메뉴 건너뛰기




Volumn 6, Issue 4, 2015, Pages

Haploid genetic screen reveals a profound and direct dependence on cholesterol for hantavirus membrane fusion

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; MATRIX PROTEIN; MEMBRANE BOUND TRANSCRIPTION FACTOR PEPTIDASE; MEMBRANE FUSION PROTEIN; STEROL REGULATORY ELEMENT BINDING PROTEIN; UNCLASSIFIED DRUG; CHOLESTEROL;

EID: 84940856868     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00801-15     Document Type: Article
Times cited : (91)

References (73)
  • 1
    • 0032980319 scopus 로고    scopus 로고
    • Spectrum of hantavirus infection: Hemorrhagic fever with renal syndrome and hantavirus pulmonary syndrome
    • Peters CJ, Simpson GL, Levy H. 1999. Spectrum of hantavirus infection: hemorrhagic fever with renal syndrome and hantavirus pulmonary syndrome. Annu Rev Med 50:531–545. http://dx.doi.org/10.1146/annurev.med.50.1.531
    • (1999) Annu Rev Med , vol.50 , pp. 531-545
    • Peters, C.J.1    Simpson, G.L.2    Levy, H.3
  • 2
    • 0031113395 scopus 로고    scopus 로고
    • Hantaviruses: A global disease problem
    • Schmaljohn C, Hjelle B. 1997. Hantaviruses: a global disease problem. Emerg Infect Dis 3:95–104. http://dx.doi.org/10.3201/eid0302.970202
    • (1997) Emerg Infect Dis , vol.3 , pp. 95-104
    • Schmaljohn, C.1    Hjelle, B.2
  • 4
    • 0000289028 scopus 로고    scopus 로고
    • Epidemiology and pathogenesis of hemorrhagic fever with renal syndrome
    • Elliott RM, Springer US, Boston, MA
    • Lee HW. 1996. Epidemiology and pathogenesis of hemorrhagic fever with renal syndrome, p 253–267. In Elliott RM (ed), The Bunyaviridae. Springer US, Boston, MA
    • (1996) The Bunyaviridae , pp. 253-267
    • Lee, H.W.1
  • 5
    • 81555228714 scopus 로고    scopus 로고
    • Hantavirus pulmonary syndrome
    • MacNeil A, Nichol ST, Spiropoulou CF. 2011. Hantavirus pulmonary syndrome. Virus Res 162:138–147. http://dx.doi.org/10.1016/j.virusres.2011.09.017
    • (2011) Virus Res , vol.162 , pp. 138-147
    • Macneil, A.1    Nichol, S.T.2    Spiropoulou, C.F.3
  • 7
    • 84896900051 scopus 로고    scopus 로고
    • Bunyaviridae
    • 6th ed. Lippincott Williams & Wilkins, Philadelphia, PA
    • Elliott RM, Schmaljohn CS. 2014. Bunyaviridae, p 1244–1282. In Fields virology, 6th ed. Lippincott Williams & Wilkins, Philadelphia, PA
    • (2014) Fields Virology , pp. 1244-1282
    • Elliott, R.M.1    Schmaljohn, C.S.2
  • 8
    • 0023092796 scopus 로고
    • Hantaan virus M RNA: Coding strategy, nucleotide sequence, and gene order
    • Schmaljohn CS, Schmaljohn AL, Dalrymple JM. 1987. Hantaan virus M RNA: coding strategy, nucleotide sequence, and gene order. Virology 157: 31–39. http://dx.doi.org/10.1016/0042-6822(87)90310-2
    • (1987) Virology , vol.157 , pp. 31-39
    • Schmaljohn, C.S.1    Schmaljohn, A.L.2    Dalrymple, J.M.3
  • 9
    • 0028008809 scopus 로고
    • Expression strategy of the M genome segment of Hantaan virus
    • Kamrud KI, Schmaljohn CS. 1994. Expression strategy of the M genome segment of Hantaan virus. Virus Res 31:109–121. http://dx.doi.org/10.1016/0168-1702(94)90074-4
    • (1994) Virus Res , vol.31 , pp. 109-121
    • Kamrud, K.I.1    Schmaljohn, C.S.2
  • 10
    • 0035950598 scopus 로고    scopus 로고
    • The Hantaan virus glycoprotein precursor is cleaved at the conserved pentapeptide WAASA
