메뉴 건너뛰기




Volumn 85, Issue 18, 2011, Pages 9588-9598

Human immunodeficiency virus rev-binding protein is essential for influenza a virus replication and promotes genome trafficking in late-stage infection

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEAR EXPORT PROTEIN; REV PROTEIN; RIBONUCLEOPROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 80052444493     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05064-11     Document Type: Article
Times cited : (23)

References (45)
  • 1
    • 0141737104 scopus 로고    scopus 로고
    • Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)
    • Akarsu, H., et al. 2003. Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2). EMBO J. 22: 4646-4655.
    • (2003) EMBO J , vol.22 , pp. 4646-4655
    • Akarsu, H.1
  • 2
    • 79955415241 scopus 로고    scopus 로고
    • A Rab11- and microtubule-dependent mechanism for cytoplasmic transport of influenza A virus vRNA
    • Amorim, M. J., et al. 2011. A Rab11- and microtubule-dependent mechanism for cytoplasmic transport of influenza A virus vRNA. J. Virol. 85:4143- 4156.
    • (2011) J. Virol. , vol.85 , pp. 4143-4156
    • Amorim, M.J.1
  • 3
    • 0029149833 scopus 로고
    • Identification of a novel cellular cofactor for the Rev/Rex class of retroviral regulatory proteins
    • Bogerd, H. P., R. A. Fridell, S. Madore, and B. R. Cullen. 1995. Identification of a novel cellular cofactor for the Rev/Rex class of retroviral regulatory proteins. Cell 82:485-494.
    • (1995) Cell , vol.82 , pp. 485-494
    • Bogerd, H.P.1    Fridell, R.A.2    Madore, S.3    Cullen, B.R.4
  • 4
    • 34547114253 scopus 로고    scopus 로고
    • ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs
    • Bowzard, J. B., D. Cheng, J. Peng, and R. A. Kahn. 2007. ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs. J. Biol. Chem. 282: 17568-17580.
    • (2007) J. Biol. Chem. , vol.282 , pp. 17568-17580
    • Bowzard, J.B.1    Cheng, D.2    Peng, J.3    Kahn, R.A.4
  • 5
    • 67649840703 scopus 로고    scopus 로고
    • Budding of filamentous and non-filamentous influenza A virus occurs via a VPS4- and VPS28-independent pathway
    • Bruce, E. A., et al. 2009. Budding of filamentous and non-filamentous influenza A virus occurs via a VPS4- and VPS28-independent pathway. Virology 390:268-278.
    • (2009) Virology , vol.390 , pp. 268-278
    • Bruce, E.A.1
  • 6
    • 0033946767 scopus 로고    scopus 로고
    • Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins
    • Bui, M., E. G. Wills, A. Helenius, and G. R. Whittaker. 2000. Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins. J. Virol. 74:1781-1786.
    • (2000) J. Virol. , vol.74 , pp. 1781-1786
    • Bui, M.1    Wills, E.G.2    Helenius, A.3    Whittaker, G.R.4
  • 8
    • 0033611126 scopus 로고    scopus 로고
    • The eps15 homology (EH) domain-based interaction between eps15 and hrb connects the molecular machinery of endocytosis to that of nucleocytosolic transport
    • Doria, M., et al. 1999. The eps15 homology (EH) domain-based interaction between eps15 and hrb connects the molecular machinery of endocytosis to that of nucleocytosolic transport. J. Cell Biol. 147:1379-1384.
    • (1999) J. Cell Biol. , vol.147 , pp. 1379-1384
    • Doria, M.1
  • 9
    • 78149333191 scopus 로고    scopus 로고
    • The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells
    • Eierhoff, T., E. R. Hrincius, U. Rescher, S. Ludwig, and C. Ehrhardt. 2010. The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells. PLoS Pathog. 6:e1001099.
