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Volumn 84, Issue 2, 2010, Pages 983-992

Characterization of Lassa virus glycoprotein oligomerization and influence of cholesterol on virus replication

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; MONOMER; OLIGOMER; VIRUS GLYCOPROTEIN; VIRUS PROTEIN;

EID: 73849123124     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02039-09     Document Type: Article
Times cited : (39)

References (87)
  • 1
    • 70349284496 scopus 로고    scopus 로고
    • Assembly of arenavirus envelope glycoprotein GPC in detergent-soluble membrane microdomains
    • Agnihothram, S. S., B. Dancho, K. W. Grant, M. L. Grimes, D. S. Lyles, and J. H. Nunberg. 2009. Assembly of arenavirus envelope glycoprotein GPC in detergent-soluble membrane microdomains. J. Virol. 83:9890-9900.
    • (2009) J. Virol , vol.83 , pp. 9890-9900
    • Agnihothram, S.S.1    Dancho, B.2    Grant, K.W.3    Grimes, M.L.4    Lyles, D.S.5    Nunberg, J.H.6
  • 2
    • 33646737672 scopus 로고    scopus 로고
    • Role of the stable signal peptide and cytoplasmic domain of G2 in regulating intracellular transport of the Junin virus envelope glycoprotein complex
    • Agnihothram, S. S., J. York, and J. H. Nunberg. 2006. Role of the stable signal peptide and cytoplasmic domain of G2 in regulating intracellular transport of the Junin virus envelope glycoprotein complex. J. Virol. 80: 5189-5198.
    • (2006) J. Virol , vol.80 , pp. 5189-5198
    • Agnihothram, S.S.1    York, J.2    Nunberg, J.H.3
  • 3
    • 34247118403 scopus 로고    scopus 로고
    • Bitopic membrane topology of the stable signal peptide in the tripartite Junin virus GP-C envelope glycoprotein complex
    • Agnihothram, S. S., J. York, M. Trahey, and J. H. Nunberg. 2007. Bitopic membrane topology of the stable signal peptide in the tripartite Junin virus GP-C envelope glycoprotein complex. J. Virol. 81:4331-4337.
    • (2007) J. Virol , vol.81 , pp. 4331-4337
    • Agnihothram, S.S.1    York, J.2    Trahey, M.3    Nunberg, J.H.4
  • 5
    • 0037372280 scopus 로고    scopus 로고
    • Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P
    • Beyer, W. R., D. Popplau, W. Garten, D. von Laer, and O. Lenz. 2003. Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P. J. Virol. 77:2866-2872.
    • (2003) J. Virol , vol.77 , pp. 2866-2872
    • Beyer, W.R.1    Popplau, D.2    Garten, W.3    von Laer, D.4    Lenz, O.5
  • 6
    • 42949150297 scopus 로고    scopus 로고
    • Cholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin
    • Biswas, S., S. R. Yin, P. S. Blank, and J. Zimmerberg. 2008. Cholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin. J. Gen. Physiol. 131:503-513.
    • (2008) J. Gen. Physiol , vol.131 , pp. 503-513
    • Biswas, S.1    Yin, S.R.2    Blank, P.S.3    Zimmerberg, J.4
  • 7
    • 0029939662 scopus 로고    scopus 로고
    • Dimerization of transcobalamin II receptor. Requirement of a structurally ordered lipid bilayer
    • Bose, S., J. Feix, S. Seetharam, and B. Seetharam. 1996. Dimerization of transcobalamin II receptor. Requirement of a structurally ordered lipid bilayer. J. Biol. Chem. 271:11718-11725.
    • (1996) J. Biol. Chem , vol.271 , pp. 11718-11725
    • Bose, S.1    Feix, J.2    Seetharam, S.3    Seetharam, B.4
  • 8
    • 33748950305 scopus 로고    scopus 로고
    • Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium
    • Böttcher, E., T. Matrosovich, M. Beyerle, H. D. Klenk, W. Garten, and M. Matrosovich. 2006. Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium. J. Virol. 80: 9896-9898.
    • (2006) J. Virol , vol.80 , pp. 9896-9898
    • Böttcher, E.1    Matrosovich, T.2    Beyerle, M.3    Klenk, H.D.4    Garten, W.5    Matrosovich, M.6
  • 9
    • 58349122284 scopus 로고    scopus 로고
    • Hepatitis B virus infection is dependent on cholesterol in the viral envelope
    • Bremer, C. M., C. Bung, N. Kott, M. Hardt, and D. Glebe. 2009. Hepatitis B virus infection is dependent on cholesterol in the viral envelope. Cell Microbiol. 11:249-260.
    • (2009) Cell Microbiol , vol.11 , pp. 249-260
    • Bremer, C.M.1    Bung, C.2    Kott, N.3    Hardt, M.4    Glebe, D.5
  • 10
    • 67249156188 scopus 로고    scopus 로고
    • Briese, T., J. T. Paweska, L. K. McMullan, S. K. Hutchison, C. Street, G. Palacios, M. L. Khristova, J. Weyer, R. Swanepoel, M. Egholm, S. T. Nichol, and W. I. Lipkin. 2009. Genetic detection and characterization of Lujo virus, a new hemorrhagic fever-associated arenavirus from southern Africa. PLoS Pathog. 5:e1000455.
