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Volumn 10, Issue 6, 2006, Pages 443-454

Foamy virus, an original retroviral model;Les virus foamy, un modèle rétroviral original

Author keywords

Complex retrovirus; Foamy virus; Spumavirus

Indexed keywords

HEPATITIS B VIRUS; NONHUMAN; PREVALENCE; RETROPOSON; RETROVIRUS; REVIEW; SPUMA VIRUS; VIRUS INFECTION; VIRUS ISOLATION; VIRUS REPLICATION; VIRUS TRANSMISSION; YEAST;

EID: 33847295730     PISSN: 12678694     EISSN: None     Source Type: Journal    
DOI: 10.1684/vir.2006.0038     Document Type: Review
Times cited : (1)

References (115)
  • 1
    • 0001151220 scopus 로고
    • Propagation in tissue cultures of cytopathogenic agents from patients with measles
    • Enders JF, Peebles TC. Propagation in tissue cultures of cytopathogenic agents from patients with measles. Proc Soc Exp Biol Med 1954 ; 86 : 277-86.
    • (1954) Proc Soc Exp Biol Med , vol.86 , pp. 277-286
    • Enders, J.F.1    Peebles, T.C.2
  • 2
    • 0014686678 scopus 로고
    • Syncytium-forming agent isolated from domestic cats
    • Riggs JL, et al. Syncytium-forming agent isolated from domestic cats. Nature 1969 ; 222 : 1190-1.
    • (1969) Nature , vol.222 , pp. 1190-1191
    • Riggs, J.L.1
  • 3
  • 4
    • 0033994311 scopus 로고    scopus 로고
    • Isolation and characterization of an equine foamy virus
    • Tobaly-Tapiero J, et al. Isolation and characterization of an equine foamy virus. J Virol 2000 ; 74 : 4064-73.
    • (2000) J Virol , vol.74 , pp. 4064-4073
    • Tobaly-Tapiero, J.1
  • 6
    • 0033602562 scopus 로고    scopus 로고
    • Sites of simian foamy virus persistence in naturally infected African green monkeys : Latent provirus is ubiquitous, whereas viral replication is restricted to the oral mucosa
    • Falcone V, et al. Sites of simian foamy virus persistence in naturally infected African green monkeys : latent provirus is ubiquitous, whereas viral replication is restricted to the oral mucosa. Virology 1999 ; 257 : 7-14.
    • (1999) Virology , vol.257 , pp. 7-14
    • Falcone, V.1
  • 7
    • 33747106904 scopus 로고    scopus 로고
    • Modes of transmission and genetic diversity of foamy viruses in a Macaca tonkeana colony
    • Calattini S, et al. Modes of transmission and genetic diversity of foamy viruses in a Macaca tonkeana colony. Retrovirology 2006 ; 3 : 23.
    • (2006) Retrovirology , vol.3 , pp. 23
    • Calattini, S.1
  • 8
    • 0030664073 scopus 로고    scopus 로고
    • Characterization of new simian foamy viruses from African nonhuman primates
    • Broussard SR, et al. Characterization of new simian foamy viruses from African nonhuman primates. Virology 1997 ; 237 : 349-59.
    • (1997) Virology , vol.237 , pp. 349-359
    • Broussard, S.R.1
  • 9
    • 26444584377 scopus 로고    scopus 로고
    • Mucosal and systemic antibody responses in humans infected with simian foamy virus
    • Cummins JE, et al. Mucosal and systemic antibody responses in humans infected with simian foamy virus. J Virol 2005 ; 79 : 13186-9.
    • (2005) J Virol , vol.79 , pp. 13186-13189
    • Cummins, J.E.1
  • 10
    • 0015008389 scopus 로고
    • An unusual virus in cultures from a human nasopharyngeal carcinoma
    • Achong BG, et al. An unusual virus in cultures from a human nasopharyngeal carcinoma. J Natl Cancer Inst 1971 ; 46 : 299-307.
    • (1971) J Natl Cancer Inst , vol.46 , pp. 299-307
    • Achong, B.G.1
  • 11
    • 0015017188 scopus 로고
    • A new human virus in cultures from a nasopharyngeal carcinoma
    • Achong BG, Mansell PW, Epstein MA. A new human virus in cultures from a nasopharyngeal carcinoma. J Pathol 1971 ; 103 : 18.
    • (1971) J Pathol , vol.103 , pp. 18
    • Achong, B.G.1    Mansell, P.W.2    Epstein, M.A.3
  • 12
    • 0028360748 scopus 로고
    • Isolation, cloning, and sequencing of simian foamy viruses from chimpanzees (SFVcpz) : High homology to human foamy virus (HFV)
    • Herchenroder O, et al. Isolation, cloning, and sequencing of simian foamy viruses from chimpanzees (SFVcpz) : high homology to human foamy virus (HFV). Virology 1994 ; 201 : 187-99.
    • (1994) Virology , vol.201 , pp. 187-199
    • Herchenroder, O.1
  • 13
    • 0030926281 scopus 로고    scopus 로고
    • Simian foamy virus isolated from an accidentally infected human individual
    • Schweizer M, et al. Simian foamy virus isolated from an accidentally infected human individual. J Virol 1997 ; 71 : 4821-4.
    • (1997) J Virol , vol.71 , pp. 4821-4824
    • Schweizer, M.1
  • 14
    • 21144453476 scopus 로고    scopus 로고
    • Primate-to-human retroviral transmission in Asia
    • Jones-Engel L, et al. Primate-to-human retroviral transmission in Asia. Emerg Infect Dis 2005 ; 11 : 1028-35.
