메뉴 건너뛰기




Volumn 483, Issue , 2015, Pages 291-301

Conformational changes required for reovirus cell entry are sensitive to pH

Author keywords

DsRNA virus; Nonenveloped; Reovirus; Virus entry

Indexed keywords

BAFILOMYCIN A1; OUABAIN; ENZYME INHIBITOR;

EID: 84929497324     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2015.04.025     Document Type: Article
Times cited : (13)

References (80)
  • 1
    • 33750819587 scopus 로고    scopus 로고
    • Mammalian reovirus, a nonfusogenic nonenveloped virus, forms size-selective pores in a model membrane
    • Agosto M.A., Ivanovic T., Nibert M.L. Mammalian reovirus, a nonfusogenic nonenveloped virus, forms size-selective pores in a model membrane. Proc. Natl. Acad. Sci. USA 2006, 103:16496-16501.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16496-16501
    • Agosto, M.A.1    Ivanovic, T.2    Nibert, M.L.3
  • 2
    • 34447274263 scopus 로고    scopus 로고
    • Thermolabilizing pseudoreversions in reovirus outer-capsid protein micro 1 rescue the entry defect conferred by a thermostabilizing mutation
    • Agosto M.A., Middleton J.K., Freimont E.C., Yin J., Nibert M.L. Thermolabilizing pseudoreversions in reovirus outer-capsid protein micro 1 rescue the entry defect conferred by a thermostabilizing mutation. J. Virol. 2007, 81:7400-7409.
    • (2007) J. Virol. , vol.81 , pp. 7400-7409
    • Agosto, M.A.1    Middleton, J.K.2    Freimont, E.C.3    Yin, J.4    Nibert, M.L.5
  • 3
    • 48749094796 scopus 로고    scopus 로고
    • A positive-feedback mechanism promotes reovirus particle conversion to the intermediate associated with membrane penetration
    • Agosto M.A., Myers K.S., Ivanovic T., Nibert M.L. A positive-feedback mechanism promotes reovirus particle conversion to the intermediate associated with membrane penetration. Proc. Natl. Acad. Sci. USA 2008, 105:10571-10576.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 10571-10576
    • Agosto, M.A.1    Myers, K.S.2    Ivanovic, T.3    Nibert, M.L.4
  • 4
    • 84879048489 scopus 로고    scopus 로고
    • Interferon-inducible transmembrane protein 3 (IFITM3) restricts reovirus cell entry
    • Anafu A.A., Bowen C.H., Chin C.R., Brass A.L., Holm G.H. Interferon-inducible transmembrane protein 3 (IFITM3) restricts reovirus cell entry. J. Biol. Chem. 2013, 288:17261-17271.
    • (2013) J. Biol. Chem. , vol.288 , pp. 17261-17271
    • Anafu, A.A.1    Bowen, C.H.2    Chin, C.R.3    Brass, A.L.4    Holm, G.H.5
  • 5
    • 0032830324 scopus 로고    scopus 로고
    • Mutant cells selected during persistent reovirus infection do not express mature cathepsin L and do not support reovirus disassembly
    • Baer G.S., Ebert D.H., Chung C.J., Erickson A.H., Dermody T.S. Mutant cells selected during persistent reovirus infection do not express mature cathepsin L and do not support reovirus disassembly. J. Virol. 1999, 73:9532-9543.
    • (1999) J. Virol. , vol.73 , pp. 9532-9543
    • Baer, G.S.1    Ebert, D.H.2    Chung, C.J.3    Erickson, A.H.4    Dermody, T.S.5
  • 6
    • 0035910468 scopus 로고    scopus 로고
    • Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening
    • Barton E.S., Connolly J.L., Forrest J.C., Chappell J.D., Dermody T.S. Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening. J. Biol. Chem. 2001, 276:2200-2211.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2200-2211
    • Barton, E.S.1    Connolly, J.L.2    Forrest, J.C.3    Chappell, J.D.4    Dermody, T.S.5
  • 8
    • 0025249289 scopus 로고
    • Intraluminal proteolytic activation plays an important role in replication of type 1 reovirus in the intestines of neonatal mice
    • Bass D.M., Bodkin D., Dambrauskas R., Trier J.S., Fields B.N., Wolf J.L. Intraluminal proteolytic activation plays an important role in replication of type 1 reovirus in the intestines of neonatal mice. J. Virol. 1990, 64:1830-1833.