    • Löber C, Anheier B, Lindow S, Klenk HD, Feldmann H. 2001. The Hantaan virus glycoprotein precursor is cleaved at the conserved pentapeptide WAASA. Virology 289:224–229. http://dx.doi.org/10.1006/viro.2001.1171
    • (2001) Virology , vol.289 , pp. 224-229
    • Löber, C.1    Anheier, B.2    Lindow, S.3    Klenk, H.D.4    Feldmann, H.5
  • 11
    • 0026571713 scopus 로고
    • Coexpression of the membrane glycoproteins G1 and G2 of Hantaan virus is required for targeting to the Golgi complex
    • Ruusala A, Persson R, Schmaljohn CS, Pettersson RF. 1992. Coexpression of the membrane glycoproteins G1 and G2 of Hantaan virus is required for targeting to the Golgi complex. Virology 186:53–64. http://dx.doi.org/10.1016/0042-6822(92)90060-3
    • (1992) Virology , vol.186 , pp. 53-64
    • Ruusala, A.1    Persson, R.2    Schmaljohn, C.S.3    Pettersson, R.F.4
  • 12
    • 11344292598 scopus 로고    scopus 로고
    • Interactions and trafficking of Andes and sin Nombre hantavirus glycoproteins G1 and G2
    • Deyde VM, Rizvanov AA, Chase J, Otteson EW, St Jeor SC. 2005. Interactions and trafficking of Andes and sin Nombre hantavirus glycoproteins G1 and G2. Virology 331:307–315. http://dx.doi.org/10.1016/j.virol.2004.11.003
    • (2005) Virology , vol.331 , pp. 307-315
    • Deyde, V.M.1    Rizvanov, A.A.2    Chase, J.3    Otteson, E.W.4    St Jeor, S.C.5
  • 13
    • 0026625276 scopus 로고
    • Maturation of Hantaan virus glycoproteins G1 and G2
    • Antic D, Wright KE, Kang CY. 1992. Maturation of Hantaan virus glycoproteins G1 and G2. Virology 189:324–328. http://dx.doi.org/10.1016/0042-6822(92)90709-X
    • (1992) Virology , vol.189 , pp. 324-328
    • Antic, D.1    Wright, K.E.2    Kang, C.Y.3
  • 14
    • 84899148864 scopus 로고    scopus 로고
    • Hantavirus Gn and Gc envelope glycoproteins: Key structural units for virus cell entry and virus assembly
    • Cifuentes-Muñoz N, Salazar-Quiroz N, Tischler ND. 2014. Hantavirus Gn and Gc envelope glycoproteins: key structural units for virus cell entry and virus assembly. Viruses 6:1801–1822. http://dx.doi.org/10.3390/v6041801
    • (2014) Viruses , vol.6 , pp. 1801-1822
    • Cifuentes-Muñoz, N.1    Salazar-Quiroz, N.2    Tischler, N.D.3
  • 15
    • 0032499532 scopus 로고    scopus 로고
    • Mackow ER. 1998. +3 Integrins mediate the cellular entry of hantaviruses that cause respiratory failure
    • Gavrilovskaya IN, Shepley M, Shaw R, Ginsberg MH, Mackow ER. 1998. +3 Integrins mediate the cellular entry of hantaviruses that cause respiratory failure. Proc Natl Acad Sci U S A 95:7074–7079. http://dx.doi.org/10.1073/pnas.95.12.7074
    • Proc Natl Acad Sci U S A , vol.95 , pp. 7074-7079
    • Gavrilovskaya, I.N.1    Shepley, M.2    Shaw, R.3    Ginsberg, M.H.4
  • 16
    • 0032946942 scopus 로고    scopus 로고
    • Cellular entry of hantaviruses which cause hemorrhagic fever with renal syndrome is mediated by b3 integrins
    • Gavrilovskaya IN, Brown EJ, Ginsberg MH, Mackow ER. 1999. Cellular entry of hantaviruses which cause hemorrhagic fever with renal syndrome is mediated by b3 integrins. J Virol 73:3951–3959
    • (1999) J Virol , vol.73 , pp. 3951-3959
    • Gavrilovskaya, I.N.1    Brown, E.J.2    Ginsberg, M.H.3    Mackow, E.R.4
  • 17
    • 0034530465 scopus 로고    scopus 로고
    • Cellular receptors and hantavirus pathogenesis