    • (2005) Emerg Infect Dis , vol.11 , pp. 1028-1035
    • Jones-Engel, L.1
  • 15
    • 0031924536 scopus 로고    scopus 로고
    • Identification of a human population infected with simian foamy viruses
    • Heneine W, et al. Identification of a human population infected with simian foamy viruses. Nat Med 1998 ; 4 : 403-7.
    • (1998) Nat Med , vol.4 , pp. 403-407
    • Heneine, W.1
  • 16
    • 0034639688 scopus 로고    scopus 로고
    • Simian foamy virus infection among zoo keepers
    • Sandstrom PA, et al. Simian foamy virus infection among zoo keepers. Lancet 2000 ; 355 : 551-2.
    • (2000) Lancet , vol.355 , pp. 551-552
    • Sandstrom, P.A.1
  • 17
    • 0037910269 scopus 로고    scopus 로고
    • Human infection with foamy viruses
    • Heneine W, et al. Human infection with foamy viruses. Curr Top Microbiol Immunol 2003 ; 277 : 181-96.
    • (2003) Curr Top Microbiol Immunol , vol.277 , pp. 181-196
    • Heneine, W.1
  • 18
    • 0026688887 scopus 로고
    • Viral DNA carried by human immunodeficiency virus type 1 virions
    • Lori F, et al. Viral DNA carried by human immunodeficiency virus type 1 virions. J Virol 1992 ; 66 : 5067-74.
    • (1992) J Virol , vol.66 , pp. 5067-5074
    • Lori, F.1
  • 19
    • 0026623001 scopus 로고
    • Partial reverse transcripts in virions from human immunodeficiency and murine leukemia viruses
    • Trono D. Partial reverse transcripts in virions from human immunodeficiency and murine leukemia viruses. J Virol 1992 ; 66 : 4893-900.
    • (1992) J Virol , vol.66 , pp. 4893-4900
    • Trono, D.1
  • 20
    • 0037744628 scopus 로고    scopus 로고
    • Biphasic DNA synthesis in spumaviruses
    • Delelis O, Saib A, Sonigo P. Biphasic DNA synthesis in spumaviruses. J Virol 2003 ; 77 : 8141-6.
    • (2003) J Virol , vol.77 , pp. 8141-8146
    • Delelis, O.1    Saib, A.2    Sonigo, P.3
  • 21
    • 0029869049 scopus 로고    scopus 로고
    • Human foamy virus replication, a pathway distinct from that of retroviruses and hepadnaviruses, 271, 1579-82
    • Yu SF, et al. Human foamy virus replication : a pathway distinct from that of retroviruses and hepadnaviruses. Science 1996 ; 271 : 1579-82.
    • (1996) Science
    • Yu, S.F.1
  • 22
    • 0030768753 scopus 로고    scopus 로고
    • Human foamy virus reverse transcription that occurs late in the viral replication cycle
    • Moebes A, et al. Human foamy virus reverse transcription that occurs late in the viral replication cycle. J Virol 1997 ; 71 : 7305-11.
    • (1997) J Virol , vol.71 , pp. 7305-7311
    • Moebes, A.1
  • 23
    • 0032932713 scopus 로고    scopus 로고
    • Evidence that the human foamy virus genome is DNA
    • Yu SF, Sullivan MD, Linial ML. Evidence that the human foamy virus genome is DNA. J Virol 1999 ; 73 : 1565-72.
    • (1999) J Virol , vol.73 , pp. 1565-1572
    • Yu, S.F.1    Sullivan, M.D.2    Linial, M.L.3
  • 24
  • 25
    • 0024121507 scopus 로고
    • An indicator gene to demonstrate intracellular transposition of defective retroviruses
    • Heidmann T, Heidmann O, Nicolas JF. An indicator gene to demonstrate intracellular transposition of defective retroviruses. Proc Natl Acad Sci USA 1988 ; 85 : 2219-23.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2219-2223
    • Heidmann, T.1    Heidmann, O.2    Nicolas, J.F.3
  • 26
    • 0025976299 scopus 로고
    • Retrotransposition of a mouse IAP sequence tagged with an indicator gene
    • Heidmann O, Heidmann T. Retrotransposition of a mouse IAP sequence tagged with an indicator gene. Cell 1991 ; 64 : 159-70.
    • (1991) Cell , vol.64 , pp. 159-170
    • Heidmann, O.1    Heidmann, T.2
  • 27
    • 0034601077 scopus 로고    scopus 로고
    • Efficient intracellular retrotransposition of an exogenous primate retrovirus genome
    • Heinkelein M, et al. Efficient intracellular retrotransposition of an exogenous primate retrovirus genome. EMBO J 2000 ; 19 : 3436-45.
    • (2000) EMBO J , vol.19 , pp. 3436-3445
    • Heinkelein, M.1
  • 28
    • 0026794096 scopus 로고
    • Mechanism of action of regulatory proteins encoded by complex retroviruses
    • Cullen BR. Mechanism of action of regulatory proteins encoded by complex retroviruses. Microbiol Rev 1992 ; 56 : 375-94.
    • (1992) Microbiol Rev , vol.56 , pp. 375-394
    • Cullen, B.R.1
  • 29
    • 0027304644 scopus 로고
    • Functional analysis of human foamy virus accessory reading frames
    • Baunach G, et al. Functional analysis of human foamy virus accessory reading frames. J Virol 1993 ; 67 : 5411-8.
