 로고
    • CHARMM-GUI membrane builder for mixed bilayers and its application to yeast membranes
    • S. Jo, J.B. Lim, J.B. Klauda, and W. Im CHARMM-GUI membrane builder for mixed bilayers and its application to yeast membranes Biophys. J. 97 2009 50 58
    • (2009) Biophys. J. , vol.97 , pp. 50-58
    • Jo, S.1    Lim, J.B.2    Klauda, J.B.3    Im, W.4
  • 26
    • 53549088587 scopus 로고    scopus 로고
    • The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines
    • J. Kadlec, S. Loureiro, N.G. Abrescia, D.I. Stuart, and I.M. Jones The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines Nat. Struct. Mol. Biol. 15 2008 1024 1030
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1024-1030
    • Kadlec, J.1    Loureiro, S.2    Abrescia, N.G.3    Stuart, D.I.4    Jones, I.M.5
  • 27
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • J.R. Kremer, D.N. Mastronarde, and J.R. McIntosh Computer visualization of three-dimensional image data using IMOD J. Struct. Biol. 116 1996 71 76
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 28
    • 2942702017 scopus 로고    scopus 로고
    • Influenza hemagglutinins outside of the contact zone are necessary for fusion pore expansion
    • E. Leikina, A. Mittal, M.S. Cho, K. Melikov, M.M. Kozlov, and L.V. Chernomordik Influenza hemagglutinins outside of the contact zone are necessary for fusion pore expansion J. Biol. Chem. 279 2004 26526 26532
    • (2004) J. Biol. Chem. , vol.279 , pp. 26526-26532
    • Leikina, E.1    Mittal, A.2    Cho, M.S.3    Melikov, K.4    Kozlov, M.M.5    Chernomordik, L.V.6
  • 29
    • 70350319200 scopus 로고    scopus 로고
    • The pre-transmembrane domain of the Autographa californica multicapsid nucleopolyhedrovirus GP64 protein is critical for membrane fusion and virus infectivity
    • Z. Li, and G.W. Blissard The pre-transmembrane domain of the Autographa californica multicapsid nucleopolyhedrovirus GP64 protein is critical for membrane fusion and virus infectivity J. Virol. 83 2009 10993 11004
    • (2009) J. Virol. , vol.83 , pp. 10993-11004
    • Li, Z.1    Blissard, G.W.2
  • 30
    • 0023906081 scopus 로고
    • A herpes simplex virus mutant in which glycoprotein D sequences are replaced by beta-galactosidase sequences binds to but is unable to penetrate into cells
    • M.W. Ligas, and D.C. Johnson A herpes simplex virus mutant in which glycoprotein D sequences are replaced by beta-galactosidase sequences binds to but is unable to penetrate into cells J. Virol. 62 1988 1486 1494
    • (1988) J. Virol. , vol.62 , pp. 1486-1494
    • Ligas, M.W.1    Johnson, D.C.2
  • 32
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: Disparate players and common principles
    • S. Martens, and H.T. McMahon Mechanisms of membrane fusion: disparate players and common principles Nat. Rev. Mol. Cell Biol. 9 2008 543 556
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 33
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • D.N. Mastronarde Automated electron microscope tomography using robust prediction of specimen movements J. Struct. Biol. 152 2005 36 51
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 34
    • 48749114826 scopus 로고    scopus 로고
    • Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry
    • U.E. Maurer, B. Sodeik, and K. Grünewald Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry Proc. Natl. Acad. Sci. USA 105 2008 10559 10564
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 10559-10564
    • Maurer, U.E.1    Sodeik, B.2    Grünewald, K.3
  • 35
    • 0030298375 scopus 로고    scopus 로고
    • Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family
    • R.I. Montgomery, M.S. Warner, B.J. Lum, and P.G. Spear Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family Cell 87 1996 427 436
    • (1996) Cell , vol.87 , pp. 427-436
    • Montgomery, R.I.1    Warner, M.S.2    Lum, B.J.3    Spear, P.G.4