    • (2010) PLoS Pathog , vol.6
    • Eierhoff, T.1    Hrincius, E.R.2    Rescher, U.3    Ludwig, S.4    Ehrhardt, C.5
  • 10
    • 80052041082 scopus 로고    scopus 로고
    • RAB11A is essential for influenza genome transport to the plasma membrane
    • Eisfeld, A. J., E. Kawakami, T. Watanabe, G. Neumann, and Y. Kawaoka. 2011. RAB11A is essential for influenza genome transport to the plasma membrane. J. Virol. 85:6117-6126.
    • (2011) J. Virol. , vol.85 , pp. 6117-6126
    • Eisfeld, A.J.1    Kawakami, E.2    Watanabe, T.3    Neumann, G.4    Kawaoka, Y.5
  • 11
    • 0034749515 scopus 로고    scopus 로고
    • Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway
    • Elton, D., et al. 2001. Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway. J. Virol. 75:408-419.
    • (2001) J. Virol. , vol.75 , pp. 408-419
    • Elton, D.1
  • 12
    • 0033522920 scopus 로고    scopus 로고
    • Putative reaction intermediates in Crm1-mediated nuclear protein export
    • Floer, M., and G. Blobel. 1999. Putative reaction intermediates in Crm1-mediated nuclear protein export. J. Biol. Chem. 274:16279-16286.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16279-16286
    • Floer, M.1    Blobel, G.2
  • 13
    • 0029098538 scopus 로고
    • A human nucleoporin-like protein that specifically interacts with HIV Rev
    • Fritz, C. C., M. L. Zapp, and M. R. Green. 1995. A human nucleoporin-like protein that specifically interacts with HIV Rev. Nature 376:530-533.
    • (1995) Nature , vol.376 , pp. 530-533
    • Fritz, C.C.1    Zapp, M.L.2    Green, M.R.3
  • 14
    • 0037418322 scopus 로고    scopus 로고
    • RNA interference of influenza virus production by directly targeting mRNA for degradation and indirectly inhibiting all viral RNA transcription
    • Ge, Q., et al. 2003. RNA interference of influenza virus production by directly targeting mRNA for degradation and indirectly inhibiting all viral RNA transcription. Proc. Natl. Acad. Sci. U. S. A. 100:2718-2723.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 2718-2723
    • Ge, Q.1
  • 15
    • 0027946853 scopus 로고
    • Abortive replication of influenza virus A/WSN/33 in HeLa229 cells: defective viral entry and budding processes
    • Gujuluva, C. N., A. Kundu, K. G. Murti, and D. P. Nayak. 1994. Abortive replication of influenza virus A/WSN/33 in HeLa229 cells: defective viral entry and budding processes. Virology 204:491-505.
    • (1994) Virology , vol.204 , pp. 491-505
    • Gujuluva, C.N.1    Kundu, A.2    Murti, K.G.3    Nayak, D.P.4
  • 16
    • 0033577860 scopus 로고    scopus 로고
    • A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export
    • Kehlenbach, R. H., A. Dickmanns, A. Kehlenbach, T. Guan, and L. Gerace. 1999. A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export. J. Cell Biol. 145:645-657.
    • (1999) J. Cell Biol. , vol.145 , pp. 645-657
    • Kehlenbach, R.H.1    Dickmanns, A.2    Kehlenbach, A.3    Guan, T.4    Gerace, L.5
  • 17
    • 77954989425 scopus 로고    scopus 로고
    • HIV-1 Rev-binding protein accelerates cellular uptake of iron to drive Notch-induced T cell leukemogenesis in mice
    • Khwaja, S. S., et al. 2010. HIV-1 Rev-binding protein accelerates cellular uptake of iron to drive Notch-induced T cell leukemogenesis in mice. J. Clin. Invest. 120:2537-2548.
