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Volumn 5, Issue 1, 2014, Pages 34-41

Relating structure to evolution in class II viral membrane fusion proteins

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS ENVELOPE PROTEIN; VIRUS FUSION PROTEIN;

EID: 84893278973     PISSN: 18796257     EISSN: 18796265     Source Type: Journal    
DOI: 10.1016/j.coviro.2014.01.009     Document Type: Review
Times cited : (52)

References (61)
  • 1
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • J.J. Skehel, and D.C. Wiley Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin Annu Rev Biochem 69 2000 531 569
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 2
    • 34548824835 scopus 로고    scopus 로고
    • Structural basis of viral invasion: Lessons from paramyxovirus F
    • R.A. Lamb, and T.S. Jardetzky Structural basis of viral invasion: lessons from paramyxovirus F Curr Opin Struct Biol 17 2007 427 436
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 427-436
    • Lamb, R.A.1    Jardetzky, T.S.2
  • 3
    • 11144340301 scopus 로고    scopus 로고
    • Class i and class II viral fusion protein structures reveal similar principles in membrane fusion
    • D.J. Schibli, and W. Weissenhorn Class I and class II viral fusion protein structures reveal similar principles in membrane fusion Mol Membr Biol 21 2004 361 371
    • (2004) Mol Membr Biol , vol.21 , pp. 361-371
    • Schibli, D.J.1    Weissenhorn, W.2
  • 4
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: More than one way to make a hairpin
    • M. Kielian, and F.A. Rey Virus membrane-fusion proteins: more than one way to make a hairpin Nat Rev Microbiol 4 2006 67 76
    • (2006) Nat Rev Microbiol , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 5
    • 84873205968 scopus 로고    scopus 로고
    • Crystal structure of glycoprotein C from Rift Valley fever virus
    • M. Dessau, and Y. Modis Crystal structure of glycoprotein C from Rift Valley fever virus Proc Natl Acad Sci U S A 110 2013 1696 1701
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 1696-1701
    • Dessau, M.1    Modis, Y.2
  • 7
    • 79960903181 scopus 로고    scopus 로고
    • Class III viral membrane fusion proteins
    • M. Backovic, and T.S. Jardetzky Class III viral membrane fusion proteins Adv Exp Med Biol 714 2011 91 101
    • (2011) Adv Exp Med Biol , vol.714 , pp. 91-101
    • Backovic, M.1    Jardetzky, T.S.2
  • 8
    • 84973436381 scopus 로고    scopus 로고
    • Flaviviridae
    • D.M. Knipe, P.M. Howley, Lippincott Williams & Wilkins Philadelphia
    • B.D. Lindenbach, C.L. Murray, H.J. Thiel, and C.M. Rice Flaviviridae D.M. Knipe, P.M. Howley, Fields Virology vol. 1 (Sixth Edition) 2013 Lippincott Williams & Wilkins Philadelphia 712 746
    • (2013) Fields Virology , vol.1 VOL. SIXTH EDITION , pp. 712-746
    • Lindenbach, B.D.1    Murray, C.L.2    Thiel, H.J.3    Rice, C.M.4
  • 9
    • 84876865608 scopus 로고    scopus 로고
    • Crystal structure of glycoprotein E2 from bovine viral diarrhea virus
    • Y. Li, J. Wang, R. Kanai, and Y. Modis Crystal structure of glycoprotein E2 from bovine viral diarrhea virus Proc Natl Acad Sci U S A 110 2013 6805 6810
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 6805-6810
    • Li, Y.1    Wang, J.2    Kanai, R.3    Modis, Y.4
  • 10
    • 84873133718 scopus 로고    scopus 로고
    • Structure of a pestivirus envelope glycoprotein E2 clarifies its role in cell entry
    • K. El Omari, O. Iourin, K. Harlos, J.M. Grimes, and D.I. Stuart Structure of a pestivirus envelope glycoprotein E2 clarifies its role in cell entry Cell Rep 3 2013 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
  • 11
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
    • F.A. Rey, F.X. Heinz, C. Mandl, C. Kunz, and S.C. Harrison The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution Nature 375 1995 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
  • 12
    • 0037495036 scopus 로고    scopus 로고
    • A ligand-binding pocket in the dengue virus envelope glycoprotein
    • Y. Modis, S. Ogata, D. Clements, and S.C. Harrison A ligand-binding pocket in the dengue virus envelope glycoprotein Proc Natl Acad Sci U S A 100 2003 6986 6990
