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Volumn 479-480, Issue , 2015, Pages 498-507

Viral membrane fusion

Author keywords

Fusion mechanism; Fusion protein; Virus entry

Indexed keywords

VIRUS FUSION PROTEIN;

EID: 84937761010     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2015.03.043     Document Type: Review
Times cited : (557)

References (101)
  • 1
    • 84860909461 scopus 로고    scopus 로고
    • Characterization of monomeric intermediates during VSV glycoprotein structural transition
    • Albertini A.A., Merigoux C., Libersou S., Madiona K., Bressanelli S., et al. Characterization of monomeric intermediates during VSV glycoprotein structural transition. PLoS Pathog. 2012, 8:e1002556.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002556
    • Albertini, A.A.1    Merigoux, C.2    Libersou, S.3    Madiona, K.4    Bressanelli, S.5
  • 2
    • 0034676041 scopus 로고    scopus 로고
    • The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition
    • Armstrong R.T., Kushnir A.S., White J.M. The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition. J Cell Biol. 2000, 151:425-437.
    • (2000) J Cell Biol. , vol.151 , pp. 425-437
    • Armstrong, R.T.1    Kushnir, A.S.2    White, J.M.3
  • 4
    • 84890196626 scopus 로고    scopus 로고
    • Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy
    • Bartesaghi A., Merk A., Borgnia M.J., Milne J.L., Subramaniam S. Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy. Nat. Struct. Mol. Biol. 2013, 20:1352-1357.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1352-1357
    • Bartesaghi, A.1    Merk, A.2    Borgnia, M.J.3    Milne, J.L.4    Subramaniam, S.5
  • 6
    • 0028864614 scopus 로고
    • A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein
    • Blacklow S.C., Lu M., Kim P.S. A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein. Biochemistry 1995, 34:14955-14962.
    • (1995) Biochemistry , vol.34 , pp. 14955-14962
    • Blacklow, S.C.1    Lu, M.2    Kim, P.S.3
  • 7
    • 0016821407 scopus 로고
    • Sindbis virus glycoproteins form a regular icosahedral surface lattice
    • von Bonsdorff C.H., Harrison S.C. Sindbis virus glycoproteins form a regular icosahedral surface lattice. J. Virol. 1975, 16:141-145.
    • (1975) J. Virol. , vol.16 , pp. 141-145
    • von Bonsdorff, C.H.1    Harrison, S.C.2
  • 8
    • 0016839826 scopus 로고
    • Surface structure of Uukuniemi virus
    • von Bonsdorff C.H., Pettersson R. Surface structure of Uukuniemi virus. J. Virol. 1975, 16:1296-1307.
    • (1975) J. Virol. , vol.16 , pp. 1296-1307
    • von Bonsdorff, C.H.1    Pettersson, R.2
  • 9
    • 84866859065 scopus 로고    scopus 로고
    • Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering
    • Bose S., Zokarkar A., Welch B.D., Leser G.P., Jardetzky T.S., et al. Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering. Proc. Natl. Acad. Sci. USA 2012, 109:E2625-2634.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. E2625-2634
    • Bose, S.1    Zokarkar, A.2    Welch, B.D.3    Leser, G.P.4    Jardetzky, T.S.5
  • 10
    • 84886927744 scopus 로고    scopus 로고
    • A stabilized headless measles virus attachment protein stalk efficiently triggers membrane fusion
    • Brindley M.A., Suter R., Schestak I., Kiss G., Wright E.R., et al. A stabilized headless measles virus attachment protein stalk efficiently triggers membrane fusion. J. Virol. 2013, 87:11693-11703.
    • (2013) J. Virol. , vol.87 , pp. 11693-11703
    • Brindley, M.A.1    Suter, R.2    Schestak, I.3    Kiss, G.4    Wright, E.R.5
  • 11
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough P.A., Hughson F.M., Skehel J.J., Wiley D.C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 1994, 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 13
    • 80052851832 scopus 로고    scopus 로고
    • Ebola virus entry requires the cholesterol transporter Niemann-Pick C1
    • Carette J.E., Raaben M., Wong A.C., Herbert A.S., et al. Ebola virus entry requires the cholesterol transporter Niemann-Pick C1. Nature 2011, 477:340-343.
    • (2011) Nature , vol.477 , pp. 340-343
    • Carette, J.E.1    Raaben, M.2    Wong, A.C.3    Herbert, A.S.4
  • 14
  • 15
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan D.C., Kim P.S. HIV entry and its inhibition. Cell 1998, 93:681-684.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 16
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan D.C., Fass D., Berger J.M., Kim P.S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 1997, 89:263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 17
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran K., Sullivan N.J., Felbor U., Whelan S.P., Cunningham J.M. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 2005, 308:1643-1645.