    • Briese, T., J. T. Paweska, L. K. McMullan, S. K. Hutchison, C. Street, G. Palacios, M. L. Khristova, J. Weyer, R. Swanepoel, M. Egholm, S. T. Nichol, and W. I. Lipkin. 2009. Genetic detection and characterization of Lujo virus, a new hemorrhagic fever-associated arenavirus from southern Africa. PLoS Pathog. 5:e1000455.
  • 11
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D. A., and J. K. Rose. 1992. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68:533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 12
    • 0037377710 scopus 로고    scopus 로고
    • Organization of the vesicular stomatitis virus glycoprotein into membrane microdomains occurs independently of intracellular viral components
    • Brown, E. L., and D. S. Lyles. 2003. Organization of the vesicular stomatitis virus glycoprotein into membrane microdomains occurs independently of intracellular viral components. J. Virol. 77:3985-3992.
    • (2003) J. Virol , vol.77 , pp. 3985-3992
    • Brown, E.L.1    Lyles, D.S.2
  • 13
    • 0033793871 scopus 로고    scopus 로고
    • Regulation of receptor function by cholesterol
    • Burger, K., G. Gimpl, and F. Fahrenholz. 2000. Regulation of receptor function by cholesterol. Cell Mol. Life Sci. 57:1577-1592.
    • (2000) Cell Mol. Life Sci , vol.57 , pp. 1577-1592
    • Burger, K.1    Gimpl, G.2    Fahrenholz, F.3
  • 14
    • 0025908807 scopus 로고
    • Protein-protein interactions in lymphocytic choriomeningitis virus
    • Burns, J. W., and M. J. Buchmeier. 1991. Protein-protein interactions in lymphocytic choriomeningitis virus. Virology 183:620-629.
    • (1991) Virology , vol.183 , pp. 620-629
    • Burns, J.W.1    Buchmeier, M.J.2
  • 15
    • 0037159920 scopus 로고    scopus 로고
    • Virion-associated cholesterol is critical for the maintenance of HIV-1 structure and infectivity
    • Campbell, S. M., S. M. Crowe, and J. Mak. 2002. Virion-associated cholesterol is critical for the maintenance of HIV-1 structure and infectivity. AIDS 16:2253-2261.
    • (2002) AIDS , vol.16 , pp. 2253-2261
    • Campbell, S.M.1    Crowe, S.M.2    Mak, J.3
  • 16
    • 0032892311 scopus 로고    scopus 로고
    • Involvement of the cytoskeleton in Junin virus multiplication
    • Candurra, N. A., M. J. Lago, L. Maskin, and E. B. Damonte. 1999. Involvement of the cytoskeleton in Junin virus multiplication. J. Gen. Virol. 80(Pt. 1):147-156.
    • (1999) J. Gen. Virol , vol.80 , Issue.PART. 1 , pp. 147-156
    • Candurra, N.A.1    Lago, M.J.2    Maskin, L.3    Damonte, E.B.4
  • 17
    • 34548170431 scopus 로고    scopus 로고
    • Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains
    • Capul, A. A., M. Perez, E. Burke, S. Kunz, M. J. Buchmeier, and J. C. de la Torre. 2007. Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains. J. Virol. 81:9451-9460.
    • (2007) J. Virol , vol.81 , pp. 9451-9460
    • Capul, A.A.1    Perez, M.2    Burke, E.3    Kunz, S.4    Buchmeier, M.J.5    de la Torre, J.C.6
  • 18
    • 0035910036 scopus 로고    scopus 로고
    • Center, R. J., P. Schuck, R. D. Leapman, L. O. Arthur, P. L. Earl, B. Moss, and J. Lebowitz. 2001. Oligomeric structure of virion-associated and soluble forms of the simian immunodeficiency virus envelope protein in the prefusion activated conformation. Proc. Natl. Acad. Sci. U. S. A. 98:14877-14882.
    • Center, R. J., P. Schuck, R. D. Leapman, L. O. Arthur, P. L. Earl, B. Moss, and J. Lebowitz. 2001. Oligomeric structure of virion-associated and soluble forms of the simian immunodeficiency virus envelope protein in the prefusion activated conformation. Proc. Natl. Acad. Sci. U. S. A. 98:14877-14882.
  • 20
    • 62749092549 scopus 로고    scopus 로고
    • Borna disease virus requires cholesterol in both cellular membrane and viral envelope for efficient cell entry
    • Clemente, R., A. de Parseval, M. Perez, and J. C. de la Torre. 2009. Borna disease virus requires cholesterol in both cellular membrane and viral envelope for efficient cell entry. J. Virol. 83:2655-2662.
    • (2009) J. Virol , vol.83 , pp. 2655-2662
    • Clemente, R.1    de Parseval, A.2    Perez, M.3    de la Torre, J.C.4
  • 21
    • 0345734205 scopus 로고    scopus 로고
    • Cholesterol removal by methyl-beta-cyclodextrin inhibits poliovirus entry
    • Danthi, P., and M. Chow. 2004. Cholesterol removal by methyl-beta-cyclodextrin inhibits poliovirus entry. J. Virol. 78:33-41.