    • (2010) J. Clin. Invest. , vol.120 , pp. 2537-2548
    • Khwaja, S.S.1
  • 18
    • 0030796172 scopus 로고    scopus 로고
    • Neuraminidase hemadsorption activity, conserved in avian influenza A viruses, does not influence viral replication in ducks
    • Kobasa, D., M. E. Rodgers, K. Wells, and Y. Kawaoka. 1997. Neuraminidase hemadsorption activity, conserved in avian influenza A viruses, does not influence viral replication in ducks. J. Virol. 71:6706-6713.
    • (1997) J. Virol. , vol.71 , pp. 6706-6713
    • Kobasa, D.1    Rodgers, M.E.2    Wells, K.3    Kawaoka, Y.4
  • 20
    • 77949523738 scopus 로고    scopus 로고
    • Reassortment between avian H5N1 and human H3N2 influenza viruses creates hybrid viruses with substantial virulence
    • Li, C., et al. 2010. Reassortment between avian H5N1 and human H3N2 influenza viruses creates hybrid viruses with substantial virulence. Proc. Natl. Acad. Sci. U. S. A. 107:4687-4692.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 4687-4692
    • Li, C.1
  • 21
    • 0032562579 scopus 로고    scopus 로고
    • Catalytic domain of the p120 Ras GAP binds to RAb5 and stimulates its GTPase activity
    • Liu, K., and G. Li. 1998. Catalytic domain of the p120 Ras GAP binds to RAb5 and stimulates its GTPase activity. J. Biol. Chem. 273:10087-10090.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10087-10090
    • Liu, K.1    Li, G.2
  • 22
    • 0035836373 scopus 로고    scopus 로고
    • Nuclear export of influenza virus ribonucleoproteins: identification of an export intermediate at the nuclear periphery
    • Ma, K., A. M. Roy, and G. R. Whittaker. 2001. Nuclear export of influenza virus ribonucleoproteins: identification of an export intermediate at the nuclear periphery. Virology 282:215-220.
    • (2001) Virology , vol.282 , pp. 215-220
    • Ma, K.1    Roy, A.M.2    Whittaker, G.R.3
  • 23
    • 0026006258 scopus 로고
    • Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import
    • Martin, K., and A. Helenius. 1991. Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import. Cell 67:117-130.
    • (1991) Cell , vol.67 , pp. 117-130
    • Martin, K.1    Helenius, A.2
  • 24
    • 35548976680 scopus 로고    scopus 로고
    • Visualization of microtubule-mediated transport of influenza viral progeny ribonucleoprotein
    • Momose, F., Y. Kikuchi, K. Komase, and Y. Morikawa. 2007. Visualization of microtubule-mediated transport of influenza viral progeny ribonucleoprotein. Microbes Infect. 9:1422-1433.
    • (2007) Microbes Infect , vol.9 , pp. 1422-1433
    • Momose, F.1    Kikuchi, Y.2    Komase, K.3    Morikawa, Y.4
  • 25
    • 79151477797 scopus 로고    scopus 로고
    • EHD proteins: key conductors of endocytic transport
    • Naslavsky, N., and S. Caplan. 2011. EHD proteins: key conductors of endocytic transport. Trends Cell Biol. 21:122-131.
    • (2011) Trends Cell Biol. , vol.21 , pp. 122-131
    • Naslavsky, N.1    Caplan, S.2
  • 26
    • 0030731422 scopus 로고    scopus 로고
    • Nuclear import and export of influenza virus nucleoprotein
    • Neumann, G., M. R. Castrucci, and Y. Kawaoka. 1997. Nuclear import and export of influenza virus nucleoprotein. J. Virol. 71:9690-9700.
    • (1997) J. Virol. , vol.71 , pp. 9690-9700
    • Neumann, G.1    Castrucci, M.R.2    Kawaoka, Y.3
  • 27
    • 0034671826 scopus 로고    scopus 로고
    • Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1
    • Neumann, G., M. T. Hughes, and Y. Kawaoka. 2000. Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1. EMBO J. 19:6751-6758.