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 18
    • 0031445916 scopus 로고    scopus 로고
    • Flickering fusion pores comparable with initial exocytotic pores occur in protein-free phospholipid bilayers
    • Chanturiya A., Chernomordik L.V., Zimmerberg J. Flickering fusion pores comparable with initial exocytotic pores occur in protein-free phospholipid bilayers. Proc. Natl. Acad. Sci. USA 1997, 94:14423-14428.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14423-14428
    • Chanturiya, A.1    Chernomordik, L.V.2    Zimmerberg, J.3
  • 19
    • 84937768831 scopus 로고    scopus 로고
    • Sequential conformational rearrangements in flavivirus membrane fusion
    • Chao L.H., Klein D.E., Schmidt A.G., Pena J.M., Harrison S.C. Sequential conformational rearrangements in flavivirus membrane fusion. eLife 2014, 3:e04389.
    • (2014) eLife , vol.3 , pp. e04389
    • Chao, L.H.1    Klein, D.E.2    Schmidt, A.G.3    Pena, J.M.4    Harrison, S.C.5
  • 20
    • 18844470928 scopus 로고    scopus 로고
    • Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
    • Chen J., Lee K.H., Steinhauer D.A., Stevens D.J., Skehel J.J., et al. Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 1998, 95:409-417.
    • (1998) Cell , vol.95 , pp. 409-417
    • Chen, J.1    Lee, K.H.2    Steinhauer, D.A.3    Stevens, D.J.4    Skehel, J.J.5
  • 21
    • 0033529752 scopus 로고    scopus 로고
    • N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil
    • Chen J., Skehel J.J., Wiley D.C. N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil. Proc. Natl. Acad. Sci. USA 1999, 96:8967-8972.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8967-8972
    • Chen, J.1    Skehel, J.J.2    Wiley, D.C.3
  • 24
    • 80052868218 scopus 로고    scopus 로고
    • Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection
    • Cote M., Misasi J., Ren T., Bruchez A., Lee K., et al. Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection. Nature 2011, 477:344-348.
    • (2011) Nature , vol.477 , pp. 344-348
    • Cote, M.1    Misasi, J.2    Ren, T.3    Bruchez, A.4    Lee, K.5
  • 25
    • 0033762350 scopus 로고    scopus 로고
    • Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase
    • Crennell S., Takimoto T., Portner A., Taylor G. Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase. Nat. Struct. Biol. 2000, 7:1068-1074.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1068-1074
    • Crennell, S.1    Takimoto, T.2    Portner, A.3    Taylor, G.4
  • 26
    • 84873205968 scopus 로고    scopus 로고
    • Crystal structure of glycoprotein C from Rift valley fever virus
    • Dessau M., Modis Y. Crystal structure of glycoprotein C from Rift valley fever virus. Proc. Natl. Acad. Sci. USA 2013, 110:1696-1701.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 1696-1701
    • Dessau, M.1    Modis, Y.2
  • 27
    • 84881514823 scopus 로고    scopus 로고
    • Synaptic proteins promote calcium-triggered fast transition from point contact to full fusion
    • Diao J., Grob P., Cipriano D.J., Kyoung M., Zhang Y., et al. Synaptic proteins promote calcium-triggered fast transition from point contact to full fusion. eLife 2012, 1:e00109.
    • (2012) eLife , vol.1 , pp. e00109
    • Diao, J.1    Grob, P.2    Cipriano, D.J.3    Kyoung, M.4    Zhang, Y.5
  • 28
    • 84872973964 scopus 로고    scopus 로고
    • Functional and evolutionary insight from the crystal structure of rubella virus protein E1
    • DuBois R.M., Vaney M.C., Tortorici M.A., Kurdi R.A., Barba-Spaeth G., et al. Functional and evolutionary insight from the crystal structure of rubella virus protein E1. Nature 2013, 493:552-556.
    • (2013) Nature , vol.493 , pp. 552-556
    • DuBois, R.M.1    Vaney, M.C.2    Tortorici, M.A.3    Kurdi, R.A.4    Barba-Spaeth, G.5
  • 29
    • 84873133718 scopus 로고    scopus 로고
    • Structure of a pestivirus envelope glycoprotein E2 clarifies its role in cell entry
    • El Omari K., Iourin O., Harlos K., Grimes J.M., Stuart D.I. Structure of a pestivirus envelope glycoprotein E2 clarifies its role in cell entry. Cell Rep. 2013, 3:30-35.
    • (2013) Cell Rep. , vol.3 , pp. 30-35
    • El Omari, K.1    Iourin, O.2    Harlos, K.3    Grimes, J.M.4    Stuart, D.I.5
  • 30
    • 0021414772 scopus 로고
    • Free energy potential for aggregation of mixed phosphatidylcholine/phosphatidylserine lipid vesicles in glucose polymer (dextran) solutions
    • Evans E., Metcalfe M. Free energy potential for aggregation of mixed phosphatidylcholine/phosphatidylserine lipid vesicles in glucose polymer (dextran) solutions. Biophys. J. 1984, 45:715-720.