    • (2004) J. Virol , vol.78 , pp. 33-41
    • Danthi, P.1    Chow, M.2
  • 22
    • 43049116526 scopus 로고    scopus 로고
    • Delgado, S., B. R. Erickson, R. Agudo, P. J. Blair, E. Vallejo, C. G. Albarino, J. Vargas, J. A. Comer, P. E. Rollin, T. G. Ksiazek, J. G. Olson, and S. T. Nichol. 2008. Chapare virus, a newly discovered arenavirus isolated from a fatal hemorrhagic fever case in Bolivia. PLoS Pathog. 4:e1000047.
    • Delgado, S., B. R. Erickson, R. Agudo, P. J. Blair, E. Vallejo, C. G. Albarino, J. Vargas, J. A. Comer, P. E. Rollin, T. G. Ksiazek, J. G. Olson, and S. T. Nichol. 2008. Chapare virus, a newly discovered arenavirus isolated from a fatal hemorrhagic fever case in Bolivia. PLoS Pathog. 4:e1000047.
  • 23
    • 44649199242 scopus 로고    scopus 로고
    • Plasma membrane cholesterol is required for efficient pseudorabies virus entry
    • Desplanques, A. S., H. J. Nauwynck, D. Vercauteren, T. Geens, and H. W. Favoreel. 2008. Plasma membrane cholesterol is required for efficient pseudorabies virus entry. Virology 376:339-345.
    • (2008) Virology , vol.376 , pp. 339-345
    • Desplanques, A.S.1    Nauwynck, H.J.2    Vercauteren, D.3    Geens, T.4    Favoreel, H.W.5
  • 24
    • 0028241840 scopus 로고
    • Acidic pH triggers LCMV membrane fusion activity and conformational change in the glycoprotein spike
    • Di Simone, C., M. A. Zandonatti, and M. J. Buchmeier. 1994. Acidic pH triggers LCMV membrane fusion activity and conformational change in the glycoprotein spike. Virology 198:455-465.
    • (1994) Virology , vol.198 , pp. 455-465
    • Di Simone, C.1    Zandonatti, M.A.2    Buchmeier, M.J.3
  • 25
    • 33746562281 scopus 로고    scopus 로고
    • Eichler, R., O. Lenz, W. Garten, and T. Strecker. 2006. The role of single N-glycans in proteolytic processing and cell surface transport of the Lassa virus glycoprotein GP-C. Virol. J. 3:41.
    • Eichler, R., O. Lenz, W. Garten, and T. Strecker. 2006. The role of single N-glycans in proteolytic processing and cell surface transport of the Lassa virus glycoprotein GP-C. Virol. J. 3:41.
  • 26
    • 0346242739 scopus 로고    scopus 로고
    • Identification of Lassa virus glycoprotein signal peptide as a transacting maturation factor
    • Eichler, R., O. Lenz, T. Strecker, M. Eickmann, H. D. Klenk, and W. Garten. 2003. Identification of Lassa virus glycoprotein signal peptide as a transacting maturation factor. EMBO Rep. 4:1084-1088.
    • (2003) EMBO Rep , vol.4 , pp. 1084-1088
    • Eichler, R.1    Lenz, O.2    Strecker, T.3    Eickmann, M.4    Klenk, H.D.5    Garten, W.6
  • 27
    • 1842478088 scopus 로고    scopus 로고
    • Lassa virus glycoprotein signal peptide displays a novel topology with an extended endoplasmic reticulum luminal region
    • Eichler, R., O. Lenz, T. Strecker, M. Eickmann, H. D. Klenk, and W. Garten. 2004. Lassa virus glycoprotein signal peptide displays a novel topology with an extended endoplasmic reticulum luminal region. J. Biol. Chem. 279: 12293-12299.
    • (2004) J. Biol. Chem , vol.279 , pp. 12293-12299
    • Eichler, R.1    Lenz, O.2    Strecker, T.3    Eickmann, M.4    Klenk, H.D.5    Garten, W.6
  • 28
    • 0037434923 scopus 로고    scopus 로고
    • Signal peptide of Lassa virus glycoprotein GP-C exhibits an unusual length
    • Eichler, R., O. Lenz, T. Strecker, and W. Garten. 2003. Signal peptide of Lassa virus glycoprotein GP-C exhibits an unusual length. FEBS Lett. 538: 203-206.
    • (2003) FEBS Lett , vol.538 , pp. 203-206
    • Eichler, R.1    Lenz, O.2    Strecker, T.3    Garten, W.4
  • 29
    • 1442299797 scopus 로고    scopus 로고
    • Characterization of the Lassa virus matrix protein Z: Electron microscopic study of virus-like particles and interaction with the nucleoprotein (NP)
    • Eichler, R., T. Strecker, L. Kolesnikova, J. ter Meulen, W. Weissenhorn, S. Becker, H. D. Klenk, W. Garten, and O. Lenz. 2004. Characterization of the Lassa virus matrix protein Z: electron microscopic study of virus-like particles and interaction with the nucleoprotein (NP). Virus Res. 100:249-255.