    • Mackow ER, Gavrilovskaya IN. 2001. Cellular receptors and hantavirus pathogenesis. Curr Top Microbiol Immunol 256:91–115. http://dx.doi.org/10.1007/978-3-642-56753-7_6
    • (2001) Curr Top Microbiol Immunol , vol.256 , pp. 91-115
    • Mackow, E.R.1    Gavrilovskaya, I.N.2
  • 18
    • 42449162288 scopus 로고    scopus 로고
    • Hantavirus causing hemorrhagic fever with renal syndrome enters from the apical surface and requires decayaccelerating factor (DAF/CD55)
    • Krautkrämer E, Zeier M. 2008. Hantavirus causing hemorrhagic fever with renal syndrome enters from the apical surface and requires decayaccelerating factor (DAF/CD55). J Virol 82:4257–4264. http://dx.doi.org/10.1128/JVI.02210-07
    • (2008) J Virol , vol.82 , pp. 4257-4264
    • Krautkrämer, E.1    Zeier, M.2
  • 19
    • 54549083102 scopus 로고    scopus 로고
    • A hantavirus causing hemorrhagic fever with renal syndrome requires gC1qR/p32 for efficient cell binding and infection
    • Choi Y, Kwon YC, Kim SI, Park JM, Lee KH, Ahn BY. 2008. A hantavirus causing hemorrhagic fever with renal syndrome requires gC1qR/p32 for efficient cell binding and infection. Virology 381:178–183. http://dx.doi.org/10.1016/j.virol.2008.08.035
    • (2008) Virology , vol.381 , pp. 178-183
    • Choi, Y.1    Kwon, Y.C.2    Kim, S.I.3    Park, J.M.4    Lee, K.H.5    Ahn, B.Y.6
  • 26
    • 0032489460 scopus 로고    scopus 로고
    • Cleavage of sterol regulatory element-binding proteins (SREBPs) at site-1 requires interaction with SREBP cleavage-activating protein. Evidence from in vivo competition studies
    • Sakai J, Nohturfft A, Goldstein JL, Brown MS. 1998. Cleavage of sterol regulatory element-binding proteins (SREBPs) at site-1 requires interaction with SREBP cleavage-activating protein. Evidence from in vivo competition studies. J Biol Chem 273:5785–5793. http://dx.doi.org/10.1074/jbc.273.10.5785
    • (1998) J Biol Chem , vol.273 , pp. 5785-5793
    • Sakai, J.1    Nohturfft, A.2    Goldstein, J.L.3    Brown, M.S.4
  • 27
    • 0033613147 scopus 로고    scopus 로고
    • A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood
    • Brown MS, Goldstein JL. 1999. A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood. Proc Natl Acad Sci U S A 96:11041–11048. http://dx.doi.org/10.1073/pnas.96.20.11041
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11041-11048
    • Brown, M.S.1    Goldstein, J.L.2
  • 28
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: Regulation review of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • Brown MS, Goldstein JL. 1997. The SREBP pathway: regulation review of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell 89:331–340. http://dx.doi.org/10.1016/S0092-8674(00)80213-5
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 29
    • 0030604717 scopus 로고    scopus 로고
    • Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment
    • Sakai J, Duncan EA, Rawson RB, Hua X, Brown MS, Goldstein JL. 1996. Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment. Cell 85: 1037–1046. http://dx.doi.org/10.1016/S0092-8674(00)81304-5
    • (1996) Cell , vol.85 , pp. 1037-1046
    • Sakai, J.1    Duncan, E.A.2    Rawson, R.B.3    Hua, X.4    Brown, M.S.5    Goldstein, J.L.6
  • 30
    • 0029878960 scopus 로고    scopus 로고
    • Regulated cleavage of sterol regulatory element binding proteins requires sequences on both sides of the endoplasmic reticulum membrane