    • (2000) EMBO J , vol.19 , pp. 6751-6758
    • Neumann, G.1    Hughes, M.T.2    Kawaoka, Y.3
  • 28
    • 13044287344 scopus 로고    scopus 로고
    • Generation of influenza A viruses entirely from cloned cDNAs
    • Neumann, G., et al. 1999. Generation of influenza A viruses entirely from cloned cDNAs. Proc. Natl. Acad. Sci. U. S. A. 96:9345-9350.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 9345-9350
    • Neumann, G.1
  • 29
    • 0031260540 scopus 로고    scopus 로고
    • The importin-beta family member Crm1p bridges the interaction between Rev and the nuclear pore complex during nuclear export
    • Neville, M., F. Stutz, L. Lee, L. I. Davis, and M. Rosbash. 1997. The importin-beta family member Crm1p bridges the interaction between Rev and the nuclear pore complex during nuclear export. Curr. Biol. 7:767-775.
    • (1997) Curr. Biol. , vol.7 , pp. 767-775
    • Neville, M.1    Stutz, F.2    Lee, L.3    Davis, L.I.4    Rosbash, M.5
  • 30
    • 0025884056 scopus 로고
    • Efficient selection for high-expression transfectants with a novel eukaryotic vector
    • Niwa, H., K. Yamamura, and J. Miyazaki. 1991. Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 108:193-199.
    • (1991) Gene , vol.108 , pp. 193-199
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 31
    • 0032472328 scopus 로고    scopus 로고
    • The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins
    • O'Neill, R. E., J. Talon, and P. Palese. 1998. The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins. EMBO J. 17:288-296.
    • (1998) EMBO J. , vol.17 , pp. 288-296
    • O'Neill, R.E.1    Talon, J.2    Palese, P.3
  • 32
    • 14544299215 scopus 로고    scopus 로고
    • Mechanisms of receptor-mediated nuclear import and nuclear export
    • Pemberton, L. F., and B. M. Paschal. 2005. Mechanisms of receptor-mediated nuclear import and nuclear export. Traffic 6:187-198.
    • (2005) Traffic , vol.6 , pp. 187-198
    • Pemberton, L.F.1    Paschal, B.M.2
  • 33
    • 50549086057 scopus 로고    scopus 로고
    • Molecular basis for the sorting of the SNARE VAMP7 into endocytic clathrin-coated vesicles by the ArfGAP Hrb
    • Pryor, P. R., et al. 2008. Molecular basis for the sorting of the SNARE VAMP7 into endocytic clathrin-coated vesicles by the ArfGAP Hrb. Cell 134:817-827.
    • (2008) Cell , vol.134 , pp. 817-827
    • Pryor, P.R.1
  • 34
    • 77956637693 scopus 로고    scopus 로고
    • Influenza virus M2 protein mediates ESCRT-independent membrane scission
    • Rossman, J. S., X. Jing, G. P. Leser, and R. A. Lamb. 2010. Influenza virus M2 protein mediates ESCRT-independent membrane scission. Cell 142: 902-913.
    • (2010) Cell , vol.142 , pp. 902-913
    • Rossman, J.S.1    Jing, X.2    Leser, G.P.3    Lamb, R.A.4
  • 35
    • 0037440711 scopus 로고    scopus 로고
    • Nuclear export of influenza viral ribonucleoprotein is temperature-dependently inhibited by dissociation of viral matrix protein
    • Sakaguchi, A., E. Hirayama, A. Hiraki, Y. Ishida, and J. Kim. 2003. Nuclear export of influenza viral ribonucleoprotein is temperature-dependently inhibited by dissociation of viral matrix protein. Virology 306:244-253.
    • (2003) Virology , vol.306 , pp. 244-253
    • Sakaguchi, A.1    Hirayama, E.2    Hiraki, A.3    Ishida, Y.4    Kim, J.5
  • 36
    • 0346497767 scopus 로고    scopus 로고
    • hRIP, a cellular cofactor for Rev function, promotes release of HIV RNAs from the perinuclear region
    • Sanchez-Velar, N., E. B. Udofia, Z. Yu, and M. L. Zapp. 2004. hRIP, a cellular cofactor for Rev function, promotes release of HIV RNAs from the perinuclear region. Genes Dev. 18:23-34.