    • (2004) Virus Res , vol.100 , pp. 249-255
    • Eichler, R.1    Strecker, T.2    Kolesnikova, L.3    ter Meulen, J.4    Weissenhorn, W.5    Becker, S.6    Klenk, H.D.7    Garten, W.8    Lenz, O.9
  • 31
    • 33744935523 scopus 로고    scopus 로고
    • Identification of an N-terminal trimeric coiled-coil core within arenavirus glycoprotein 2 permits assignment to class I viral fusion proteins
    • Eschli, B., K. Quirin, A. Wepf, J. Weber, R. Zinkernagel, and H. Hengartner. 2006. Identification of an N-terminal trimeric coiled-coil core within arenavirus glycoprotein 2 permits assignment to class I viral fusion proteins. J. Virol. 80:5897-5907.
    • (2006) J. Virol , vol.80 , pp. 5897-5907
    • Eschli, B.1    Quirin, K.2    Wepf, A.3    Weber, J.4    Zinkernagel, R.5    Hengartner, H.6
  • 32
    • 0029556891 scopus 로고
    • Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin
    • Fass, D., and P. S. Kim. 1995. Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin. Curr. Biol. 5:1377-1383.
    • (1995) Curr. Biol , vol.5 , pp. 1377-1383
    • Fass, D.1    Kim, P.S.2
  • 33
    • 0142242233 scopus 로고    scopus 로고
    • Longlived signal peptide of lymphocytic choriomeningitis virus glycoprotein pGP-C
    • Froeschke, M., M. Basler, M. Groettrup, and B. Dobberstein. 2003. Longlived signal peptide of lymphocytic choriomeningitis virus glycoprotein pGP-C. J. Biol. Chem. 278:41914-41920.
    • (2003) J. Biol. Chem , vol.278 , pp. 41914-41920
    • Froeschke, M.1    Basler, M.2    Groettrup, M.3    Dobberstein, B.4
  • 34
    • 3142545672 scopus 로고    scopus 로고
    • The viral transmembrane superfamily: Possible divergence of Arenavirus and Filovirus glycoproteins from a common RNA virus ancestor
    • Gallaher, W. R., C. DiSimone, and M. J. Buchmeier. 2001. The viral transmembrane superfamily: possible divergence of Arenavirus and Filovirus glycoproteins from a common RNA virus ancestor. BMC Microbiol. 1:1.
    • (2001) BMC Microbiol , vol.1 , pp. 1
    • Gallaher, W.R.1    DiSimone, C.2    Buchmeier, M.J.3
  • 36
    • 0025031771 scopus 로고
    • Prediction of arenavirus fusion peptides on the basis of computer analysis of envelope protein sequences
    • Glushakova, S. E., I. S. Lukashevich, and L. A. Baratova. 1990. Prediction of arenavirus fusion peptides on the basis of computer analysis of envelope protein sequences. FEBS Lett. 269:145-147.
    • (1990) FEBS Lett , vol.269 , pp. 145-147
    • Glushakova, S.E.1    Lukashevich, I.S.2    Baratova, L.A.3
  • 37
    • 0036786465 scopus 로고    scopus 로고
    • Role for human immunodeficiency virus type 1 membrane cholesterol in viral internalization
    • Guyader, M., E. Kiyokawa, L. Abrami, P. Turelli, and D. Trono. 2002. Role for human immunodeficiency virus type 1 membrane cholesterol in viral internalization. J. Virol. 76:10356-10364.
    • (2002) J. Virol , vol.76 , pp. 10356-10364
    • Guyader, M.1    Kiyokawa, E.2    Abrami, L.3    Turelli, P.4    Trono, D.5
  • 38
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder, T., P. Scheiffele, P. Verkade, and K. Simons. 1998. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 141:929-942.
    • (1998) J. Cell Biol , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 40
    • 34247130572 scopus 로고    scopus 로고
    • Canine distemper virus infection requires cholesterol in the viral envelope
    • Imhoff, H., V. von Messling, G. Herrler, and L. Haas. 2007. Canine distemper virus infection requires cholesterol in the viral envelope. J. Virol. 81: 4158-4165.
    • (2007) J. Virol , vol.81 , pp. 4158-4165
    • Imhoff, H.1    von Messling, V.2    Herrler, G.3    Haas, L.4
  • 41
    • 0032529672 scopus 로고    scopus 로고
    • A core trimer of the paramyxovirus fusion protein: Parallels to influenza virus hemagglutinin and HIV-1 gp41
    • Joshi, S. B., R. E. Dutch, and R. A. Lamb. 1998. A core trimer of the paramyxovirus fusion protein: parallels to influenza virus hemagglutinin and HIV-1 gp41. Virology 248:20-34.
    • (1998) Virology , vol.248 , pp. 20-34
    • Joshi, S.B.1    Dutch, R.E.2    Lamb, R.A.3
  • 42
    • 0242351756 scopus 로고    scopus 로고
    • Cholesterol-dependent infection of Burkitt's lymphoma cell lines by Epstein-Barr virus
    • Katzman, R. B., and R. Longnecker. 2003. Cholesterol-dependent infection of Burkitt's lymphoma cell lines by Epstein-Barr virus. J. Gen. Virol. 84: 2987-2992.