    • (1993) J Virol , vol.67 , pp. 5411-5418
    • Baunach, G.1
  • 30
    • 0027297102 scopus 로고
    • Human foamy virus genome possesses an internal, Bel-1-dependent and functional promoter
    • Lochelt M, Muranyi W, Flugel RM. Human foamy virus genome possesses an internal, Bel-1-dependent and functional promoter. Proc Natl Acad Sci USA 1993 ; 90 : 7317-21.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7317-7321
    • Lochelt, M.1    Muranyi, W.2    Flugel, R.M.3
  • 31
    • 0028115839 scopus 로고
    • The human foamy virus internal promoter directs the expression of the functional Bel 1 transactivator and Bet protein early after infection
    • Lochelt M, Flugel RM, Aboud M. The human foamy virus internal promoter directs the expression of the functional Bel 1 transactivator and Bet protein early after infection. J Virol 1994 ; 68 : 638-45.
    • (1994) J Virol , vol.68 , pp. 638-645
    • Lochelt, M.1    Flugel, R.M.2    Aboud, M.3
  • 32
    • 0345363306 scopus 로고    scopus 로고
    • Molecular characterization of proteolytic processing of the Gag proteins of human spumavirus
    • Pfrepper KI, et al. Molecular characterization of proteolytic processing of the Gag proteins of human spumavirus. J Virol 1999 ; 73 : 7907-11.
    • (1999) J Virol , vol.73 , pp. 7907-7911
    • Pfrepper, K.I.1
  • 33
    • 0030775620 scopus 로고    scopus 로고
    • Carboxy-terminal cleavage of the human foamy virus Gag precursor molecule is an essential step in the viral life cycle
    • Enssle J, et al. Carboxy-terminal cleavage of the human foamy virus Gag precursor molecule is an essential step in the viral life cycle. J Virol 1997 ; 71 : 7312-7.
    • (1997) J Virol , vol.71 , pp. 7312-7317
    • Enssle, J.1
  • 34
    • 0032551378 scopus 로고    scopus 로고
    • The carboxy-terminal p3Gag domain of the human foamy virus Gag precursor is required for efficient virus infectivity
    • Zemba M, et al. The carboxy-terminal p3Gag domain of the human foamy virus Gag precursor is required for efficient virus infectivity. Virology 1998 ; 247 : 7-13.
    • (1998) Virology , vol.247 , pp. 7-13
    • Zemba, M.1
  • 35
    • 0029974928 scopus 로고    scopus 로고
    • A critical proteolytic cleavage site near the C terminus of the yeast retrotransposon Ty1 Gag protein
    • Merkulov GV, et al. A critical proteolytic cleavage site near the C terminus of the yeast retrotransposon Ty1 Gag protein. J Virol 1996 ; 70 : 5548-56.
    • (1996) J Virol , vol.70 , pp. 5548-5556
    • Merkulov, G.V.1
  • 36
    • 0035050188 scopus 로고    scopus 로고
    • Human foamy virus capsid formation requires an interaction domain in the N terminus of Gag
    • Tobaly-Tapiero J, et al. Human foamy virus capsid formation requires an interaction domain in the N terminus of Gag. J Virol 2001 ; 75 : 4367-75.
    • (2001) J Virol , vol.75 , pp. 4367-4375
    • Tobaly-Tapiero, J.1
  • 37
    • 0034947737 scopus 로고    scopus 로고
    • Identification of a conserved residue of foamy virus Gag required for intracellular capsid assembly
    • Eastman SW, Linial ML. Identification of a conserved residue of foamy virus Gag required for intracellular capsid assembly. J Virol 2001 ; 75 : 6857-64.
    • (2001) J Virol , vol.75 , pp. 6857-6864
    • Eastman, S.W.1    Linial, M.L.2
  • 38
    • 0032991707 scopus 로고    scopus 로고
    • Identification of a cytoplasmic targeting/retention signal in a retroviral Gag polyprotein
    • Choi G, et al. Identification of a cytoplasmic targeting/retention signal in a retroviral Gag polyprotein. J Virol 1999 ; 73 : 5431-7.
    • (1999) J Virol , vol.73 , pp. 5431-5437
    • Choi, G.1
  • 39
    • 0029961656 scopus 로고    scopus 로고
    • Foamy virus reverse transcriptase is expressed independently from the Gag protein
    • Enssle J, et al. Foamy virus reverse transcriptase is expressed independently from the Gag protein. Proc Natl Acad Sci USA 1996 ; 93 : 4137-41.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4137-4141
    • Enssle, J.1
  • 40
    • 0030273049 scopus 로고    scopus 로고
    • Expression of human foamy virus reverse transcriptase involves a spliced pol mRNA
    • Jordan I, et al. Expression of human foamy virus reverse transcriptase involves a spliced pol mRNA. Virology 1996 ; 224 : 314-9.
    • (1996) Virology , vol.224 , pp. 314-319
    • Jordan, I.1
  • 41
    • 0030053661 scopus 로고    scopus 로고
    • The human foamy virus pol gene is expressed as a Pro-Pol polyprotein and not as a Gag-Pol fusion protein
    • Lochelt M, Flugel RM. The human foamy virus pol gene is expressed as a Pro-Pol polyprotein and not as a Gag-Pol fusion protein. J Virol 1996 ; 70 : 1033-40.
    • (1996) J Virol , vol.70 , pp. 1033-1040
    • Lochelt, M.1    Flugel, R.M.2
  • 42
    • 0031816127 scopus 로고    scopus 로고
    • Molecular characterization of proteolytic processing of the Pol proteins of human foamy virus reveals novel features of the viral protease
    • Pfrepper KI, et al. Molecular characterization of proteolytic processing of the Pol proteins of human foamy virus reveals novel features of the viral protease. J Virol 1998 ; 72 : 7648-52.