    • (2004) Genes Dev. , vol.18 , pp. 23-34
    • Sanchez-Velar, N.1    Udofia, E.B.2    Yu, Z.3    Zapp, M.L.4
  • 37
    • 33748626246 scopus 로고    scopus 로고
    • Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly
    • Schmid, E. M., et al. 2006. Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly. PLoS Biol. 4:e262.
    • (2006) PLoS Biol. , vol.4
    • Schmid, E.M.1
  • 38
    • 78650884304 scopus 로고    scopus 로고
    • Crucial role of the influenza virus NS2 (NEP) C-terminal domain in M1 binding and nuclear export of vRNP
    • Shimizu, T., N. Takizawa, K. Watanabe, K. Nagata, and N. Kobayashi. 2011. Crucial role of the influenza virus NS2 (NEP) C-terminal domain in M1 binding and nuclear export of vRNP. FEBS Lett. 585:41-46.
    • (2011) FEBS Lett. , vol.585 , pp. 41-46
    • Shimizu, T.1    Takizawa, N.2    Watanabe, K.3    Nagata, K.4    Kobayashi, N.5
  • 39
    • 1642417689 scopus 로고    scopus 로고
    • Role of Unc51.1 and its binding partners in CNS axon outgrowth
    • Tomoda, T., J. H. Kim, C. Zhan, and M. E. Hatten. 2004. Role of Unc51.1 and its binding partners in CNS axon outgrowth. Genes Dev. 18:541-558.
    • (2004) Genes Dev. , vol.18 , pp. 541-558
    • Tomoda, T.1    Kim, J.H.2    Zhan, C.3    Hatten, M.E.4
  • 40
    • 0034929835 scopus 로고    scopus 로고
    • Inhibition of nuclear export of ribonucleoprotein complexes of influenza virus by leptomycin B
    • Watanabe, K., et al. 2001. Inhibition of nuclear export of ribonucleoprotein complexes of influenza virus by leptomycin B. Virus Res. 77:31-42.
    • (2001) Virus Res. , vol.77 , pp. 31-42
    • Watanabe, K.1
  • 41
    • 77956227450 scopus 로고    scopus 로고
    • Influenza virus budding does not require a functional AAA+ ATPase
    • Watanabe, R., and R. A. Lamb. 2010. Influenza virus budding does not require a functional AAA+ ATPase, VPS4. Virus Res. 153:58-63.
    • (2010) VPS4. Virus Res. , vol.153 , pp. 58-63
    • Watanabe, R.1    Lamb, R.A.2
  • 43
    • 84858618648 scopus 로고    scopus 로고
    • World Health Organization (WHO). April World Health Organization, Geneva, Switzerland
    • World Health Organization (WHO). April 2009, posting date. Fact sheet no. 211. World Health Organization, Geneva, Switzerland. http://www.who.int /mediacentre/factsheets/fs211/en.
    • (2009) posting date. Fact sheet no. 211
  • 44
    • 0030972969 scopus 로고    scopus 로고
    • The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis
    • Xiao, G. H., F. Shoarinejad, F. Jin, E. A. Golemis, and R. S. Yeung. 1997. The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis. J. Biol. Chem. 272: 6097-6100.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6097-6100
    • Xiao, G.H.1    Shoarinejad, F.2    Jin, F.3    Golemis, E.A.4    Yeung, R.S.5
  • 45
    • 15244362533 scopus 로고    scopus 로고
    • The cellular HIV-1 Rev cofactor hRIP is required for viral replication
    • Yu, Z., et al. 2005. The cellular HIV-1 Rev cofactor hRIP is required for viral replication. Proc. Natl. Acad. Sci. U. S. A. 102:4027-4032.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 4027-4032
    • Yu, Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.