    • (2003) J. Gen. Virol , vol.84 , pp. 2987-2992
    • Katzman, R.B.1    Longnecker, R.2
  • 43
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: More than one way to make a hairpin
    • Kielian, M., and F. A. Rey. 2006. Virus membrane-fusion proteins: more than one way to make a hairpin. Nat. Rev. Microbiol. 4:67-76.
    • (2006) Nat. Rev. Microbiol , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 44
    • 34547585371 scopus 로고    scopus 로고
    • Amino acids from both N-terminal hydrophobic regions of the Lassa virus envelope glycoprotein GP-2 are critical for pH-dependent membrane fusion and infectivity
    • Klewitz, C., H. D. Klenk, and J. ter Meulen. 2007. Amino acids from both N-terminal hydrophobic regions of the Lassa virus envelope glycoprotein GP-2 are critical for pH-dependent membrane fusion and infectivity. J. Gen. Virol. 88:2320-2328.
    • (2007) J. Gen. Virol , vol.88 , pp. 2320-2328
    • Klewitz, C.1    Klenk, H.D.2    ter Meulen, J.3
  • 45
    • 12144291075 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef activates p21-activated kinase via recruitment into lipid rafts
    • Krautkrämer, E., S. I. Giese, J. E. Gasteier, W. Muranyi, and O. T. Fackler. 2004. Human immunodeficiency virus type 1 Nef activates p21-activated kinase via recruitment into lipid rafts. J. Virol. 78:4085-4097.
    • (2004) J. Virol , vol.78 , pp. 4085-4097
    • Krautkrämer, E.1    Giese, S.I.2    Gasteier, J.E.3    Muranyi, W.4    Fackler, O.T.5
  • 46
    • 0030834125 scopus 로고    scopus 로고
    • Highefficiency incorporation of functional influenza virus glycoproteins into recombinant vesicular stomatitis viruses
    • Kretzschmar, E., L. Buonocore, M. J. Schnell, and J. K. Rose. 1997. Highefficiency incorporation of functional influenza virus glycoproteins into recombinant vesicular stomatitis viruses. J. Virol. 71:5982-5989.
    • (1997) J. Virol , vol.71 , pp. 5982-5989
    • Kretzschmar, E.1    Buonocore, L.2    Schnell, M.J.3    Rose, J.K.4
  • 47
    • 34548824835 scopus 로고    scopus 로고
    • Structural basis of viral invasion: Lessons from paramyxovirus F
    • Lamb, R. A., and T. S. Jardetzky. 2007. Structural basis of viral invasion: lessons from paramyxovirus F. Curr. Opin. Struct. Biol. 17:427-436.
    • (2007) Curr. Opin. Struct. Biol , vol.17 , pp. 427-436
    • Lamb, R.A.1    Jardetzky, T.S.2
  • 49
    • 34249654612 scopus 로고    scopus 로고
    • Genetic identification of Kodoko virus, a novel arenavirus of the African pigmy mouse (Mus Nannomys minutoides) in West Africa
    • Lecompte, E., J. ter Meulen, S. Emonet, S. Daffis, and R. N. Charrel. 2007. Genetic identification of Kodoko virus, a novel arenavirus of the African pigmy mouse (Mus Nannomys minutoides) in West Africa. Virology 364: 178-183.
    • (2007) Virology , vol.364 , pp. 178-183
    • Lecompte, E.1    ter Meulen, J.2    Emonet, S.3    Daffis, S.4    Charrel, R.N.5
  • 50
    • 47049107589 scopus 로고    scopus 로고
    • Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor
    • Lee, J. E., M. L. Fusco, A. J. Hessell, W. B. Oswald, D. R. Burton, and E. O. Saphire. 2008. Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature 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    Saphire, E.O.6
  • 51
    • 0034466514 scopus 로고    scopus 로고
    • Identification of a novel consensus sequence at the cleavage site of the Lassa virus glycoprotein
    • Lenz, O., J. ter Meulen, H. Feldmann, H. D. Klenk, and W. Garten. 2000. Identification of a novel consensus sequence at the cleavage site of the Lassa virus glycoprotein. J. Virol. 74:11418-11421.
    • (2000) J. Virol , vol.74 , pp. 11418-11421
    • Lenz, O.1    ter Meulen, J.2    Feldmann, H.3    Klenk, H.D.4    Garten, W.5
  • 52
    • 0035940409 scopus 로고    scopus 로고
    • The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P
    • Lenz, O., J. ter Meulen, H. D. Klenk, N. G. Seidah, and W. Garten. 2001. The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P. Proc. Natl. Acad. Sci. U. S. A. 98:12701-12705.