    • (1984) Biophys. J. , vol.45 , pp. 715-720
    • Evans, E.1    Metcalfe, M.2
  • 31
    • 0024034873 scopus 로고
    • Attraction between lipid bilayer membranes in concentrated solutions of nonadsorbing polymers: comparison of mean-field theory with measurements of adhesion energy
    • Evans E., Needham D. Attraction between lipid bilayer membranes in concentrated solutions of nonadsorbing polymers: comparison of mean-field theory with measurements of adhesion energy. Macromolecules 1988, 21:1822-1831.
    • (1988) Macromolecules , vol.21 , pp. 1822-1831
    • Evans, E.1    Needham, D.2
  • 33
    • 41649090223 scopus 로고    scopus 로고
    • A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies
    • Frey G., Peng H., Rits-Volloch S., Morelli M., Cheng Y., et al. A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies. Proc. Natl. Acad. Sci. USA 2012, 105:3739-3744.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3739-3744
    • Frey, G.1    Peng, H.2    Rits-Volloch, S.3    Morelli, M.4    Cheng, Y.5
  • 34
    • 15444371889 scopus 로고    scopus 로고
    • Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein (beta-penetrenes)
    • Garry C.E., Garry R.F. Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein (beta-penetrenes). Theor. Biol. Med. Model. 2004, 1:10.
    • (2004) Theor. Biol. Med. Model. , vol.1 , pp. 10
    • Garry, C.E.1    Garry, R.F.2
  • 35
    • 1642540249 scopus 로고    scopus 로고
    • Conformational change and protein-protein interactions of the fusion protein of Semliki forest virus
    • Gibbons D.L., Vaney M.C., Roussel A., Vigouroux A., Reilly B., et al. Conformational change and protein-protein interactions of the fusion protein of Semliki forest virus. Nature 2004, 427:320-325.
    • (2004) Nature , vol.427 , pp. 320-325
    • Gibbons, D.L.1    Vaney, M.C.2    Roussel, A.3    Vigouroux, A.4    Reilly, B.5
  • 36
    • 0025855266 scopus 로고
    • Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions
    • Guirakhoo F., Heinz F.X., Mandl C.W., Holzmann H., Kunz C. Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions. J. Gen. Virol. 1991, 72(Pt 6):1323-1329.
    • (1991) J. Gen. Virol. , vol.72 , pp. 1323-1329
    • Guirakhoo, F.1    Heinz, F.X.2    Mandl, C.W.3    Holzmann, H.4    Kunz, C.5
  • 38
    • 33746005904 scopus 로고    scopus 로고
    • Crystal structure of glycoprotein B from herpes simplex virus 1
    • Heldwein E.E., Lou H., Bender F.C., Cohen G.H., Eisenberg R.J., et al. Crystal structure of glycoprotein B from herpes simplex virus 1. Science 2006, 313:217-220.
    • (2006) Science , vol.313 , pp. 217-220
    • Heldwein, E.E.1    Lou, H.2    Bender, F.C.3    Cohen, G.H.4    Eisenberg, R.J.5
  • 39
    • 0026637939 scopus 로고
    • Biological activity of paramyxovirus fusion proteins: factors influencing formation of syncytia
    • Horvath C.M., Paterson R.G., Shaughnessy M.A., Wood R., Lamb R.A. Biological activity of paramyxovirus fusion proteins: factors influencing formation of syncytia. J. Virol. 1992, 66:4564-4569.
    • (1992) J. Virol. , vol.66 , pp. 4564-4569
    • Horvath, C.M.1    Paterson, R.G.2    Shaughnessy, M.A.3    Wood, R.4    Lamb, R.A.5
  • 40
    • 0026525004 scopus 로고
    • Functional interactions between the fusion protein and hemagglutinin-neuraminidase of human parainfluenza viruses
    • Hu X.L., Ray R., Compans R.W. Functional interactions between the fusion protein and hemagglutinin-neuraminidase of human parainfluenza viruses. J. Virol. 1992, 66:1528-1534.
    • (1992) J. Virol. , vol.66 , pp. 1528-1534
    • Hu, X.L.1    Ray, R.2    Compans, R.W.3
  • 41
    • 84879053104 scopus 로고    scopus 로고
    • Influenza-virus membrane fusion by cooperative fold-back of stochastically induced hemagglutinin intermediates
    • Ivanovic T., Choi J.L., Whelan S.P., van Oijen A.M., Harrison S.C. Influenza-virus membrane fusion by cooperative fold-back of stochastically induced hemagglutinin intermediates. eLife 2013, 2:e00333.
    • (2013) eLife , vol.2 , pp. e00333
    • Ivanovic, T.1    Choi, J.L.2    Whelan, S.P.3    van Oijen, A.M.4    Harrison, S.C.5
  • 42
    • 84893301662 scopus 로고    scopus 로고
    • Activation of paramyxovirus membrane fusion and virus entry
    • Jardetzky T.S., Lamb R.A. Activation of paramyxovirus membrane fusion and virus entry. Curr. Opin. Virol. 2014, 5:24-33.