  • 36
    • 84857033345 scopus 로고    scopus 로고
    • Finding rigid bodies in protein structures: Application to flexible fitting into cryoEM maps
    • A.P. Pandurangan, and M. Topf Finding rigid bodies in protein structures: Application to flexible fitting into cryoEM maps J. Struct. Biol. 177 2012 520 531
    • (2012) J. Struct. Biol. , vol.177 , pp. 520-531
    • Pandurangan, A.P.1    Topf, M.2
  • 38
    • 77952581453 scopus 로고    scopus 로고
    • Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions
    • G.D. Pintilie, J. Zhang, T.D. Goddard, W. Chiu, and D.C. Gossard Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions J. Struct. Biol. 170 2010 427 438
    • (2010) J. Struct. Biol. , vol.170 , pp. 427-438
    • Pintilie, G.D.1    Zhang, J.2    Goddard, T.D.3    Chiu, W.4    Gossard, D.C.5
  • 39
    • 33749264646 scopus 로고    scopus 로고
    • Molecular gymnastics at the herpesvirus surface
    • F.A. Rey Molecular gymnastics at the herpesvirus surface EMBO Rep. 7 2006 1000 1005
    • (2006) EMBO Rep. , vol.7 , pp. 1000-1005
    • Rey, F.A.1
  • 40
    • 33745974537 scopus 로고    scopus 로고
    • Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G
    • S. Roche, S. Bressanelli, F.A. Rey, and Y. Gaudin Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G Science 313 2006 187 191
    • (2006) Science , vol.313 , pp. 187-191
    • Roche, S.1    Bressanelli, S.2    Rey, F.A.3    Gaudin, Y.4
  • 41
    • 33846959065 scopus 로고    scopus 로고
    • Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G
    • S. Roche, F.A. Rey, Y. Gaudin, and S. Bressanelli Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G Science 315 2007 843 848
    • (2007) Science , vol.315 , pp. 843-848
    • Roche, S.1    Rey, F.A.2    Gaudin, Y.3    Bressanelli, S.4
  • 43
    • 0027502727 scopus 로고
    • A mutant herpes simplex virus type 1 unable to express glycoprotein L cannot enter cells, and its particles lack glycoprotein H
    • C. Roop, L. Hutchinson, and D.C. Johnson A mutant herpes simplex virus type 1 unable to express glycoprotein L cannot enter cells, and its particles lack glycoprotein H J. Virol. 67 1993 2285 2297
    • (1993) J. Virol. , vol.67 , pp. 2285-2297
    • Roop, C.1    Hutchinson, L.2    Johnson, D.C.3
  • 44
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • A. Sali, and T.L. Blundell Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234 1993 779 815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 45
    • 0344011098 scopus 로고    scopus 로고
    • A fast reconstruction algorithm for electron microscope tomography
    • K. Sandberg, D.N. Mastronarde, and G. Beylkin A fast reconstruction algorithm for electron microscope tomography J. Struct. Biol. 144 2003 61 72
    • (2003) J. Struct. Biol. , vol.144 , pp. 61-72
    • Sandberg, K.1    Mastronarde, D.N.2    Beylkin, G.3
  • 46
    • 37749019200 scopus 로고    scopus 로고
    • Viral and developmental cell fusion mechanisms: Conservation and divergence
    • A. Sapir, O. Avinoam, B. Podbilewicz, and L.V. Chernomordik Viral and developmental cell fusion mechanisms: conservation and divergence Dev. Cell 14 2008 11 21
    • (2008) Dev. Cell , vol.14 , pp. 11-21
    • Sapir, A.1    Avinoam, O.2    Podbilewicz, B.3    Chernomordik, L.V.4
  • 47
    • 78649413011 scopus 로고    scopus 로고
    • Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1
    • S.D. Stampfer, H. Lou, G.H. Cohen, R.J. Eisenberg, and E.E. Heldwein Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1 J. Virol. 84 2010 12924 12933
    • (2010) J. Virol. , vol.84 , pp. 12924-12933
    • Stampfer, S.D.1    Lou, H.2    Cohen, G.H.3    Eisenberg, R.J.4    Heldwein, E.E.5
  • 48
    • 0023127956 scopus 로고
    • Herpes simplex virus glycoproteins associated with different morphological entities projecting from the virion envelope