    • (1998) J Virol , vol.72 , pp. 7648-7652
    • Pfrepper, K.I.1
  • 43
    • 0034977944 scopus 로고    scopus 로고
    • A particle-associated glycoprotein signal peptide essential for virus maturation and infectivity
    • Lindemann D, et al. A particle-associated glycoprotein signal peptide essential for virus maturation and infectivity. J Virol 2001 ; 75 : 5762-71.
    • (2001) J Virol , vol.75 , pp. 5762-5771
    • Lindemann, D.1
  • 44
    • 0041384017 scopus 로고    scopus 로고
    • Targeting of incoming retroviral Gag to the centrosome involves a direct interaction with the dynein light chain 8
    • Petit C, et al. Targeting of incoming retroviral Gag to the centrosome involves a direct interaction with the dynein light chain 8. J Cell Sci 2003 ; 116(Pt 16) : 3433-42.
    • (2003) J Cell Sci , vol.116 , Issue.PART 16 , pp. 3433-3442
    • Petit, C.1
  • 45
    • 1842404827 scopus 로고    scopus 로고
    • Nuclear targeting of incoming human foamy virus Gag proteins involves a centriolar step
    • Saib A, et al. Nuclear targeting of incoming human foamy virus Gag proteins involves a centriolar step. J Virol 1997 ; 71 : 1155-61.
    • (1997) J Virol , vol.71 , pp. 1155-1161
    • Saib, A.1
  • 46
    • 0031027096 scopus 로고    scopus 로고
    • Expression and maturation of human foamy virus Gag precursor polypeptides
    • Giron ML, et al. Expression and maturation of human foamy virus Gag precursor polypeptides. J Virol 1997 ; 71 : 1635-9.
    • (1997) J Virol , vol.71 , pp. 1635-1639
    • Giron, M.L.1
  • 47
    • 21644435326 scopus 로고    scopus 로고
    • Protease-dependent uncoating of a complex retrovirus
    • Lehmann-Che J, et al. Protease-dependent uncoating of a complex retrovirus. J Virol 2005 ; 79 : 9244-53.
    • (2005) J Virol , vol.79 , pp. 9244-9253
    • Lehmann-Che, J.1
  • 48
    • 0037664350 scopus 로고    scopus 로고
    • Specific in vitro cleavage of Mason-Pfizer monkey virus capsid protein : Evidence for a potential role of retroviral protease in early stages of infection
    • Rumlova M, et al. Specific in vitro cleavage of Mason-Pfizer monkey virus capsid protein : evidence for a potential role of retroviral protease in early stages of infection. Virology 2003 ; 310 : 310-8.
    • (2003) Virology , vol.310 , pp. 310-318
    • Rumlova, M.1
  • 49
    • 0027954403 scopus 로고
    • Antiviral activity of human immunodeficiency virus type 1 protease inhibitors in a single cycle of infection : Evidence for a role of protease in the early phase
    • Nagy K, et al. Antiviral activity of human immunodeficiency virus type 1 protease inhibitors in a single cycle of infection : evidence for a role of protease in the early phase. J Virol 1994 ; 68 : 757-65.
    • (1994) J Virol , vol.68 , pp. 757-765
    • Nagy, K.1
  • 50
    • 0028882189 scopus 로고
    • Cell cycle dependence of foamy retrovirus infection
    • Bieniasz PD, Weiss RA, McClure MO. Cell cycle dependence of foamy retrovirus infection. J Virol 1995 ; 69 : 7295-9.
    • (1995) J Virol , vol.69 , pp. 7295-7299
    • Bieniasz, P.D.1    Weiss, R.A.2    McClure, M.O.3
  • 51
    • 1242296984 scopus 로고    scopus 로고
    • Cell cycle requirements for transduction by foamy virus vectors compared to those of oncovirus and lentivirus vectors
    • Trobridge G, Russell DW. Cell cycle requirements for transduction by foamy virus vectors compared to those of oncovirus and lentivirus vectors. J Virol 2004 ; 78 : 2327-35.
    • (2004) J Virol , vol.78 , pp. 2327-2335
    • Trobridge, G.1    Russell, D.W.2
  • 52
    • 0027158091 scopus 로고
    • Integration of murine leukemia virus DNA depends on mitosis
    • Roe T, et al. Integration of murine leukemia virus DNA depends on mitosis. EMBO J 1993 ; 12 : 2099-108.
    • (1993) EMBO J , vol.12 , pp. 2099-2108
    • Roe, T.1
  • 53
    • 0026654682 scopus 로고
    • Human immunodeficiency virus infection of cells arrested in the cell cycle
    • Lewis P, Hensel M, Emerman M. Human immunodeficiency virus infection of cells arrested in the cell cycle. EMBO J 1992 ; 11 : 3053-8.
    • (1992) EMBO J , vol.11 , pp. 3053-3058
    • Lewis, P.1    Hensel, M.2    Emerman, M.3
  • 54
    • 31144434399 scopus 로고    scopus 로고
    • Transduction of nondividing human macrophages with gammaretrovirus-derived vectors
    • Jarrosson-Wuilleme L, et al. Transduction of nondividing human macrophages with gammaretrovirus-derived vectors. J Virol 2006 ; 80 : 1152-9.
    • (2006) J Virol , vol.80 , pp. 1152-1159
    • Jarrosson-Wuilleme, L.1
  • 55
    • 27244444559 scopus 로고    scopus 로고
    • TRIM family proteins : Retroviral restriction and antiviral defence
    • Nisole S, Stoye JP, Saib A. TRIM family proteins : retroviral restriction and antiviral defence. Nat Rev Microbiol 2005 ; 3 : 799-808.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 799-808
    • Nisole, S.1    Stoye, J.P.2    Saib, A.3
  • 56
    • 0348140581 scopus 로고    scopus 로고
    • DNA-cytosine deaminases : From antibody maturation to antiviral defense
    • Bhagwat AS. DNA-cytosine deaminases : from antibody maturation to antiviral defense. DNA Repair (Amst) 2004 ; 3 : 85-9.