    • (2014) Curr. Opin. Virol. , vol.5 , pp. 24-33
    • Jardetzky, T.S.1    Lamb, R.A.2
  • 43
    • 84890858459 scopus 로고    scopus 로고
    • Crystal structure of a soluble cleaved HIV-1 envelope trimer
    • Julien J.P., Cupo A., Sok D., Stanfield R.L., Lyumkis D., et al. Crystal structure of a soluble cleaved HIV-1 envelope trimer. Science 2013, 342:1477-1483.
    • (2013) Science , vol.342 , pp. 1477-1483
    • Julien, J.P.1    Cupo, A.2    Sok, D.3    Stanfield, R.L.4    Lyumkis, D.5
  • 44
    • 53549088587 scopus 로고    scopus 로고
    • The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines
    • Kadlec J., Loureiro S, Abrescia N.G., Stuart D.I., Jones I.M. The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines. Nat. Struct. Mol. Biol. 2008, 15:1024-1030.
    • (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
  • 45
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble G.W., Danieli T., White J.M. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell 1994, 76:383-391.
    • (1994) Cell , vol.76 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 46
    • 59649122639 scopus 로고    scopus 로고
    • Structure of Epstein-Barr virus glycoprotein 42 suggests a mechanism for triggering receptor-activated virus entry
    • Kirschner A.N., Sorem J., Longnecker R., Jardetzky T.S. Structure of Epstein-Barr virus glycoprotein 42 suggests a mechanism for triggering receptor-activated virus entry. Structure 2009, 17:223-233.
    • (2009) Structure , vol.17 , pp. 223-233
    • Kirschner, A.N.1    Sorem, J.2    Longnecker, R.3    Jardetzky, T.S.4
  • 47
    • 84873849253 scopus 로고    scopus 로고
    • Structure of a dengue virus envelope protein late-stage fusion intermediate
    • Klein D.E., Choi J.L., Harrison S.C. Structure of a dengue virus envelope protein late-stage fusion intermediate. J. Virol. 2013, 87:2287-2293.
    • (2013) J. Virol. , vol.87 , pp. 2287-2293
    • Klein, D.E.1    Choi, J.L.2    Harrison, S.C.3
  • 48
    • 84888778890 scopus 로고    scopus 로고
    • Hepatitis C virus E2 envelope glycoprotein core structure
    • Kong L., Giang E., Nieusma T., Kadam R.U., Cogburn K.E., et al. Hepatitis C virus E2 envelope glycoprotein core structure. Science 2013, 342:1090-1094.
    • (2013) Science , vol.342 , pp. 1090-1094
    • Kong, L.1    Giang, E.2    Nieusma, T.3    Kadam, R.U.4    Cogburn, K.E.5
  • 49
    • 28644433999 scopus 로고    scopus 로고
    • Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry
    • Krummenacher C., Supekar V.M., Whitbeck J.C., Lazear E., Connolly S.A., et al. Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry. EMBO J. 2005, 24:4144-4153.
    • (2005) EMBO J. , vol.24 , pp. 4144-4153
    • Krummenacher, C.1    Supekar, V.M.2    Whitbeck, J.C.3    Lazear, E.4    Connolly, S.A.5
  • 50
    • 0001733884 scopus 로고    scopus 로고
    • Direct measurement of polyethylene glycol induced depletion attraction between lipid bilayers
    • Kuhl T., Guo Y., Alderfer J.L., Berman A.D., Leckband D., et al. Direct measurement of polyethylene glycol induced depletion attraction between lipid bilayers. Langmuir 1996, 12:3003-3014.
    • (1996) Langmuir , vol.12 , pp. 3003-3014
    • Kuhl, T.1    Guo, Y.2    Alderfer, J.L.3    Berman, A.D.4    Leckband, D.5
  • 51
    • 18344387519 scopus 로고    scopus 로고
    • Structure of dengue virus: implications for flavivirus organization, maturation, and fusion
    • Kuhn R.J., Zhang W., Rossmann M.G., Pletnev S.V., Corver J., et al. Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 2002, 108:717-725.
    • (2002) Cell , vol.108 , pp. 717-725
    • Kuhn, R.J.1    Zhang, W.2    Rossmann, M.G.3    Pletnev, S.V.4    Corver, J.5
  • 53
    • 0346654073 scopus 로고    scopus 로고
    • Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III
    • Lawrence M.C., Borg N.A., Streltsov V.A., Pilling P.A., Epa V.C., et al. Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III. J. Mol. Biol. 2004, 335:1343-1357.