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , pp. 12701-12705
    • Lenz, O.1    ter Meulen, J.2    Klenk, H.D.3    Seidah, N.G.4    Garten, W.5
  • 53
    • 0034834457 scopus 로고    scopus 로고
    • Lipid rafts and HIV pathogenesis: Host membrane cholesterol is required for infection by HIV type 1
    • Liao, Z., L. M. Cimakasky, R. Hampton, D. H. Nguyen, and J. E. Hildreth. 2001. Lipid rafts and HIV pathogenesis: host membrane cholesterol is required for infection by HIV type 1. AIDS Res. Hum. Retroviruses 17:1009-1019.
    • (2001) AIDS Res. Hum. Retroviruses , vol.17 , pp. 1009-1019
    • Liao, Z.1    Cimakasky, L.M.2    Hampton, R.3    Nguyen, D.H.4    Hildreth, J.E.5
  • 54
    • 0029080687 scopus 로고
    • Formation of membrane domains created during the budding of vesicular stomatitis virus. A model for selective lipid and protein sorting in biological membranes
    • Luan, P., L. Yang, and M. Glaser. 1995. Formation of membrane domains created during the budding of vesicular stomatitis virus. A model for selective lipid and protein sorting in biological membranes. Biochemistry 34: 9874-9883.
    • (1995) Biochemistry , vol.34 , pp. 9874-9883
    • Luan, P.1    Yang, L.2    Glaser, M.3
  • 55
    • 68349099050 scopus 로고    scopus 로고
    • Maisa, A., U. Ströher, H. D. Klenk, W. Garten, and T. Strecker. 2009. Inhibition of lassa virus glycoprotein cleavage and multicycle replication by site 1 protease-adapted alpha(1)-antitrypsin variants. PLoS Negl. Trop. Dis. 3:e446.
    • Maisa, A., U. Ströher, H. D. Klenk, W. Garten, and T. Strecker. 2009. Inhibition of lassa virus glycoprotein cleavage and multicycle replication by site 1 protease-adapted alpha(1)-antitrypsin variants. PLoS Negl. Trop. Dis. 3:e446.
  • 56
    • 43949122204 scopus 로고    scopus 로고
    • West Nile virus entry requires cholesterol-rich membrane microdomains and is independent of alphavbeta3 integrin
    • Medigeshi, G. R., A. J. Hirsch, D. N. Streblow, J. Nikolich-Zugich, and J. A. Nelson. 2008. West Nile virus entry requires cholesterol-rich membrane microdomains and is independent of alphavbeta3 integrin. J. Virol. 82:5212-5219.
    • (2008) J. Virol , vol.82 , pp. 5212-5219
    • Medigeshi, G.R.1    Hirsch, A.J.2    Streblow, D.N.3    Nikolich-Zugich, J.4    Nelson, J.A.5
  • 57
    • 14744278960 scopus 로고    scopus 로고
    • Complementarity in the supramolecular design of arenaviruses and retroviruses revealed by electron cryomicroscopy and image analysis
    • Neuman, B. W., B. D. Adair, J. W. Burns, R. A. Milligan, M. J. Buchmeier, and M. Yeager. 2005. Complementarity in the supramolecular design of arenaviruses and retroviruses revealed by electron cryomicroscopy and image analysis. J. Virol. 79:3822-3830.
    • (2005) J. Virol , vol.79 , pp. 3822-3830
    • Neuman, B.W.1    Adair, B.D.2    Burns, J.W.3    Milligan, R.A.4    Buchmeier, M.J.5    Yeager, M.6
  • 58
    • 0037097585 scopus 로고    scopus 로고
    • Cholesterol is essential for macrophage inflammatory protein 1 beta binding and conformational integrity of CC chemokine receptor 5
    • Nguyen, D. H., and D. Taub. 2002. Cholesterol is essential for macrophage inflammatory protein 1 beta binding and conformational integrity of CC chemokine receptor 5. Blood 99:4298-4306.
    • (2002) Blood , vol.99 , pp. 4298-4306
    • Nguyen, D.H.1    Taub, D.2
  • 59
    • 0037090162 scopus 로고    scopus 로고
    • CXCR4 function requires membrane cholesterol: Implications for HIV infection
    • Nguyen, D. H., and D. Taub. 2002. CXCR4 function requires membrane cholesterol: implications for HIV infection. J. Immunol. 168:4121-4126.
    • (2002) J. Immunol , vol.168 , pp. 4121-4126
    • Nguyen, D.H.1    Taub, D.2
  • 60
    • 26944452885 scopus 로고    scopus 로고
    • Role of lipid rafts in virus replication
    • Ono, A., and E. O. Freed. 2005. Role of lipid rafts in virus replication. Adv. Virus Res. 64:311-358.
    • (2005) Adv. Virus Res , vol.64 , pp. 311-358
    • Ono, A.1    Freed, E.O.2
  • 61
    • 0242331609 scopus 로고    scopus 로고
    • The small RING finger protein Z drives arenavirus budding: Implications for antiviral strategies
    • Perez, M., R. C. Craven, and J. C. de la Torre. 2003. The small RING finger protein Z drives arenavirus budding: implications for antiviral strategies. Proc. Natl. Acad. Sci. U. S. A. 100:12978-12983.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 12978-12983
    • Perez, M.1    Craven, R.C.2    de la Torre, J.C.3
  • 62
    • 44749085794 scopus 로고    scopus 로고
    • Structures of vesicular stomatitis virus glycoprotein: Membrane fusion revisited
    • Roche, S., A. A. Albertini, J. Lepault, S. Bressanelli, and Y. Gaudin. 2008. Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited. Cell Mol. Life Sci. 65:1716-1728.