    • (2004) DNA Repair (Amst) , vol.3 , pp. 85-89
    • Bhagwat, A.S.1
  • 57
    • 33144471153 scopus 로고    scopus 로고
    • Anti-viral RNA silencing : Do we look like plants?
    • Saumet A, Lecellier CH. Anti-viral RNA silencing : do we look like plants? Retrovirology 2006 ; 3 : 3.
    • (2006) Retrovirology , vol.3 , pp. 3
    • Saumet, A.1    Lecellier, C.H.2
  • 58
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Mangeat B, et al. Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 2003 ; 424 : 99-103.
    • (2003) Nature , vol.424 , pp. 99-103
    • Mangeat, B.1
  • 59
    • 0038681901 scopus 로고    scopus 로고
    • DNA deamination mediates innate immunity to retroviral infection
    • Harris RS, et al. DNA deamination mediates innate immunity to retroviral infection. Cell 2003 ; 113 : 803-9.
    • (2003) Cell , vol.113 , pp. 803-809
    • Harris, R.S.1
  • 60
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • Stopak K, et al. HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol Cell 2003 ; 12 : 591-601.
    • (2003) Mol Cell , vol.12 , pp. 591-601
    • Stopak, K.1
  • 61
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin M, et al. HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat Med 2003 ; 9 : 1398-403.
    • (2003) Nat Med , vol.9 , pp. 1398-1403
    • Marin, M.1
  • 62
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle A, et al. Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J Biol Chem 2004 ; 279 : 7792-8.
    • (2004) J Biol Chem , vol.279 , pp. 7792-7798
    • Mehle, A.1
  • 63
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • Sheehy AM, Gaddis NC, Malim MH. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat Med 2003 ; 9 : 1404-7.
    • (2003) Nat Med , vol.9 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 64
    • 13844270834 scopus 로고    scopus 로고
    • Complementary function of the two catalytic domains of APOBEC3G
    • Navarro F, et al. Complementary function of the two catalytic domains of APOBEC3G. Virology 2005 ; 333 : 374-86.
    • (2005) Virology , vol.333 , pp. 374-386
    • Navarro, F.1
  • 65
    • 17144384021 scopus 로고    scopus 로고
    • Inhibition of a yeast LTR retrotransposon by human APOBEC3 cytidine deaminases
    • Dutko JA, et al. Inhibition of a yeast LTR retrotransposon by human APOBEC3 cytidine deaminases. Curr Biol 2005 ; 15 : 661-6.
    • (2005) Curr Biol , vol.15 , pp. 661-666
    • Dutko, J.A.1
  • 66
    • 13444282074 scopus 로고    scopus 로고
    • APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses
    • Esnault C, et al. APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses. Nature 2005 ; 433 : 430-3.
    • (2005) Nature , vol.433 , pp. 430-433
    • Esnault, C.1
  • 67
    • 14244254668 scopus 로고    scopus 로고
    • G to A hypermutation of hepatitis B virus
    • Noguchi C, et al. G to A hypermutation of hepatitis B virus. Hepatology 2005 ; 4 : 626-33.
    • (2005) Hepatology , vol.4 , pp. 626-633
    • Noguchi, C.1
  • 68
    • 21644460676 scopus 로고    scopus 로고
    • Foamy virus Bet proteins function as novel inhibitors of the APOBEC3 family of innate antiretroviral defense factors
    • Russell RA, et al. Foamy virus Bet proteins function as novel inhibitors of the APOBEC3 family of innate antiretroviral defense factors. J Virol 2005 ; 79 : 8724-31.
    • (2005) J Virol , vol.79 , pp. 8724-8731
    • Russell, R.A.1
  • 69
    • 30344450447 scopus 로고    scopus 로고
    • Restriction of Foamy Viruses by APOBEC cytidine deaminases
    • Delebecque F, et al. Restriction of Foamy Viruses by APOBEC cytidine deaminases. J Virol 2006 ; 80 : 605-14.
    • (2006) J Virol , vol.80 , pp. 605-614
    • Delebecque, F.1
  • 70
    • 20344379929 scopus 로고    scopus 로고
    • The antiretroviral activity of APOBEC3 is inhibited by the foamy virus accessory Bet protein
    • Lochelt M, et al. The antiretroviral activity of APOBEC3 is inhibited by the foamy virus accessory Bet protein. Proc Natl Acad Sci USA 2005 ; 102 : 7982-7.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 7982-7987
    • Lochelt, M.1
  • 71
    • 27444434644 scopus 로고    scopus 로고
    • APOBEC3G & HTLV1 : Inhibition without deamination
    • Strebel K. APOBEC3G & HTLV1 : inhibition without deamination. Retrovirology 2005 ; 2 : 37.
    • (2005) Retrovirology , vol.2 , pp. 37
    • Strebel, K.1
  • 72
    • 0035905766 scopus 로고    scopus 로고
    • Role for a bidentate ribonuclease in the initiation step of RNA interference
    • Bernstein E, et al. Role for a bidentate ribonuclease in the initiation step of RNA interference. Nature 2001 ; 409 : 363-6.
    • (2001) Nature , vol.409 , pp. 363-366
    • Bernstein, E.1
  • 73
    • 0033615491 scopus 로고    scopus 로고
    • A species of small antisense RNA in posttranscriptional gene silencing in plants
    • Hamilton AJ, Baulcombe DC. A species of small antisense RNA in posttranscriptional gene silencing in plants. Science 1999 ; 286 : 950-2.