    • (2004) J. Mol. Biol. , vol.335 , pp. 1343-1357
    • Lawrence, M.C.1    Borg, N.A.2    Streltsov, V.A.3    Pilling, P.A.4    Epa, V.C.5
  • 54
    • 47049107589 scopus 로고    scopus 로고
    • Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor
    • Lee J.E., Fusco M.L., Hessell A.J., Oswald W.B., Burton D.R., et al. Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature 2008, 454:177-182.
    • (2008) Nature , vol.454 , pp. 177-182
    • Lee, J.E.1    Fusco, M.L.2    Hessell, A.J.3    Oswald, W.B.4    Burton, D.R.5
  • 55
    • 77950528480 scopus 로고    scopus 로고
    • Architecture of a nascent viral fusion pore
    • Lee K.K. Architecture of a nascent viral fusion pore. EMBO J. 2010, 29:1299-1311.
    • (2010) EMBO J. , vol.29 , pp. 1299-1311
    • Lee, K.K.1
  • 56
    • 0035815282 scopus 로고    scopus 로고
    • The fusion glycoprotein shell of Semliki forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH
    • Lescar J., Roussel A., Wien M.W., Navaza J., Fuller S.D., et al. The fusion glycoprotein shell of Semliki forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH. Cell 2001, 105:137-148.
    • (2001) Cell , vol.105 , pp. 137-148
    • Lescar, J.1    Roussel, A.2    Wien, M.W.3    Navaza, J.4    Fuller, S.D.5
  • 57
    • 41349112506 scopus 로고    scopus 로고
    • The flavivirus precursor membrane-envelope protein complex: structure and maturation
    • Li L., Lok S.M., Yu I.M., Zhang Y., Kuhn R.J., et al. The flavivirus precursor membrane-envelope protein complex: structure and maturation. Science 2008, 319:1830-1834.
    • (2008) Science , vol.319 , pp. 1830-1834
    • Li, L.1    Lok, S.M.2    Yu, I.M.3    Zhang, Y.4    Kuhn, R.J.5
  • 58
    • 78649891889 scopus 로고    scopus 로고
    • Structural changes of envelope proteins during alphavirus fusion
    • Li L., Jose J., Xiang Y., Kuhn R.J., Rossmann M.G. Structural changes of envelope proteins during alphavirus fusion. Nature 2010, 468:705-708.
    • (2010) Nature , vol.468 , pp. 705-708
    • Li, L.1    Jose, J.2    Xiang, Y.3    Kuhn, R.J.4    Rossmann, M.G.5
  • 59
    • 24644511078 scopus 로고    scopus 로고
    • Membrane structures of the hemifusion-inducing fusion peptide mutant G1S and the fusion-blocking mutant G1V of influenza virus hemagglutinin suggest a mechanism for pore opening in membrane fusion
    • Li Y., Han X., Lai A.L., Bushweller J.H., Cafiso D.S., et al. Membrane structures of the hemifusion-inducing fusion peptide mutant G1S and the fusion-blocking mutant G1V of influenza virus hemagglutinin suggest a mechanism for pore opening in membrane fusion. J. Virol. 2005, 79:12065-12076.
    • (2005) J. Virol. , vol.79 , pp. 12065-12076
    • Li, Y.1    Han, X.2    Lai, A.L.3    Bushweller, J.H.4    Cafiso, D.S.5
  • 60
    • 84876865608 scopus 로고    scopus 로고
    • Crystal structure of glycoprotein E2 from bovine viral diarrhea virus
    • Li Y., Wang J., Kanai R., Modis Y. Crystal structure of glycoprotein E2 from bovine viral diarrhea virus. Proc. Natl. Acad. Sci. USA 2013, 110:6805-6810.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 6805-6810
    • Li, Y.1    Wang, J.2    Kanai, R.3    Modis, Y.4
  • 61
    • 84888271006 scopus 로고    scopus 로고
    • Unraveling a three-step spatiotemporal mechanism of triggering of receptor-induced Nipah virus fusion and cell entry
    • Liu Q., Stone J.A., Bradel-Tretheway B., Dabundo J., Benavides Montano J.A., et al. Unraveling a three-step spatiotemporal mechanism of triggering of receptor-induced Nipah virus fusion and cell entry. PLoS Pathog. 2013, 9:e1003770.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003770
    • Liu, Q.1    Stone, J.A.2    Bradel-Tretheway, B.3    Dabundo, J.4    Benavides Montano, J.A.5
  • 62
    • 0025219313 scopus 로고
    • Fusion function of the Semliki forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62
    • Lobigs M., Garoff H. Fusion function of the Semliki forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62. J. Virol. 1990, 64:1233-1240.
    • (1990) J. Virol. , vol.64 , pp. 1233-1240
    • Lobigs, M.1    Garoff, H.2
  • 63
    • 77954947285 scopus 로고    scopus 로고
    • The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface
    • Lorieau J.L., Louis J.M., Bax A. The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface. Proc. Natl. Acad. Sci. USA 2010, 107:11341-11346.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 11341-11346
    • Lorieau, J.L.1    Louis, J.M.2    Bax, A.3
  • 64
    • 84890859441 scopus 로고    scopus 로고
    • Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
    • Lyumkis D., Julien J.P., de Val N., Cupo A., Potter C.S., et al. Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer. Science 2013, 342:1484-1490.