    • Hua X, Sakai J, Brown MS, Goldstein JL. 1996. Regulated cleavage of sterol regulatory element binding proteins requires sequences on both sides of the endoplasmic reticulum membrane. J Biol Chem 271: 10379–10384. http://dx.doi.org/10.1074/jbc.271.17.10379
    • (1996) J Biol Chem , vol.271 , pp. 10379-10384
    • Hua, X.1    Sakai, J.2    Brown, M.S.3    Goldstein, J.L.4
  • 34
    • 0037690744 scopus 로고    scopus 로고
    • Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses
    • Sieczkarski SB, Whittaker GR. 2003. Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses. Traffic 4:333–343. http://dx.doi.org/10.1034/j.1600-0854.2003.00090.x
    • (2003) Traffic , vol.4 , pp. 333-343
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 35
    • 80053437934 scopus 로고    scopus 로고
    • Old world arenaviruses enter the host cell via the multivesicular body and depend on the endosomal sorting complex required for transport
    • Pasqual G, Rojek JM, Masin M, Chatton J-Y, Kunz S. 2011. Old world arenaviruses enter the host cell via the multivesicular body and depend on the endosomal sorting complex required for transport. PLoS Pathog 7:e1002232. http://dx.doi.org/10.1371/journal.ppat.1002232
    • (2011) Plos Pathog , vol.7
    • Pasqual, G.1    Rojek, J.M.2    Masin, M.3    Chatton, J.-Y.4    Kunz, S.5
  • 36
    • 18744391355 scopus 로고    scopus 로고
    • The C-terminal domain of perfringolysin O is an essential cholesterol-binding unit targeting to cholesterol-rich microdomains
    • Shimada Y, Maruya M, Iwashita S, Ohno-Iwashita Y. 2002. The C-terminal domain of perfringolysin O is an essential cholesterol-binding unit targeting to cholesterol-rich microdomains. Eur J Biochem 269: 6195–6203. http://dx.doi.org/10.1046/j.1432-1033.2002.03338.x
    • (2002) Eur J Biochem , vol.269 , pp. 6195-6203
    • Shimada, Y.1    Maruya, M.2    Iwashita, S.3    Ohno-Iwashita, Y.4
  • 37
    • 0033215204 scopus 로고    scopus 로고
    • Failure to cleave sterol regulatory element-binding proteins (SREBPs) causes cholesterol auxotrophy in Chinese hamster ovary cells with genetic absence of SREBP cleavage-activating protein
    • Rawson RB, DeBose-Boyd R, Goldstein JL, Brown MS. 1999. Failure to cleave sterol regulatory element-binding proteins (SREBPs) causes cholesterol auxotrophy in Chinese hamster ovary cells with genetic absence of SREBP cleavage-activating protein. J Biol Chem 274:28549–28556. http://dx.doi.org/10.1074/jbc.274.40.28549
    • (1999) J Biol Chem , vol.274 , pp. 28549-28556
    • Rawson, R.B.1    Debose-Boyd, R.2    Goldstein, J.L.3    Brown, M.S.4
  • 38
    • 0032185770 scopus 로고    scopus 로고
    • Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells
    • Sakai J, Rawson RB, Espenshade PJ, Cheng D, Seegmiller AC, Goldstein JL, Brown MS. 1998. Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells. Mol Cell 2:505–514. http://dx.doi.org/10.1016/S1097-2765(00)80150-1
    • (1998) Mol Cell , vol.2 , pp. 505-514
    • Sakai, J.1    Rawson, R.B.2    Espenshade, P.J.3    Cheng, D.4    Seegmiller, A.C.5    Goldstein, J.L.6    Brown, M.S.7
  • 40
    • 41649095179 scopus 로고    scopus 로고
    • New and Old World hantaviruses differentially utilize host cytoskeletal components during their life cycles