    • (1990) J. Virol. , vol.64 , pp. 1830-1833
    • Bass, D.M.1    Bodkin, D.2    Dambrauskas, R.3    Trier, J.S.4    Fields, B.N.5    Wolf, J.L.6
  • 9
    • 68949188073 scopus 로고    scopus 로고
    • Mammalian reoviruses: propagation, quantification, and storage
    • chapter 15, Unit15C 11.
    • Berard, A., Coombs, K.M., 2009. Mammalian reoviruses: propagation, quantification, and storage. Current Protocols in Microbiology, chapter 15, Unit15C 11.
    • (2009) Current Protocols in Microbiology
    • Berard, A.1    Coombs, K.M.2
  • 10
    • 0024418092 scopus 로고
    • Proteolytic digestion of reovirus in the intestinal lumens of neonatal mice
    • Bodkin D.K., Nibert M.L., Fields B.N. Proteolytic digestion of reovirus in the intestinal lumens of neonatal mice. J. Virol. 1989, 63:4676-4681.
    • (1989) J. Virol. , vol.63 , pp. 4676-4681
    • Bodkin, D.K.1    Nibert, M.L.2    Fields, B.N.3
  • 11
    • 0015827479 scopus 로고
    • New intermediate subviral particles in the in vitro uncoating of reovirus virions by chymotrypsin
    • Borsa J., Copps T.P., Sargent M.D., Long D.G., Chapman J.D. New intermediate subviral particles in the in vitro uncoating of reovirus virions by chymotrypsin. J. Virol. 1973, 11:552-564.
    • (1973) J. Virol. , vol.11 , pp. 552-564
    • Borsa, J.1    Copps, T.P.2    Sargent, M.D.3    Long, D.G.4    Chapman, J.D.5
  • 13
    • 84876577893 scopus 로고    scopus 로고
    • Similar uptake but different trafficking and escape routes of reovirus virions and infectious subvirion particles imaged in polarized Madin-Darby canine kidney cells
    • Boulant S., Stanifer M., Kural C., Cureton D.K., Massol R., Nibert M.L., Kirchhausen T. Similar uptake but different trafficking and escape routes of reovirus virions and infectious subvirion particles imaged in polarized Madin-Darby canine kidney cells. Mol. Biol. Cell 2013, 24:1196-1207.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1196-1207
    • Boulant, S.1    Stanifer, M.2    Kural, C.3    Cureton, D.K.4    Massol, R.5    Nibert, M.L.6    Kirchhausen, T.7
  • 14
    • 0037405104 scopus 로고    scopus 로고
    • Conformational changes, plasma membrane penetration, and infection by human rhinovirus type 2: role of receptors and low pH
    • Brabec M., Baravalle G., Blaas D., Fuchs R. Conformational changes, plasma membrane penetration, and infection by human rhinovirus type 2: role of receptors and low pH. J. Virol. 2003, 77:5370-5377.
    • (2003) J. Virol. , vol.77 , pp. 5370-5377
    • Brabec, M.1    Baravalle, G.2    Blaas, D.3    Fuchs, R.4
  • 15
    • 0343384915 scopus 로고
    • Regulation of endocytic pH by the Na+,K+-ATPase in living cells
    • Cain C.C., Sipe D.M., Murphy R.F. Regulation of endocytic pH by the Na+,K+-ATPase in living cells. Proc. Natl. Acad. Sci. USA 1989, 86:544-548.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 544-548
    • Cain, C.C.1    Sipe, D.M.2    Murphy, R.F.3
  • 16
    • 0036776328 scopus 로고    scopus 로고
    • Strategy for nonenveloped virus entry: a hydrophobic conformer of the reovirus membrane penetration protein m1 mediates membrane disruption
    • Chandran K., Farsetta D.L., Nibert M.L. Strategy for nonenveloped virus entry: a hydrophobic conformer of the reovirus membrane penetration protein m1 mediates membrane disruption. J. Virol. 2002, 76:9920-9933.
    • (2002) J. Virol. , vol.76 , pp. 9920-9933
    • Chandran, K.1    Farsetta, D.L.2    Nibert, M.L.3
  • 17
    • 0345166984 scopus 로고    scopus 로고
    • The delta region of outer-capsid protein m1 undergoes conformational change and release from reovirus particles during cell entry
    • Chandran K., Parker J.S., Ehrlich M., Kirchhausen T., Nibert M.L. The delta region of outer-capsid protein m1 undergoes conformational change and release from reovirus particles during cell entry. J. Virol. 2003, 77:13361-13375.
    • (2003) J. Virol. , vol.77 , pp. 13361-13375