    • (2013) Science , vol.342 , pp. 1484-1490
    • Lyumkis, D.1    Julien, J.P.2    de Val, N.3    Cupo, A.4    Potter, C.S.5
  • 65
    • 78651074196 scopus 로고    scopus 로고
    • Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex
    • Matsuura H., Kirschner A.N., Longnecker R., Jardetzky T.S. Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex. Proc. Natl. Acad. Sci. USA 2010, 107:22641-22646.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 22641-22646
    • Matsuura, H.1    Kirschner, A.N.2    Longnecker, R.3    Jardetzky, T.S.4
  • 66
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis Y., Ogata S., Clements D., Harrison S.C. Structure of the dengue virus envelope protein after membrane fusion. Nature 2004, 427:313-319.
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 67
    • 33644815756 scopus 로고    scopus 로고
    • Mapping the structure and function of the E1 and E2 glycoproteins in alphaviruses
    • Mukhopadhyay S., Zhang W., Gabler S., Chipman P.R., Strauss E.G., et al. Mapping the structure and function of the E1 and E2 glycoproteins in alphaviruses. Structure 2006, 14:63-73.
    • (2006) Structure , vol.14 , pp. 63-73
    • Mukhopadhyay, S.1    Zhang, W.2    Gabler, S.3    Chipman, P.R.4    Strauss, E.G.5
  • 68
    • 0038065763 scopus 로고    scopus 로고
    • Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41
    • Munoz-Barroso I., Durell S., Sakaguchi K., Appella E., Blumenthal R. Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41. J. Cell Biol. 1998, 140:315-323.
    • (1998) J. Cell Biol. , vol.140 , pp. 315-323
    • Munoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Appella, E.4    Blumenthal, R.5
  • 69
    • 79551621397 scopus 로고    scopus 로고
    • The heads of the measles virus attachment protein move to transmit the fusion-triggering signal
    • Navaratnarajah C.K., Oezguen N., Rupp L., Kay L., Leonard V.H., et al. The heads of the measles virus attachment protein move to transmit the fusion-triggering signal. Nat. Struct. Mol. Biol. 2011, 18:128-134.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 128-134
    • Navaratnarajah, C.K.1    Oezguen, N.2    Rupp, L.3    Kay, L.4    Leonard, V.H.5
  • 70
    • 84909640954 scopus 로고    scopus 로고
    • Structure and immune recognition of trimeric pre-fusion HIV-1 Env
    • Pancera M., Zhou T., Druz A., Georgiev I.S., Soto C., et al. Structure and immune recognition of trimeric pre-fusion HIV-1 Env. Nature 2014, 514:455-461.
    • (2014) Nature , vol.514 , pp. 455-461
    • Pancera, M.1    Zhou, T.2    Druz, A.3    Georgiev, I.S.4    Soto, C.5
  • 71
    • 0000853942 scopus 로고
    • Measured work of deformation and repulsion of lecithin bilayers
    • Parsegian V.A., Fuller N., Rand R.P. Measured work of deformation and repulsion of lecithin bilayers. Proc. Natl. Acad. Sci. USA 1979, 76:2750-2754.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2750-2754
    • Parsegian, V.A.1    Fuller, N.2    Rand, R.P.3
  • 72
    • 0021136801 scopus 로고
    • Physical force considerations in model and biological membranes
    • Rand R.P., Parsegian V.A. Physical force considerations in model and biological membranes. Can. J. Biochem. Cell Biol. 1984, 62:752-759.
    • (1984) Can. J. Biochem. Cell Biol. , vol.62 , pp. 752-759
    • Rand, R.P.1    Parsegian, V.A.2
  • 73
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2A resolution
    • Rey F.A., Heinz F.X., Mandl C., Kunz C., Harrison S.C. The envelope glycoprotein from tick-borne encephalitis virus at 2A resolution. Nature 1995, 375:291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 74
    • 0036309399 scopus 로고    scopus 로고
    • Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers
    • Roche S., Gaudin Y. Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers. Virology 2002, 297:128-135.
    • (2002) Virology , vol.297 , pp. 128-135
    • Roche, S.1    Gaudin, Y.2
  • 75
    • 33745974537 scopus 로고    scopus 로고
    • Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G
    • Roche S., Bressanelli S., Rey F.A., Gaudin Y. Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G. Science 2006, 313:187-191.
    • (2006) Science , vol.313 , pp. 187-191
    • Roche, S.1    Bressanelli, S.2    Rey, F.A.3    Gaudin, Y.4
  • 76
    • 33846959065 scopus 로고    scopus 로고
    • Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G
    • Roche S., Rey F.A., Gaudin Y., Bressanelli S. Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G. Science 2007, 315:843-848.