    • Ramanathan HN, Jonsson CB. 2008. New and Old World hantaviruses differentially utilize host cytoskeletal components during their life cycles. Virology 374:138–150. http://dx.doi.org/10.1016/j.virol.2007.12.030
    • (2008) Virology , vol.374 , pp. 138-150
    • Ramanathan, H.N.1    Jonsson, C.B.2
  • 42
    • 0032930413 scopus 로고    scopus 로고
    • The cholesterol requirement for Sindbis virus entry and exit and characterization of a spike protein region involved in cholesterol dependence
    • Lu YE, Cassese T, Kielian M. 1999. The cholesterol requirement for Sindbis virus entry and exit and characterization of a spike protein region involved in cholesterol dependence. J Virol 73:4272–4278
    • (1999) J Virol , vol.73 , pp. 4272-4278
    • Lu, Y.E.1    Cassese, T.2    Kielian, M.3
  • 43
    • 78049487538 scopus 로고    scopus 로고
    • Alphavirus entry and membrane fusion
    • Kielian M, Chanel-Vos C, Liao M. 2010. Alphavirus entry and membrane fusion. Viruses 2:796–825. http://dx.doi.org/10.3390/v2040796
    • (2010) Viruses , vol.2 , pp. 796-825
    • Kielian, M.1    Chanel-Vos, C.2    Liao, M.3
  • 44
    • 46449111441 scopus 로고    scopus 로고
    • Mechanics of membrane fusion
    • Chernomordik LV, Kozlov MM. 2008. Mechanics of membrane fusion. Nat Struct Mol Biol 15:675–683. http://dx.doi.org/10.1038/nsmb.1455
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 675-683
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 45
    • 85017019017 scopus 로고    scopus 로고
    • Mechanisms of virus membrane fusion proteins
    • Kielian M. 2014. Mechanisms of virus membrane fusion proteins. Annu Rev Virol 1:171–189. http://dx.doi.org/10.1146/annurev-virology-031413-085521
    • (2014) Annu Rev Virol , vol.1 , pp. 171-189
    • Kielian, M.1
  • 47
    • 0026022952 scopus 로고
    • Cholesterol is required for infection by Semliki forest virus
    • Phalen T, Kielian M. 1991. Cholesterol is required for infection by Semliki forest virus. J Cell Biol 112:615–623. http://dx.doi.org/10.1083/jcb.112.4.615
    • (1991) J Cell Biol , vol.112 , pp. 615-623
    • Phalen, T.1    Kielian, M.2
  • 49
    • 77956225481 scopus 로고    scopus 로고
    • Development of a lentiviral vector system to study the role of the Andes virus glycoproteins
    • Cifuentes-Muñoz N, Darlix J-L, Tischler ND. 2010. Development of a lentiviral vector system to study the role of the Andes virus glycoproteins. Virus Res 153:29–35. http://dx.doi.org/10.1016/j.virusres.2010.07.001
    • (2010) Virus Res , vol.153 , pp. 29-35
    • Cifuentes-Muñoz, N.1    Darlix, J.-L.2    Tischler, N.D.3
  • 50
    • 36349027096 scopus 로고    scopus 로고
    • Crimean-Congo hemorrhagic fever virus glycoprotein processing by the endoprotease SKI-1/S1P is critical for virus infectivity
    • Bergeron E, Vincent MJ, Nichol ST. 2007. Crimean-Congo hemorrhagic fever virus glycoprotein processing by the endoprotease SKI-1/S1P is critical for virus infectivity. J Virol 81:13271–13276. http://dx.doi.org/10.1128/JVI.01647-07
    • (2007) J Virol , vol.81 , pp. 13271-13276
    • Bergeron, E.1    Vincent, M.J.2    Nichol, S.T.3
  • 51
    • 0035940409 scopus 로고    scopus 로고
    • The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P
    • Lenz O, ter Meulen J, Klenk HD, Seidah NG, Garten W. 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. http://dx.doi.org/10.1073/pnas.221447598
    • (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
  • 52