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6986-6990
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 14
    • 84857082391 scopus 로고    scopus 로고
    • Crystal structure of the Japanese encephalitis virus envelope protein
    • V.C. Luca, J. AbiMansour, C.A. Nelson, and D.H. Fremont Crystal structure of the Japanese encephalitis virus envelope protein J Virol 86 2012 2337 2346
    • (2012) J Virol , vol.86 , pp. 2337-2346
    • Luca, V.C.1    Abimansour, J.2    Nelson, C.A.3    Fremont, D.H.4
  • 15
    • 11144244755 scopus 로고    scopus 로고
    • Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein
    • Y. Modis, S. Ogata, D. Clements, and S.C. Harrison Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein J Virol 79 2005 1223 1231
    • (2005) J Virol , vol.79 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 16
  • 19
    • 0035815282 scopus 로고    scopus 로고
    • The Fusion glycoprotein shell of Semliki Forest virus: An icosahedral assembly primed for fusogenic activation at endosomal pH
    • J. Lescar, A. Roussel, M.W. Wien, J. Navaza, S.D. Fuller, G. Wengler, and F.A. Rey The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH Cell 105 2001 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    Wengler, G.6    Rey, F.A.7
  • 20
    • 78649891889 scopus 로고    scopus 로고
    • Structural changes of envelope proteins during alphavirus fusion
    • L. Li, J. Jose, Y. Xiang, R.J. Kuhn, and M.G. Rossmann Structural changes of envelope proteins during alphavirus fusion Nature 468 2010 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
  • 23
    • 80052503042 scopus 로고    scopus 로고
    • The structure of barmah forest virus as revealed by cryo-electron microscopy at a 6-angstrom resolution has detailed transmembrane protein architecture and interactions
    • V.A. Kostyuchenko, J. Jakana, X. Liu, A.D. Haddow, M. Aung, S.C. Weaver, W. Chiu, and S.M. Lok The structure of barmah forest virus as revealed by cryo-electron microscopy at a 6-angstrom resolution has detailed transmembrane protein architecture and interactions J Virol 85 2011 9327 9333
    • (2011) J Virol , vol.85 , pp. 9327-9333
    • Kostyuchenko, V.A.1    Jakana, J.2    Liu, X.3    Haddow, A.D.4    Aung, M.5    Weaver, S.C.6    Chiu, W.7    Lok, S.M.8
  • 27
    • 0034899311 scopus 로고    scopus 로고
    • Monoclonal antibodies that bind to domain III of dengue virus e glycoprotein are the most efficient blockers of virus adsorption to Vero cells
    • W.D. Crill, and J.T. Roehrig Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells J Virol 75 2001 7769 7773
    • (2001) J Virol , vol.75 , pp. 7769-7773
    • Crill, W.D.1    Roehrig, J.T.2
  • 30
    • 0347626038 scopus 로고    scopus 로고
    • An external loop region of domain III of dengue virus type 2 envelope protein is involved in serotype-specific binding to mosquito but not mammalian cells
    • J.J. Hung, M.T. Hsieh, M.J. Young, C.L. Kao, C.C. King, and W. Chang An external loop region of domain III of dengue virus type 2 envelope protein is involved in serotype-specific binding to mosquito but not mammalian cells J Virol 78 2004 378 388
    • (2004) J Virol , vol.78 , pp. 378-388
    • Hung, J.J.1    Hsieh, M.T.2    Young, M.J.3    Kao, C.L.4    King, C.C.5    Chang, W.6
  • 31
    • 0033978271 scopus 로고    scopus 로고
    • Evolutionary reversals during viral adaptation to alternating hosts
    • W.D. Crill, H.A. Wichman, and J.J. Bull Evolutionary reversals during viral adaptation to alternating hosts Genetics 154 2000 27 37
    • (2000) Genetics , vol.154 , pp. 27-37
    • Crill, W.D.1    Wichman, H.A.2    Bull, J.J.3
  • 33
    • 21244462832 scopus 로고    scopus 로고
    • Dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN)-mediated enhancement of dengue virus infection is independent of DC-SIGN internalization signals
    • P.Y. Lozach, L. Burleigh, I. Staropoli, E. Navarro-Sanchez, J. Harriague, J.L. Virelizier, F.A. Rey, P. Despres, F. Arenzana-Seisdedos, and A. Amara Dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN)-mediated enhancement of dengue virus infection is independent of DC-SIGN internalization signals J Biol Chem 280 2005 23698 23708