    • L.M. Stannard, A.O. Fuller, and P.G. Spear Herpes simplex virus glycoproteins associated with different morphological entities projecting from the virion envelope J. Gen. Virol. 68 1987 715 725
    • (1987) J. Gen. Virol. , vol.68 , pp. 715-725
    • Stannard, L.M.1    Fuller, A.O.2    Spear, P.G.3
  • 49
    • 0001860050 scopus 로고    scopus 로고
    • Herpesvirus capsid assembly and envelopment
    • W. Chiu, R. Burnett, R. Garcea, Oxford University Press London
    • A. Steven, and P. Spear Herpesvirus capsid assembly and envelopment W. Chiu, R. Burnett, R. Garcea, Structural Biology of Viruses 1997 Oxford University Press London 312 351
    • (1997) Structural Biology of Viruses , pp. 312-351
    • Steven, A.1    Spear, P.2
  • 50
    • 33847295240 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B
    • R.P. Subramanian, and R.J. Geraghty Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B Proc. Natl. Acad. Sci. USA 104 2007 2903 2908
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2903-2908
    • Subramanian, R.P.1    Geraghty, R.J.2
  • 51
    • 51349115007 scopus 로고    scopus 로고
    • Retrospective on the early development of cryoelectron microscopy of macromolecules and a prospective on opportunities for the future
    • K.A. Taylor, and R.M. Glaeser Retrospective on the early development of cryoelectron microscopy of macromolecules and a prospective on opportunities for the future J. Struct. Biol. 163 2008 214 223
    • (2008) J. Struct. Biol. , vol.163 , pp. 214-223
    • Taylor, K.A.1    Glaeser, R.M.2
  • 52
    • 38949092920 scopus 로고    scopus 로고
    • Protein structure fitting and refinement guided by cryo-EM density
    • M. Topf, K. Lasker, B. Webb, H. Wolfson, W. Chiu, and A. Sali Protein structure fitting and refinement guided by cryo-EM density Structure 16 2008 295 307
    • (2008) Structure , vol.16 , pp. 295-307
    • Topf, M.1    Lasker, K.2    Webb, B.3    Wolfson, H.4    Chiu, W.5    Sali, A.6
  • 53
    • 0031963977 scopus 로고    scopus 로고
    • Glycoproteins gB, gD, and gHgL of herpes simplex virus type 1 are necessary and sufficient to mediate membrane fusion in a Cos cell transfection system
    • A. Turner, B. Bruun, T. Minson, and H. Browne Glycoproteins gB, gD, and gHgL of herpes simplex virus type 1 are necessary and sufficient to mediate membrane fusion in a Cos cell transfection system J. Virol. 72 1998 873 875
    • (1998) J. Virol. , vol.72 , pp. 873-875
    • Turner, A.1    Bruun, B.2    Minson, T.3    Browne, H.4
  • 54
    • 79954417945 scopus 로고    scopus 로고
    • Scoring functions for cryoEM density fitting
    • D. Vasishtan, and M. Topf Scoring functions for cryoEM density fitting J. Struct. Biol. 174 2011 333 343
    • (2011) J. Struct. Biol. , vol.174 , pp. 333-343
    • Vasishtan, D.1    Topf, M.2
  • 55
    • 0032726912 scopus 로고    scopus 로고
    • Mutations in the conserved carboxy-terminal hydrophobic region of glycoprotein gB affect infectivity of herpes simplex virus
    • E. Wanas, S. Efler, K. Ghosh, and H.P. Ghosh Mutations in the conserved carboxy-terminal hydrophobic region of glycoprotein gB affect infectivity of herpes simplex virus J. Gen. Virol. 80 1999 3189 3198
    • (1999) J. Gen. Virol. , vol.80 , pp. 3189-3198
    • Wanas, E.1    Efler, S.2    Ghosh, K.3    Ghosh, H.P.4
  • 56
    • 33645791673 scopus 로고    scopus 로고
    • Stable association of herpes simplex virus with target membranes is triggered by low pH in the presence of the gD receptor, HVEM
    • J.C. Whitbeck, Y. Zuo, R.S. Milne, G.H. Cohen, and R.J. Eisenberg Stable association of herpes simplex virus with target membranes is triggered by low pH in the presence of the gD receptor, HVEM J. Virol. 80 2006 3773 3780
    • (2006) J. Virol. , vol.80 , pp. 3773-3780
    • Whitbeck, J.C.1    Zuo, Y.2    Milne, R.S.3    Cohen, G.H.4    Eisenberg, R.J.5


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