    • 0037372280 scopus 로고    scopus 로고
    • Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P
    • Beyer WR, Pöpplau D, Garten W, Laer von D, Lenz O. 2003. Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P. J Virol 77:2866–2872. http://dx.doi.org/10.1128/JVI.77.5.2866-2872.2003
    • (2003) J Virol , vol.77 , pp. 2866-2872
    • Beyer, W.R.1    Pöpplau, D.2    Garten, W.3    Laer Von, D.4    Lenz, O.5
  • 53
    • 33747335165 scopus 로고    scopus 로고
    • Roles of endogenously synthesized sterols in the endocytic pathway
    • Sugii S, Lin S, Ohgami N, Ohashi M, Chang CC, Chang T-Y. 2006. Roles of endogenously synthesized sterols in the endocytic pathway. J Biol Chem 281:23191–23206. http://dx.doi.org/10.1074/jbc.M603215200
    • (2006) J Biol Chem , vol.281 , pp. 23191-23206
    • Sugii, S.1    Lin, S.2    Ohgami, N.3    Ohashi, M.4    Chang, C.C.5    Chang, T.-Y.6
  • 54
    • 0345734205 scopus 로고    scopus 로고
    • Cholesterol removal by methyl-betacyclodextrin inhibits poliovirus entry
    • Danthi P, Chow M. 2004. Cholesterol removal by methyl-betacyclodextrin inhibits poliovirus entry. J Virol 78:33–41. http://dx.doi.org/10.1128/JVI.78.1.33-41.2004
    • (2004) J Virol , vol.78 , pp. 33-41
    • Danthi, P.1    Chow, M.2
  • 56
    • 38549173564 scopus 로고    scopus 로고
    • Membrane lipids: Where they are and how they behave
    • Van Meer G, Voelker DR, Feigenson GW. 2008. Membrane lipids: where they are and how they behave. Nat Rev Mol Cell Biol 9:112–124. http://dx.doi.org/10.1038/nrm2330
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 112-124
    • Van Meer, G.1    Voelker, D.R.2    Feigenson, G.W.3
  • 58
    • 0038620205 scopus 로고    scopus 로고
    • Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway
    • Möbius W, van Donselaar E, Ohno-Iwashita Y, Shimada Y, Heijnen HF, Slot JW, Geuze HJ. 2003. Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway. Traffic 4:222–231. http://dx.doi.org/10.1034/j.1600-0854.2003.00072.x
    • (2003) Traffic , vol.4 , pp. 222-231
    • Möbius, W.1    Van Donselaar, E.2    Ohno-Iwashita, Y.3    Shimada, Y.4    Heijnen, H.F.5    Slot, J.W.6    Geuze, H.J.7
  • 60
    • 27644471666 scopus 로고    scopus 로고
    • Hantavirus Gc glycoprotein: Evidence for a class II fusion protein
    • Tischler ND, Gonzalez A, Perez-Acle T, Rosemblatt M, Valenzuela PD. 2005. Hantavirus Gc glycoprotein: evidence for a class II fusion protein. J Gen Virol 86:2937–2947. http://dx.doi.org/10.1099/vir.0.81083-0
    • (2005) J Gen Virol , vol.86 , pp. 2937-2947
    • Tischler, N.D.1    Gonzalez, A.2    Perez-Acle, T.3    Rosemblatt, M.4    Valenzuela, P.D.5
  • 61
    • 0025150146 scopus 로고
    • Elastic deformation and failure of lipid bilayer membranes containing cholesterol
    • Needham D, Nunn RS. 1990. Elastic deformation and failure of lipid bilayer membranes containing cholesterol. Biophys J 58:997–1009. http://dx.doi.org/10.1016/S0006-3495(90)82444-9
    • (1990) Biophys J , vol.58 , pp. 997-1009
    • Needham, D.1    Nunn, R.S.2
  • 63
    • 0018089671 scopus 로고
    • Isolation of the etiologic agent of Korean hemorrhagic fever
    • Lee HW, Lee PW, Johnson KM. 1978. Isolation of the etiologic agent of Korean hemorrhagic fever. J Infect Dis 137:298–308. http://dx.doi.org/10.1093/infdis/137.3.298
    • (1978) J Infect Dis , vol.137 , pp. 298-308