    • (1999) Science , vol.286 , pp. 950-952
    • Hamilton, A.J.1    Baulcombe, D.C.2
  • 74
    • 22144472969 scopus 로고    scopus 로고
    • MicroRNAs directing siRNA biogenesis
    • Bartel B. MicroRNAs directing siRNA biogenesis. Nat Struct Mol Biol 2005 ; 12 : 569-71.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 569-571
    • Bartel, B.1
  • 75
    • 0347906099 scopus 로고    scopus 로고
    • Towards a complete description of the microRNA complement of animal genomes
    • Brennecke J, Cohen SM. Towards a complete description of the microRNA complement of animal genomes. Genome Biol 2003 ; 4 : 228.
    • (2003) Genome Biol , vol.4 , pp. 228
    • Brennecke, J.1    Cohen, S.M.2
  • 76
    • 17644363376 scopus 로고    scopus 로고
    • A cellular microRNA mediates antiviral defense in human cells
    • Lecellier CH, et al. A cellular microRNA mediates antiviral defense in human cells. Science 2005 ; 308 : 557-60.
    • (2005) Science , vol.308 , pp. 557-560
    • Lecellier, C.H.1
  • 77
    • 3242749856 scopus 로고    scopus 로고
    • Crystal structure of p19 : A universal suppressor of RNA silencing
    • Baulcombe DC, Molnar A. Crystal structure of p19 : a universal suppressor of RNA silencing. Trends Biochem Sci 2004 ; 29 : 279-81.
    • (2004) Trends Biochem Sci , vol.29 , pp. 279-281
    • Baulcombe, D.C.1    Molnar, A.2
  • 78
    • 1842843155 scopus 로고    scopus 로고
    • Human influenza virus NS1 protein enhances viral pathogenicity and acts as an RNA silencing suppressor in plants
    • Delgadillo MO, et al. Human influenza virus NS1 protein enhances viral pathogenicity and acts as an RNA silencing suppressor in plants. J Gen Virol 2004 ; 85 : 993-9.
    • (2004) J Gen Virol , vol.85 , pp. 993-999
    • Delgadillo, M.O.1
  • 79
    • 1842832222 scopus 로고    scopus 로고
    • The influenza A virus NS1 protein binds small interfering RNAs and suppresses RNA silencing in plants
    • Bucher E, et al. The influenza A virus NS1 protein binds small interfering RNAs and suppresses RNA silencing in plants. J Gen Virol 2004 ; 85 : 983-91.
    • (2004) J Gen Virol , vol.85 , pp. 983-991
    • Bucher, E.1
  • 80
    • 10744225684 scopus 로고    scopus 로고
    • Interferon antagonist proteins of influenza and vaccinia viruses are suppressors of RNA silencing, 101, 1350-5
    • Li WX, et al. Interferon antagonist proteins of influenza and vaccinia viruses are suppressors of RNA silencing. Proc Natl Acad Sci USA 2004 ; 101 : 1350-5.
    • (2004) Proc Natl Acad Sci USA
    • Li, W.X.1
  • 81
    • 33744476400 scopus 로고    scopus 로고
    • Cullen BR. Is RNA interference involved in intrinsic antiviral immunity in mammals? Nat Immunol 2006 ; 7 : 563-7.
    • Cullen BR. Is RNA interference involved in intrinsic antiviral immunity in mammals? Nat Immunol 2006 ; 7 : 563-7.
  • 82
    • 0037162715 scopus 로고    scopus 로고
    • HIV-1 integration in the human genome favors active genes and local hotspots
    • Schroder AR, et al. HIV-1 integration in the human genome favors active genes and local hotspots. Cell 2002 ; 110 : 521-9.
    • (2002) Cell , vol.110 , pp. 521-529
    • Schroder, A.R.1
  • 83
    • 0037841763 scopus 로고    scopus 로고
    • Transcription start regions in the human genome are favored targets for MLV integration
    • Wu X, et al. Transcription start regions in the human genome are favored targets for MLV integration. Science 2003 ; 300 : 1749-51.
    • (2003) Science , vol.300 , pp. 1749-1751
    • Wu, X.1
  • 84
    • 0034329187 scopus 로고    scopus 로고
    • Basis of HTLV type 1 target site selection
    • Leclercq I, et al. Basis of HTLV type 1 target site selection. AIDS Res Hum Retroviruses 2000 ; 16 : 1653-9.
    • (2000) AIDS Res Hum Retroviruses , vol.16 , pp. 1653-1659
    • Leclercq, I.1
  • 85
    • 28144462457 scopus 로고    scopus 로고
    • Genome-wide analysis of retroviral DNA integration
    • Bushman F, et al. Genome-wide analysis of retroviral DNA integration. Nat Rev Microbiol 2005 ; 3 : 848-58.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 848-858
    • Bushman, F.1
  • 86
    • 33847256218 scopus 로고    scopus 로고
    • Insights into integration site selection : Application for vector design
    • Thebault S, ed, Nova Science Publishers
    • Lehmann-Che J. Insights into integration site selection : application for vector design. In : Thebault S, ed. Progress in virus research. Nova Science Publishers, 2005.
    • (2005) Progress in virus research
    • Lehmann-Che, J.1
  • 87
    • 19344375031 scopus 로고    scopus 로고
    • Retroviral DNA integration : ASLV, HIV, and MLV show distinct target site preferences
    • Mitchell RS, et al. Retroviral DNA integration : ASLV, HIV, and MLV show distinct target site preferences. PLoS Biol 2004 ; 2 : E234.