    • (2005) J Biol Chem , vol.280 , pp. 23698-23708
    • Lozach, P.Y.1    Burleigh, L.2    Staropoli, I.3    Navarro-Sanchez, E.4    Harriague, J.5    Virelizier, J.L.6    Rey, F.A.7    Despres, P.8    Arenzana-Seisdedos, F.9    Amara, A.10
  • 34
    • 31144445030 scopus 로고    scopus 로고
    • West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection
    • C.W. Davis, H.Y. Nguyen, S.L. Hanna, M.D. Sanchez, R.W. Doms, and T.C. Pierson West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection J Virol 80 2006 1290 1301
    • (2006) J Virol , vol.80 , pp. 1290-1301
    • Davis, C.W.1    Nguyen, H.Y.2    Hanna, S.L.3    Sanchez, M.D.4    Doms, R.W.5    Pierson, T.C.6
  • 35
    • 0041563793 scopus 로고    scopus 로고
    • Dendritic-cell-specific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses
    • E. Navarro-Sanchez, R. Altmeyer, A. Amara, O. Schwartz, F. Fieschi, J.L. Virelizier, F. Arenzana-Seisdedos, and P. Despres Dendritic-cell-specific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses EMBO Rep 4 2003 723 728
    • (2003) EMBO Rep , vol.4 , pp. 723-728
    • Navarro-Sanchez, E.1    Altmeyer, R.2    Amara, A.3    Schwartz, O.4    Fieschi, F.5    Virelizier, J.L.6    Arenzana-Seisdedos, F.7    Despres, P.8
  • 38
    • 0030764559 scopus 로고    scopus 로고
    • Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate
    • Y. Chen, T. Maguire, R.E. Hileman, J.R. Fromm, J.D. Esko, R.J. Linhardt, and R.M. Marks Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate Nat Med 3 1997 866 871
    • (1997) Nat Med , vol.3 , pp. 866-871
    • Chen, Y.1    Maguire, T.2    Hileman, R.E.3    Fromm, J.R.4    Esko, J.D.5    Linhardt, R.J.6    Marks, R.M.7
  • 39
    • 0242363253 scopus 로고    scopus 로고
    • DC-SIGN and L-SIGN can act as attachment receptors for alphaviruses and distinguish between mosquito cell- and mammalian cell-derived viruses
    • W.B. Klimstra, E.M. Nangle, M.S. Smith, A.D. Yurochko, and K.D. Ryman DC-SIGN and L-SIGN can act as attachment receptors for alphaviruses and distinguish between mosquito cell- and mammalian cell-derived viruses J Virol 77 2003 12022 12032
    • (2003) J Virol , vol.77 , pp. 12022-12032
    • Klimstra, W.B.1    Nangle, E.M.2    Smith, M.S.3    Yurochko, A.D.4    Ryman, K.D.5
  • 40
    • 0031869503 scopus 로고    scopus 로고
    • Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor
    • W.B. Klimstra, K.D. Ryman, and R.E. Johnston Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor J Virol 72 1998 7357 7366
    • (1998) J Virol , vol.72 , pp. 7357-7366
    • Klimstra, W.B.1    Ryman, K.D.2    Johnston, R.E.3
  • 41
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Y. Modis, S. Ogata, D. Clements, and S.C. Harrison Structure of the dengue virus envelope protein after membrane fusion Nature 427 2004 313 319
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 43
  • 44
    • 84871961238 scopus 로고    scopus 로고
    • Structure of the St. Louis encephalitis virus postfusion envelope trimer
    • V.C. Luca, C.A. Nelson, and D.H. Fremont Structure of the St. Louis encephalitis virus postfusion envelope trimer J Virol 87 2013 818 828
    • (2013) J Virol , vol.87 , pp. 818-828
    • Luca, V.C.1    Nelson, C.A.2    Fremont, D.H.3
  • 45
    • 84873849253 scopus 로고    scopus 로고
    • Structure of a dengue virus envelope protein late-stage fusion intermediate
    • D.E. Klein, J.L. Choi, and S.C. Harrison Structure of a dengue virus envelope protein late-stage fusion intermediate J Virol 87 2013 2287 2290
    • (2013) J Virol , vol.87 , pp. 2287-2290
    • Klein, D.E.1    Choi, J.L.2    Harrison, S.C.3
  • 46
    • 57049101667 scopus 로고    scopus 로고
    • A stable prefusion intermediate of the alphavirus fusion protein reveals critical features of class II membrane fusion
    • C. Sanchez-San Martin, H. Sosa, and M. Kielian A stable prefusion intermediate of the alphavirus fusion protein reveals critical features of class II membrane fusion Cell Host Microbe 4 2008 600 608
    • (2008) Cell Host Microbe , vol.4 , pp. 600-608
    • Sanchez-San Martin, C.1    Sosa, H.2    Kielian, M.3
  • 47
    • 33847246763 scopus 로고    scopus 로고
    • Characterization of a structural intermediate of flavivirus membrane fusion