    • (2007) Science , vol.315 , pp. 843-848
    • Roche, S.1    Rey, F.A.2    Gaudin, Y.3    Bressanelli, S.4
  • 77
    • 33644799064 scopus 로고    scopus 로고
    • Structure and interactions at the viral surface of the envelope protein E1 of Semliki forest virus
    • Roussel A., Lescar J., Vaney M.C., Wengler G., Wengler G., et al. Structure and interactions at the viral surface of the envelope protein E1 of Semliki forest virus. Structure 2006, 14:75-86.
    • (2006) Structure , vol.14 , pp. 75-86
    • Roussel, A.1    Lescar, J.2    Vaney, M.C.3    Wengler, G.4    Wengler, G.5
  • 78
    • 84911378398 scopus 로고    scopus 로고
    • Assembly and architecture of the EBV B cell entry triggering complex
    • Sathiyamoorthy K., Jiang J., Hu Y.X., Rowe C.L., Mohl B.S., et al. Assembly and architecture of the EBV B cell entry triggering complex. PLoS Pathog. 2014, 10:e1004309.
    • (2014) PLoS Pathog. , vol.10 , pp. e1004309
    • Sathiyamoorthy, K.1    Jiang, J.2    Hu, Y.X.3    Rowe, C.L.4    Mohl, B.S.5
  • 79
    • 78649436107 scopus 로고    scopus 로고
    • Peptide inhibitors of flavivirus entry derived from the E protein stem
    • Schmidt A.G., Yang P.L., Harrison S.C. Peptide inhibitors of flavivirus entry derived from the E protein stem. J. Virol. 2010, 84:12549-12554.
    • (2010) J. Virol. , vol.84 , pp. 12549-12554
    • Schmidt, A.G.1    Yang, P.L.2    Harrison, S.C.3
  • 80
    • 77954044356 scopus 로고    scopus 로고
    • Peptide inhibitors of dengue-virus entry target a late-stage fusion intermediate
    • Schmidt A.G., Yang P.L., Harrison S.C. Peptide inhibitors of dengue-virus entry target a late-stage fusion intermediate. PLoS Pathog. 2010, 6:e1000851.
    • (2010) PLoS Pathog. , vol.6 , pp. e1000851
    • Schmidt, A.G.1    Yang, P.L.2    Harrison, S.C.3
  • 81
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin
    • Skehel J.J., Wiley D.C. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 2000, 69:531-569.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 82
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: grappling with SNARE and SM proteins
    • Südhof T.C., Rothman J.E. Membrane fusion: grappling with SNARE and SM proteins. Science 2009, 323:474-477.
    • (2009) Science , vol.323 , pp. 474-477
    • Südhof, T.C.1    Rothman, J.E.2
  • 83
    • 78649817910 scopus 로고    scopus 로고
    • Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography
    • Voss J.E., Vaney M.C., Duquerroy S., Vonrhein C., Girard-Blanc C., et al. Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography. Nature 2010, 468:709-712.
    • (2010) Nature , vol.468 , pp. 709-712
    • Voss, J.E.1    Vaney, M.C.2    Duquerroy, S.3    Vonrhein, C.4    Girard-Blanc, C.5
  • 84
    • 84880615199 scopus 로고    scopus 로고
    • Protease-resistant peptide design-empowering nature's fragile warriors against HIV
    • Weinstock M.T., Francis J.N., Redman J.S., Kay M.S. Protease-resistant peptide design-empowering nature's fragile warriors against HIV. Biopolymers 2012, 98:431-442.
    • (2012) Biopolymers , vol.98 , pp. 431-442
    • Weinstock, M.T.1    Francis, J.N.2    Redman, J.S.3    Kay, M.S.4
  • 86
    • 0032214714 scopus 로고    scopus 로고
    • Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
    • Weissenhorn W., Carfi A., Lee K.H., Skehel J.J., Wiley D.C. Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain. Mol. Cell 1998, 2:605-616.