    • Chandran, K.1    Parker, J.S.2    Ehrlich, M.3    Kirchhausen, T.4    Nibert, M.L.5
  • 18
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran K., Sullivan N.J., Felbor U., Whelan S.P., Cunningham J.M. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 2005, 308:1643-1645.
    • (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
  • 19
    • 0015166005 scopus 로고
    • Fate of parental reovirus in infected cell
    • Chang C.T., Zweerink H.J. Fate of parental reovirus in infected cell. Virology 1971, 46:544-555.
    • (1971) Virology , vol.46 , pp. 544-555
    • Chang, C.T.1    Zweerink, H.J.2
  • 20
    • 33748641937 scopus 로고    scopus 로고
    • Reovirus outer capsid protein m1 induces apoptosis and associates with lipid droplets, endoplasmic reticulum, and mitochondria
    • Coffey C.M., Sheh A., Kim I.S., Chandran K., Nibert M.L., Parker J.S. Reovirus outer capsid protein m1 induces apoptosis and associates with lipid droplets, endoplasmic reticulum, and mitochondria. J. Virol. 2006, 80:8422-8438.
    • (2006) J. Virol. , vol.80 , pp. 8422-8438
    • Coffey, C.M.1    Sheh, A.2    Kim, I.S.3    Chandran, K.4    Nibert, M.L.5    Parker, J.S.6
  • 21
    • 0027499070 scopus 로고
    • The use of ATP bioluminescence as a measure of cell-proliferation and cytotoxicity
    • Crouch S.P.M., Kozlowski R., Slater K.J., Fletcher J. The use of ATP bioluminescence as a measure of cell-proliferation and cytotoxicity. J. Immunol. Methods 1993, 160:81-88.
    • (1993) J. Immunol. Methods , vol.160 , pp. 81-88
    • Crouch, S.P.M.1    Kozlowski, R.2    Slater, K.J.3    Fletcher, J.4
  • 22
    • 31144446888 scopus 로고    scopus 로고
    • JAM-A-independent, antibody-mediated uptake of reovirus into cells leads to apoptosis
    • Danthi P., Hansberger M.W., Campbell J.A., Forrest J.C., Dermody T.S. JAM-A-independent, antibody-mediated uptake of reovirus into cells leads to apoptosis. J. Virol. 2006, 80:1261-1270.
    • (2006) J. Virol. , vol.80 , pp. 1261-1270
    • Danthi, P.1    Hansberger, M.W.2    Campbell, J.A.3    Forrest, J.C.4    Dermody, T.S.5
  • 23
    • 0025049962 scopus 로고
    • A sigma 1 region important for hemagglutination by serotype 3 reovirus strains
    • Dermody T.S., Nibert M.L., Bassel-Duby R., Fields B.N. A sigma 1 region important for hemagglutination by serotype 3 reovirus strains. J. Virol. 1990, 64:5173-5176.
    • (1990) J. Virol. , vol.64 , pp. 5173-5176
    • Dermody, T.S.1    Nibert, M.L.2    Bassel-Duby, R.3    Fields, B.N.4
  • 24
    • 34548563920 scopus 로고    scopus 로고
    • Inhibitors of the sodium potassium ATPase that impair herpes simplex virus replication identified via a chemical screening approach
    • Dodson A.W., Taylor T.J., Knipe D.M., Coen D.M. Inhibitors of the sodium potassium ATPase that impair herpes simplex virus replication identified via a chemical screening approach. Virology 2007, 366:340-348.
    • (2007) Virology , vol.366 , pp. 340-348
    • Dodson, A.W.1    Taylor, T.J.2    Knipe, D.M.3    Coen, D.M.4
  • 25
    • 0027162058 scopus 로고
    • Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction
    • Dryden K.A., Wang G., Yeager M., Nibert M.L., Coombs K.M., Furlong D.B., Fields B.N., Baker T.S. Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction. J. Cell Biol. 1993, 122:1023-1041.
    • (1993) J. Cell Biol. , vol.122 , pp. 1023-1041
    • Dryden, K.A.1    Wang, G.2    Yeager, M.3    Nibert, M.L.4    Coombs, K.M.5    Furlong, D.B.6    Fields, B.N.7    Baker, T.S.8
  • 26
    • 0037025342 scopus 로고    scopus 로고
    • Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells
    • Ebert D.H., Deussing J., Peters C., Dermody T.S. Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells. J. Biol. Chem. 2002, 277:24609-24617.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24609-24617
    • Ebert, D.H.1    Deussing, J.2    Peters, C.3    Dermody, T.S.4