    • Lee, H.W.1    Lee, P.W.2    Johnson, K.M.3
  • 65
    • 0035840798 scopus 로고    scopus 로고
    • A lethal disease model for hantavirus pulmonary syndrome
    • Hooper JW, Larsen T, Custer DM, Schmaljohn CS. 2001. A lethal disease model for hantavirus pulmonary syndrome. Virology 289:6–14. http://dx.doi.org/10.1006/viro.2001.1133
    • (2001) Virology , vol.289 , pp. 6-14
    • Hooper, J.W.1    Larsen, T.2    Custer, D.M.3    Schmaljohn, C.S.4
  • 66
    • 0032169169 scopus 로고    scopus 로고
    • The role of low pH and disulfide shuffling in the entry and fusion of Semliki Forest virus and Sindbis virus
    • Glomb-Reinmund S, Kielian M. 1998. The role of low pH and disulfide shuffling in the entry and fusion of Semliki Forest virus and Sindbis virus. Virology 248:372–381. http://dx.doi.org/10.1006/viro.1998.9275
    • (1998) Virology , vol.248 , pp. 372-381
    • Glomb-Reinmund, S.1    Kielian, M.2
  • 67
    • 72849133481 scopus 로고    scopus 로고
    • A forward genetic strategy reveals destabilizing mutations in the Ebolavirus glycoprotein that alter its protease dependence during cell entry
    • Wong AC, Sandesara RG, Mulherkar N, Whelan SP, Chandran K. 2010. A forward genetic strategy reveals destabilizing mutations in the Ebolavirus glycoprotein that alter its protease dependence during cell entry. J Virol 84:163–175. http://dx.doi.org/10.1128/JVI.01832-09
    • (2010) J Virol , vol.84 , pp. 163-175
    • Wong, A.C.1    Sandesara, R.G.2    Mulherkar, N.3    Whelan, S.P.4    Chandran, K.5
  • 68
    • 0029118831 scopus 로고
    • Efficient recovery of infectious vesicular stomatitis virus entirely from cDNA clones
    • Whelan SP, Ball LA, Barr JN, Wertz GT. 1995. Efficient recovery of infectious vesicular stomatitis virus entirely from cDNA clones. Proc Natl Acad Sci U S A 92:8388–8392. http://dx.doi.org/10.1073/pnas.92.18.8388
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8388-8392
    • Whelan, S.P.1    Ball, L.A.2    Barr, J.N.3    Wertz, G.T.4
  • 70
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran K, Sullivan NJ, Felbor U, Whelan SP, Cunningham JM. 2005. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308:1643–1645. http://dx.doi.org/10.1126/science.1110656
    • (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
  • 71
    • 0028812541 scopus 로고
    • Alteration of the myometrial plasma membrane cholesterol content with _-cyclodextrin modulates the binding affinity of the oxytocin receptor
    • Klein U, Gimpl G, Fahrenholz F. 1995. Alteration of the myometrial plasma membrane cholesterol content with _-cyclodextrin modulates the binding affinity of the oxytocin receptor. Biochemistry 34:13784–13793. http://dx.doi.org/10.1021/bi00042a009
    • (1995) Biochemistry , vol.34 , pp. 13784-13793
    • Klein, U.1    Gimpl, G.2    Fahrenholz, F.3
  • 73
    • 0033918941 scopus 로고    scopus 로고
    • Biochemical consequences of a mutation that controls the cholesterol dependence of Semliki Forest virus fusion
    • Chatterjee PK, Vashishtha M, Kielian M. 2000. Biochemical consequences of a mutation that controls the cholesterol dependence of Semliki Forest virus fusion. J Virol 74:1623–1631. http://dx.doi.org/10.1128/JVI.74.4.1623-1631.2000.
    • (2000) J Virol , vol.74 , pp. 1623-1631
    • Chatterjee, P.K.1    Vashishtha, M.2    Kielian, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.