    • (1998) Mol. Cell , vol.2 , pp. 605-616
    • Weissenhorn, W.1    Carfi, A.2    Lee, K.H.3    Skehel, J.J.4    Wiley, D.C.5
  • 87
    • 84867351430 scopus 로고    scopus 로고
    • Structure of the cleavage-activated prefusion form of the parainfluenza virus 5 fusion protein
    • Welch B.D., Liu Y., Kors C.A., Leser G.P., Jardetzky T.S., et al. Structure of the cleavage-activated prefusion form of the parainfluenza virus 5 fusion protein. Proc. Natl. Acad. Sci. USA 2012, 109:16672-16677.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 16672-16677
    • Welch, B.D.1    Liu, Y.2    Kors, C.A.3    Leser, G.P.4    Jardetzky, T.S.5
  • 88
    • 84883271554 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 (PIV5) hemagglutinin-neuraminidase (HN) ectodomain
    • Welch B.D., Yuan P., Bose S., Kors C.A., Lamb R.A., et al. Structure of the parainfluenza virus 5 (PIV5) hemagglutinin-neuraminidase (HN) ectodomain. PLoS Pathog. 2013, 9:e1003534.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003534
    • Welch, B.D.1    Yuan, P.2    Bose, S.3    Kors, C.A.4    Lamb, R.A.5
  • 89
    • 84859897771 scopus 로고    scopus 로고
    • A new player in the puzzle of filovirus entry
    • White J.M., Schornberg K.L. A new player in the puzzle of filovirus entry. Nat. Rev. Microbiol. 2012, 10:317-322.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 317-322
    • White, J.M.1    Schornberg, K.L.2
  • 90
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3A resolution
    • Wilson I.A., Skehel J.J., Wiley D.C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3A resolution. Nature 1981, 289:366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 91
    • 0037072603 scopus 로고    scopus 로고
    • Observation of a membrane fusion intermediate structure
    • Yang L., Huang H.W. Observation of a membrane fusion intermediate structure. Science 2002, 297:1877-1879.
    • (2002) Science , vol.297 , pp. 1877-1879
    • Yang, L.1    Huang, H.W.2
  • 92
    • 33646185493 scopus 로고    scopus 로고
    • Subunit stoichiometry of human immunodeficiency virus type 1 envelope glycoprotein trimers during virus entry into host cells
    • Yang X., Kurteva S., Ren X., Lee S., Sodroski J. Subunit stoichiometry of human immunodeficiency virus type 1 envelope glycoprotein trimers during virus entry into host cells. J. Virol. 2006, 80:4388-4395.
    • (2006) J. Virol. , vol.80 , pp. 4388-4395
    • Yang, X.1    Kurteva, S.2    Ren, X.3    Lee, S.4    Sodroski, J.5
  • 94
    • 41349112304 scopus 로고    scopus 로고
    • Structure of the immature dengue virus at low pH primes proteolytic maturation
    • Yu I.M., Zhang W., Holdaway H.A., Li L., Kostyuchenko V.A., et al. Structure of the immature dengue virus at low pH primes proteolytic maturation. Science 2008, 319:1834-1837.
    • (2008) Science , vol.319 , pp. 1834-1837
    • Yu, I.M.1    Zhang, W.2    Holdaway, H.A.3    Li, L.4    Kostyuchenko, V.A.5
  • 95
    • 18944375873 scopus 로고    scopus 로고
    • Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose
    • Yuan P., Thompson T.B., Wurzburg B.A., Paterson R.G., Lamb R.A., et al. Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose. Structure 2005, 13:803-815.
    • (2005) Structure , vol.13 , pp. 803-815
    • Yuan, P.1    Thompson, T.B.2    Wurzburg, B.A.3    Paterson, R.G.4    Lamb, R.A.5
  • 97
    • 0242574743 scopus 로고    scopus 로고
    • Visualization of membrane protein domains by cryo-electron microscopy of dengue virus
    • Zhang W., Chipman P.R., Corver J., Johnson P.R., Zhang Y., et al. Visualization of membrane protein domains by cryo-electron microscopy of dengue virus. Nat. Struct. Biol. 2003, 10:907-912.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 907-912
    • Zhang, W.1    Chipman, P.R.2    Corver, J.3    Johnson, P.R.4    Zhang, Y.5
  • 98
    • 84872048730 scopus 로고    scopus 로고
    • Cryo-EM structure of the mature dengue virus at 3.5-A resolution
    • Zhang X., Ge P., Yu X., Brannan J.M., Bi G., et al. Cryo-EM structure of the mature dengue virus at 3.5-A resolution. Nat. Struct. Mol. Biol. 2013, 20:105-110.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 105-110
    • Zhang, X.1    Ge, P.2    Yu, X.3    Brannan, J.M.4    Bi, G.5
  • 99
    • 84919459596 scopus 로고    scopus 로고
    • Structure of acidic pH dengue virus showing the fusogenic glycoprotein trimers
    • Zhang X., Sheng J., Austin S.K., Hoornweg T.E., Smit J.M., et al. Structure of acidic pH dengue virus showing the fusogenic glycoprotein trimers. J. Virol. 2015, 89:743-750.
    • (2015) J. Virol. , vol.89 , pp. 743-750
    • Zhang, X.1    Sheng, J.2    Austin, S.K.3    Hoornweg, T.E.4    Smit, J.M.5
  • 101
    • 33745203490 scopus 로고    scopus 로고
    • Distribution and three-dimensional structure of AIDS virus envelope spikes
    • Zhu P., Liu J., Bess J., Chertova E., Lifson J.D., et al. Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 2006, 441:847-852.
    • (2006) Nature , vol.441 , pp. 847-852
    • Zhu, P.1    Liu, J.2    Bess, J.3    Chertova, E.4    Lifson, J.D.5


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