    • (2004) PLoS Biol , vol.2
    • Mitchell, R.S.1
  • 88
    • 31944444349 scopus 로고    scopus 로고
    • Foamy virus vector integration sites in normal human cells
    • Trobridge GD, et al. Foamy virus vector integration sites in normal human cells. Proc Natl Acad Sci USA 2006 ; 103 : 1498-503.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 1498-1503
    • Trobridge, G.D.1
  • 89
    • 33646161948 scopus 로고    scopus 로고
    • Genome-wide mapping of foamy virus vector integrations into a human cell line
    • Nowrouzi A, et al. Genome-wide mapping of foamy virus vector integrations into a human cell line. J Gen Virol 2006 ; 87 : 1339-47.
    • (2006) J Gen Virol , vol.87 , pp. 1339-1347
    • Nowrouzi, A.1
  • 90
    • 0038286220 scopus 로고    scopus 로고
    • Integration by design
    • Sandmeyer S. Integration by design. Proc Natl Acad Sci USA 2003 ; 100 : 5586-8.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5586-5588
    • Sandmeyer, S.1
  • 91
    • 4143091487 scopus 로고    scopus 로고
    • Role of the C terminus of foamy virus Gag in RNA packaging and Pol expression
    • Stenbak CR, Linial ML. Role of the C terminus of foamy virus Gag in RNA packaging and Pol expression. J Virol 2004 ; 78 : 9423-30.
    • (2004) J Virol , vol.78 , pp. 9423-9430
    • Stenbak, C.R.1    Linial, M.L.2
  • 92
    • 0035942236 scopus 로고    scopus 로고
    • RNA is a structural element in retrovirus particles
    • Muriaux D, et al. RNA is a structural element in retrovirus particles. Proc Natl Acad Sci USA 2001 ; 98 : 5246-51.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5246-5251
    • Muriaux, D.1
  • 93
    • 0035123571 scopus 로고    scopus 로고
    • Characterization of Rous sarcoma virus Gag particles assembled in vitro
    • Yu F, et al. Characterization of Rous sarcoma virus Gag particles assembled in vitro. J Virol 2001 ; 75 : 2753-64.
    • (2001) J Virol , vol.75 , pp. 2753-2764
    • Yu, F.1
  • 94
    • 0028247576 scopus 로고
    • Retroviral RNA packaging : A review
    • Rein A. Retroviral RNA packaging : a review. Arch Virol Suppl 1994 ; 9 : 513-22.
    • (1994) Arch Virol Suppl , vol.9 , pp. 513-522
    • Rein, A.1
  • 95
    • 0346688653 scopus 로고    scopus 로고
    • Nucleocapsid-RNA interactions are essential to structural stability but not to assembly of retroviruses
    • Wang SW, Noonan K, Aldovini A. Nucleocapsid-RNA interactions are essential to structural stability but not to assembly of retroviruses. J Virol 2004 ; 78 : 716-23.
    • (2004) J Virol , vol.78 , pp. 716-723
    • Wang, S.W.1    Noonan, K.2    Aldovini, A.3
  • 96
    • 0034107720 scopus 로고    scopus 로고
    • Complex effects of deletions in the 5′ untranslated region of primate foamy virus on viral gene expression and RNA packaging
    • Heinkelein M, et al. Complex effects of deletions in the 5′ untranslated region of primate foamy virus on viral gene expression and RNA packaging. J Virol 2000 ; 74 : 3141-8.
    • (2000) J Virol , vol.74 , pp. 3141-3148
    • Heinkelein, M.1
  • 97
    • 0004220419 scopus 로고    scopus 로고
    • Synthesis, assembly and processing of viral proteins
    • Coffin JM, ed, Cold Sping Harbor Laboratory Press
    • Swanstrom R, Wills JW. Synthesis, assembly and processing of viral proteins. In : Coffin JM, ed. Retroviruses, SHHaHEV. Cold Sping Harbor Laboratory Press, 1997.
    • (1997) Retroviruses, SHHaHEV
    • Swanstrom, R.1    Wills, J.W.2
  • 98
    • 0031902657 scopus 로고    scopus 로고
    • Characterization of a cis-acting sequence in the Pol region required to transfer human foamy virus vectors
    • Heinkelein M, et al. Characterization of a cis-acting sequence in the Pol region required to transfer human foamy virus vectors. J. Virol 1998 ; 72 : 6307-14.
    • (1998) J. Virol , vol.72 , pp. 6307-6314
    • Heinkelein, M.1
  • 99
    • 0036776597 scopus 로고    scopus 로고
    • Pregenomic RNA is required for efficient incorporation of pol polyprotein into foamy virus capsids
    • Heinkelein M, et al. Pregenomic RNA is required for efficient incorporation of pol polyprotein into foamy virus capsids. J Virol 2002 ; 76 : 10069-73.
    • (2002) J Virol , vol.76 , pp. 10069-10073
    • Heinkelein, M.1
  • 100
    • 18744386950 scopus 로고    scopus 로고
    • RNA and protein requirements for incorporation of the Pol protein into foamy virus particles
    • Peters K, et al. RNA and protein requirements for incorporation of the Pol protein into foamy virus particles. J Virol 2005 ; 79 : 7005-13.
    • (2005) J Virol , vol.79 , pp. 7005-7013
    • Peters, K.1
  • 101
    • 27344459767 scopus 로고    scopus 로고
    • Determination of the relative amounts of Gag and Pol proteins in foamy virus particles
    • Cartellieri M, et al. Determination of the relative amounts of Gag and Pol proteins in foamy virus particles. Retrovirology 2005 ; 2 : 44.
    • (2005) Retrovirology , vol.2 , pp. 44
    • Cartellieri, M.1
  • 102
    • 0032864436 scopus 로고    scopus 로고
    • An endoplasmic reticulum retrieval signal partitions human foamy virus maturation to intracytoplasmic membranes
    • Goepfert PA, et al. An endoplasmic reticulum retrieval signal partitions human foamy virus maturation to intracytoplasmic membranes. J Virol 1999 ; 73 : 7210-7.