    • K. Stiasny, C. Kossl, J. Lepault, F.A. Rey, and F.X. Heinz Characterization of a structural intermediate of flavivirus membrane fusion PLoS Pathog 3 2007 e20
    • (2007) PLoS Pathog , vol.3 , pp. 20
    • Stiasny, K.1    Kossl, C.2    Lepault, J.3    Rey, F.A.4    Heinz, F.X.5
  • 48
    • 84884680449 scopus 로고    scopus 로고
    • Viral membrane fusion and nucleocapsid delivery into the cytoplasm are distinct events in some flaviviruses
    • A.M. Nour, Y. Li, J. Wolenski, and Y. Modis Viral membrane fusion and nucleocapsid delivery into the cytoplasm are distinct events in some flaviviruses PLoS Pathog 9 2013 e5851003
    • (2013) PLoS Pathog , vol.9 , pp. 5851003
    • Nour, A.M.1    Li, Y.2    Wolenski, J.3    Modis, Y.4
  • 50
    • 80055103942 scopus 로고    scopus 로고
    • Identification of the myelin oligodendrocyte glycoprotein as a cellular receptor for rubella virus
    • H. Cong, Y. Jiang, and P. Tien Identification of the myelin oligodendrocyte glycoprotein as a cellular receptor for rubella virus J Virol 85 2011 11038 11047
    • (2011) J Virol , vol.85 , pp. 11038-11047
    • Cong, H.1    Jiang, Y.2    Tien, P.3
  • 51
    • 15444371889 scopus 로고    scopus 로고
    • Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein (beta-penetrenes)
    • C.E. Garry, and R.F. Garry Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein (beta-penetrenes) Theor Biol Med Model 1 2004 10
    • (2004) Theor Biol Med Model , vol.1 , pp. 10
    • Garry, C.E.1    Garry, R.F.2
  • 53
    • 40649115227 scopus 로고    scopus 로고
    • Insights into bunyavirus architecture from electron cryotomography of Uukuniemi virus
    • A.K. Overby, R.F. Pettersson, K. Grunewald, and J.T. Huiskonen Insights into bunyavirus architecture from electron cryotomography of Uukuniemi virus Proc Natl Acad Sci U S A 105 2008 2375 2379
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 2375-2379
    • Overby, A.K.1    Pettersson, R.F.2    Grunewald, K.3    Huiskonen, J.T.4
  • 54
    • 64049094507 scopus 로고    scopus 로고
    • Electron cryo-microscopy and single-particle averaging of Rift Valley fever virus: Evidence for GN-GC glycoprotein heterodimers
    • J.T. Huiskonen, A.K. Overby, F. Weber, and K. Grunewald Electron cryo-microscopy and single-particle averaging of Rift Valley fever virus: evidence for GN-GC glycoprotein heterodimers J Virol 83 2009 3762 3769
    • (2009) J Virol , vol.83 , pp. 3762-3769
    • Huiskonen, J.T.1    Overby, A.K.2    Weber, F.3    Grunewald, K.4
  • 57
    • 0037444329 scopus 로고    scopus 로고
    • Proteomics computational analyses suggest that hepatitis C virus E1 and pestivirus E2 envelope glycoproteins are truncated class II fusion proteins
    • R.F. Garry, and S. Dash Proteomics computational analyses suggest that hepatitis C virus E1 and pestivirus E2 envelope glycoproteins are truncated class II fusion proteins Virology 307 2003 255 265
    • (2003) Virology , vol.307 , pp. 255-265
    • Garry, R.F.1    Dash, S.2
  • 58
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • J.J. Skehel, and D.C. Wiley Coiled coils in both intracellular vesicle and viral membrane fusion Cell 95 1998 871 874
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 60
    • 67749120188 scopus 로고    scopus 로고
    • Helical extension of the neuronal SNARE complex into the membrane
    • A. Stein, G. Weber, M.C. Wahl, and R. Jahn Helical extension of the neuronal SNARE complex into the membrane Nature 460 2009 525 528
    • (2009) Nature , vol.460 , pp. 525-528
    • Stein, A.1    Weber, G.2    Wahl, M.C.3    Jahn, R.4
  • 61
    • 77957933124 scopus 로고    scopus 로고
    • Ultrastructural and biophysical characterization of hepatitis C virus particles produced in cell culture
    • P. Gastaminza, K.A. Dryden, B. Boyd, M.R. Wood, M. Law, M. Yeager, and F.V. Chisari Ultrastructural and biophysical characterization of hepatitis C virus particles produced in cell culture J Virol 84 2010 10999 11009
    • (2010) J Virol , vol.84 , pp. 10999-11009
    • Gastaminza, P.1    Dryden, K.A.2    Boyd, B.3    Wood, M.R.4    Law, M.5    Yeager, M.6    Chisari, F.V.7


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