    • (2008) Cell Mol. Life Sci , vol.65 , pp. 1716-1728
    • Roche, S.1    Albertini, A.A.2    Lepault, J.3    Bressanelli, S.4    Gaudin, Y.5
  • 63
    • 44949106502 scopus 로고    scopus 로고
    • Site 1 protease is required for proteolytic processing of the glycoproteins of the South American hemorrhagic fever viruses Junin, Machupo, and Guanarito
    • Rojek, J. M., A. M. Lee, N. Nguyen, C. F. Spiropoulou, and S. Kunz. 2008. Site 1 protease is required for proteolytic processing of the glycoproteins of the South American hemorrhagic fever viruses Junin, Machupo, and Guanarito. J. Virol. 82:6045-6051.
    • (2008) J. Virol , vol.82 , pp. 6045-6051
    • Rojek, J.M.1    Lee, A.M.2    Nguyen, N.3    Spiropoulou, C.F.4    Kunz, S.5
  • 64
    • 38349137425 scopus 로고    scopus 로고
    • Cellular entry of lymphocytic choriomeningitis virus
    • Rojek, J. M., M. Perez, and S. Kunz. 2008. Cellular entry of lymphocytic choriomeningitis virus. J. Virol. 82:1505-1517.
    • (2008) J. Virol , vol.82 , pp. 1505-1517
    • Rojek, J.M.1    Perez, M.2    Kunz, S.3
  • 65
    • 0034467097 scopus 로고    scopus 로고
    • Glycoprotein exchange vectors based on vesicular stomatitis virus allow effective boosting and generation of neutralizing antibodies to a primary isolate of human immunodeficiency virus type 1
    • Rose, N. F., A. Roberts, L. Buonocore, and J. K. Rose. 2000. Glycoprotein exchange vectors based on vesicular stomatitis virus allow effective boosting and generation of neutralizing antibodies to a primary isolate of human immunodeficiency virus type 1. J. Virol. 74:10903-10910.
    • (2000) J. Virol , vol.74 , pp. 10903-10910
    • Rose, N.F.1    Roberts, A.2    Buonocore, L.3    Rose, J.K.4
  • 67
    • 34447313361 scopus 로고    scopus 로고
    • Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis
    • Saffarian, S., Y. Li, E. L. Elson, and L. J. Pike. 2007. Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis. Biophys. J. 93:1021-1031.
    • (2007) Biophys. J , vol.93 , pp. 1021-1031
    • Saffarian, S.1    Li, Y.2    Elson, E.L.3    Pike, L.J.4
  • 68
    • 0033593321 scopus 로고    scopus 로고
    • Influenza viruses select ordered lipid domains during budding from the plasma membrane
    • Scheiffele, P., A. Rietveld, T. Wilk, and K. Simons. 1999. Influenza viruses select ordered lipid domains during budding from the plasma membrane. J. Biol. Chem. 274:2038-2044.
    • (1999) J. Biol. Chem , vol.274 , pp. 2038-2044
    • Scheiffele, P.1    Rietveld, A.2    Wilk, T.3    Simons, K.4
  • 69
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele, P., M. G. Roth, and K. Simons. 1997. Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO J. 16:5501-5508.
    • (1997) EMBO J , vol.16 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 70
    • 36048983549 scopus 로고    scopus 로고
    • Signal peptide requirements for lymphocytic choriomeningitis virus glycoprotein C maturation and virus infectivity
    • Schrempf, S., M. Froeschke, T. Giroglou, D. von Laer, and B. Dobberstein. 2007. Signal peptide requirements for lymphocytic choriomeningitis virus glycoprotein C maturation and virus infectivity. J. Virol. 81:12515-12524.
    • (2007) J. Virol , vol.81 , pp. 12515-12524
    • Schrempf, S.1    Froeschke, M.2    Giroglou, T.3    von Laer, D.4    Dobberstein, B.5
  • 71
    • 33644597713 scopus 로고    scopus 로고
    • Role of non-raft cholesterol in lymphocytic choriomeningitis virus infection via alpha-dystroglycan
    • Shah, W. A., H. Peng, and S. Carbonetto. 2006. Role of non-raft cholesterol in lymphocytic choriomeningitis virus infection via alpha-dystroglycan. J. Gen. Virol. 87:673-678.
    • (2006) J. Gen. Virol , vol.87 , pp. 673-678
    • Shah, W.A.1    Peng, H.2    Carbonetto, S.3
  • 72
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and E. Ikonen. 1997. Functional rafts in cell membranes. Nature 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 73
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J. J., and D. C. Wiley. 2000. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69:531-569.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 75
    • 0141856160 scopus 로고    scopus 로고
    • Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles [corrected]
    • Strecker, T., R. Eichler, J. Meulen, W. Weissenhorn, H. D. Klenk, W. Garten, and O. Lenz. 2003. Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles [corrected]. J. Virol. 77:10700-10705.