    • (1999) J Virol , vol.73 , pp. 7210-7217
    • Goepfert, P.A.1
  • 103
    • 0031060171 scopus 로고    scopus 로고
    • A sorting motif localizes the foamy virus glycoprotein to the endoplasmic reticulum
    • Goepfert PA, et al. A sorting motif localizes the foamy virus glycoprotein to the endoplasmic reticulum. J Virol 1997 ; 71 : 778-84.
    • (1997) J Virol , vol.71 , pp. 778-784
    • Goepfert, P.A.1
  • 104
    • 23944440453 scopus 로고    scopus 로고
    • The requirements and mechanism for capsid assembly and budding of bovine foamy virus
    • Kong XH, et al. The requirements and mechanism for capsid assembly and budding of bovine foamy virus. Arch Virol 2005 ; 150 : 1677-84.
    • (2005) Arch Virol , vol.150 , pp. 1677-1684
    • Kong, X.H.1
  • 105
    • 0034864546 scopus 로고    scopus 로고
    • Specific interaction of a novel foamy virus Env leader protein with the N-terminal Gag domain
    • Wilk T, et al. Specific interaction of a novel foamy virus Env leader protein with the N-terminal Gag domain. J Virol 2001 ; 75 : 7995-8007.
    • (2001) J Virol , vol.75 , pp. 7995-8007
    • Wilk, T.1
  • 106
    • 0038678627 scopus 로고    scopus 로고
    • Features of the Env leader protein and the N-terminal Gag domain of feline foamy virus important for virus morphogenesis
    • Geiselhart V, et al. Features of the Env leader protein and the N-terminal Gag domain of feline foamy virus important for virus morphogenesis. Virology 2003 ; 310 : 235-44.
    • (2003) Virology , vol.310 , pp. 235-244
    • Geiselhart, V.1
  • 107
    • 0032775896 scopus 로고    scopus 로고
    • Proteolytic activity, the carboxy terminus of Gag, and the primer binding site are not required for Pol incorporation into foamy virus particles
    • Baldwin DN, Liniam ML. Proteolytic activity, the carboxy terminus of Gag, and the primer binding site are not required for Pol incorporation into foamy virus particles. J Virol 1999 ; 73 : 6387-93.
    • (1999) J Virol , vol.73 , pp. 6387-6393
    • Baldwin, D.N.1    Liniam, M.L.2
  • 108
    • 0031931402 scopus 로고    scopus 로고
    • Foamy virus particle formation
    • Fischer N, et al. Foamy virus particle formation. J Virol 1998 ; 72 : 1610-5.
    • (1998) J Virol , vol.72 , pp. 1610-1615
    • Fischer, N.1
  • 109
    • 0032976195 scopus 로고    scopus 로고
    • Foamy virus capsids require the cognate envelope protein for particle export
    • Pietschmann T, et al. Foamy virus capsids require the cognate envelope protein for particle export. J Virol 1999 ; 73 : 2613-21.
    • (1999) J Virol , vol.73 , pp. 2613-2621
    • Pietschmann, T.1
  • 110
    • 0031968819 scopus 로고    scopus 로고
    • The roles of Pol and Env in the assembly pathway of human foamy virus
    • Baldwin DN, Linial ML. The roles of Pol and Env in the assembly pathway of human foamy virus. J Virol 1998 ; 72 : 3658-65.
    • (1998) J Virol , vol.72 , pp. 3658-3665
    • Baldwin, D.N.1    Linial, M.L.2
  • 111
    • 0037320007 scopus 로고    scopus 로고
    • Foamy virus envelope glycoprotein is sufficient for particle budding and release
    • Shaw KL, et al. Foamy virus envelope glycoprotein is sufficient for particle budding and release. J Virol 2003 ; 77 : 2338-48.
    • (2003) J Virol , vol.77 , pp. 2338-2348
    • Shaw, K.L.1
  • 112
    • 18144371606 scopus 로고    scopus 로고
    • Identification of domains in gag important for prototypic foamy virus egress
    • Patton GS, et al. Identification of domains in gag important for prototypic foamy virus egress. J Virol 2005 ; 79 : 6392-9.
    • (2005) J Virol , vol.79 , pp. 6392-6399
    • Patton, G.S.1
  • 113
    • 20244370593 scopus 로고    scopus 로고
    • Characterization of prototype foamy virus gag late assembly domain motifs and their role in particle egress and infectivity
    • Stange A, et al. Characterization of prototype foamy virus gag late assembly domain motifs and their role in particle egress and infectivity. J Virol 2005 ; 79 : 5466-76.
    • (2005) J Virol , vol.79 , pp. 5466-5476
    • Stange, A.1
  • 114
    • 30344450406 scopus 로고    scopus 로고
    • Expanded tissue targets for foamy virus replication with simian immunodeficiency virus-induced immunosuppression
    • Murray SM, et al. Expanded tissue targets for foamy virus replication with simian immunodeficiency virus-induced immunosuppression. J Virol 2006 ; 80 : 663-70.
    • (2006) J Virol , vol.80 , pp. 663-670
    • Murray, S.M.1
  • 115
    • 20144388927 scopus 로고    scopus 로고
    • Ancient co-speciation of simian foamy viruses and primates
    • Switzer WM, et al. Ancient co-speciation of simian foamy viruses and primates. Nature 2005 ; 434 : 376-80.
    • (2005) Nature , vol.434 , pp. 376-380
    • Switzer, W.M.1


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