    • (2003) J. Virol , vol.77 , pp. 10700-10705
    • Strecker, T.1    Eichler, R.2    Meulen, J.3    Weissenhorn, W.4    Klenk, H.D.5    Garten, W.6    Lenz, O.7
  • 76
    • 0242409482 scopus 로고    scopus 로고
    • Role for influenza virus envelope cholesterol in virus entry and infection
    • Sun, X., and G. R. Whittaker. 2003. Role for influenza virus envelope cholesterol in virus entry and infection. J. Virol. 77:12543-12551.
    • (2003) J. Virol , vol.77 , pp. 12543-12551
    • Sun, X.1    Whittaker, G.R.2
  • 77
    • 43949087845 scopus 로고    scopus 로고
    • Plasma membrane microdomains containing vesicular stomatitis virus M protein are separate from microdomains containing G protein and nucleocapsids
    • Swinteck, B. D., and D. S. Lyles. 2008. Plasma membrane microdomains containing vesicular stomatitis virus M protein are separate from microdomains containing G protein and nucleocapsids. J. Virol. 82:5536-5547.
    • (2008) J. Virol , vol.82 , pp. 5536-5547
    • Swinteck, B.D.1    Lyles, D.S.2
  • 78
    • 35748931458 scopus 로고    scopus 로고
    • Lipids as modulators of membrane fusion mediated by viral fusion proteins
    • Teissier, E., and E. I. Pecheur. 2007. Lipids as modulators of membrane fusion mediated by viral fusion proteins. Eur. Biophys. J. 36:887-899.
    • (2007) Eur. Biophys. J , vol.36 , pp. 887-899
    • Teissier, E.1    Pecheur, E.I.2
  • 79
    • 64249147324 scopus 로고    scopus 로고
    • Lipid rafts play an important role in the vesicular stomatitis virus life cycle
    • Wang, W., Y. J. Fu, Y. G. Zu, N. Wu, J. Reichling, and T. Efferth. 2009. Lipid rafts play an important role in the vesicular stomatitis virus life cycle. Arch. Virol. 154:595-600.
    • (2009) Arch. Virol , vol.154 , pp. 595-600
    • Wang, W.1    Fu, Y.J.2    Zu, Y.G.3    Wu, N.4    Reichling, J.5    Efferth, T.6
  • 80
    • 0032568634 scopus 로고    scopus 로고
    • The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil
    • Weissenhorn, W., L. J. Calder, S. A. Wharton, J. J. Skehel, and D. C. Wiley. 1998. The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil. Proc. Natl. Acad. Sci. U. S. A. 95:6032-6036.
    • (1998) Proc. Natl. Acad. Sci. U. S. A , vol.95 , pp. 6032-6036
    • Weissenhorn, W.1    Calder, L.J.2    Wharton, S.A.3    Skehel, J.J.4    Wiley, D.C.5
  • 81
    • 0029878665 scopus 로고    scopus 로고
    • The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide
    • Weissenhorn, W., S. A. Wharton, L. J. Calder, P. L. Earl, B. Moss, E. Aliprandis, J. J. Skehel, and D. C. Wiley. 1996. The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide. EMBO J. 15:1507-1514.
    • (1996) EMBO J , vol.15 , pp. 1507-1514
    • Weissenhorn, W.1    Wharton, S.A.2    Calder, L.J.3    Earl, P.L.4    Moss, B.5    Aliprandis, E.6    Skehel, J.J.7    Wiley, D.C.8
  • 83
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson, I. A., J. J. Skehel, and D. C. Wiley. 1981. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 289:366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 85
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • Yin, H. S., X. Wen, R. G. Paterson, R. A. Lamb, and T. S. Jardetzky. 2006. Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 439:38-44.
    • (2006) Nature , vol.439 , pp. 38-44
    • Yin, H.S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 86
    • 27744594720 scopus 로고    scopus 로고
    • Genetic analysis of heptad-repeat regions in the G2 fusion subunit of the Junin arenavirus envelope glycoprotein
    • York, J., S. S. Agnihothram, V. Romanowski, and J. H. Nunberg. 2005. Genetic analysis of heptad-repeat regions in the G2 fusion subunit of the Junin arenavirus envelope glycoprotein. Virology 343:267-274.
    • (2005) Virology , vol.343 , pp. 267-274
    • York, J.1    Agnihothram, S.S.2    Romanowski, V.3    Nunberg, J.H.4
  • 87
    • 4544266361 scopus 로고    scopus 로고
    • The signal peptide of the Junin arenavirus envelope glycoprotein is myristoylated and forms an essential subunit of the mature G1-G2 complex
    • York, J., V. Romanowski, M. Lu, and J. H. Nunberg. 2004. The signal peptide of the Junin arenavirus envelope glycoprotein is myristoylated and forms an essential subunit of the mature G1-G2 complex. J. Virol. 78:10783-10792.
    • (2004) J. Virol , vol.78 , pp. 10783-10792
    • York, J.1    Romanowski, V.2    Lu, M.3    Nunberg, J.H.4


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