  • 29
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
    • Forgac M. Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. 2007, 8:917-929.
    • (2007) Nat. Rev. , vol.8 , pp. 917-929
    • Forgac, M.1
  • 30
    • 0004073280 scopus 로고
    • A possible role for Na+,K+-ATPase in regulating ATP-dependent endosome acidification
    • Fuchs R., Schmid S., Mellman I. A possible role for Na+,K+-ATPase in regulating ATP-dependent endosome acidification. Proc. Natl. Acad. Sci. USA 1989, 86:539-543.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 539-543
    • Fuchs, R.1    Schmid, S.2    Mellman, I.3
  • 31
    • 0023388477 scopus 로고
    • Anti-glycoprotein D antibodies that permit adsorption but block infection by herpes simplex virus 1 prevent virion-cell fusion at the cell surface
    • Fuller A.O., Spear P.G. Anti-glycoprotein D antibodies that permit adsorption but block infection by herpes simplex virus 1 prevent virion-cell fusion at the cell surface. Proc. Natl. Acad. Sci. USA 1987, 84:5454-5458.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5454-5458
    • Fuller, A.O.1    Spear, P.G.2
  • 33
    • 0036310562 scopus 로고    scopus 로고
    • Addition of exogenous protease facilitates reovirus infection in many restrictive cells
    • Golden J.W., Linke J., Schmechel S., Thoemke K., Schiff L.A. Addition of exogenous protease facilitates reovirus infection in many restrictive cells. J. Virol. 2002, 76:7430-7443.
    • (2002) J. Virol. , vol.76 , pp. 7430-7443
    • Golden, J.W.1    Linke, J.2    Schmechel, S.3    Thoemke, K.4    Schiff, L.A.5
  • 34
    • 0027496645 scopus 로고
    • Stepwise dismantling of adenovirus 2 during entry into cells
    • Greber U.F., Willetts M., Webster P., Helenius A. Stepwise dismantling of adenovirus 2 during entry into cells. Cell 1993, 75:477-486.
    • (1993) Cell , vol.75 , pp. 477-486
    • Greber, U.F.1    Willetts, M.2    Webster, P.3    Helenius, A.4
  • 35
    • 0037166251 scopus 로고    scopus 로고
    • Src-mediated inter-receptor cross-talk between the Na+/K+-ATPase and the epidermal growth factor receptor relays the signal from ouabain to mitogen-activated protein kinases
    • Haas M., Wang H., Tian J., Xie Z. Src-mediated inter-receptor cross-talk between the Na+/K+-ATPase and the epidermal growth factor receptor relays the signal from ouabain to mitogen-activated protein kinases. J. Biol. Chem. 2002, 277:18694-18702.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18694-18702
    • Haas, M.1    Wang, H.2    Tian, J.3    Xie, Z.4
  • 36
    • 0029656249 scopus 로고    scopus 로고
    • Role of the m1 protein in reovirus stability and capacity to cause chromium release from host cells
    • Hooper J.W., Fields B.N. Role of the m1 protein in reovirus stability and capacity to cause chromium release from host cells. J. Virol. 1996, 70:459-467.
    • (1996) J. Virol. , vol.70 , pp. 459-467
    • Hooper, J.W.1    Fields, B.N.2
  • 37
    • 42449151315 scopus 로고    scopus 로고
    • Peptides released from reovirus outer capsid form membrane pores that recruit virus particles
    • Ivanovic T., Agosto M.A., Zhang L., Chandran K., Harrison S.C., Nibert M.L. Peptides released from reovirus outer capsid form membrane pores that recruit virus particles. Embo J. 2008, 27:1289-1298.
    • (2008) Embo J. , vol.27 , pp. 1289-1298
    • Ivanovic, T.1    Agosto, M.A.2    Zhang, L.3    Chandran, K.4    Harrison, S.C.5    Nibert, M.L.6
  • 38
    • 22144486880 scopus 로고    scopus 로고
    • Infectious entry of reovirus cores into mammalian cells enhanced by transfection
    • Jiang J., Coombs K.M. Infectious entry of reovirus cores into mammalian cells enhanced by transfection. J. Virol. Methods 2005, 128:88-92.
    • (2005) J. Virol. Methods , vol.128 , pp. 88-92
    • Jiang, J.1    Coombs, K.M.2
  • 39
    • 84860289105 scopus 로고    scopus 로고
    • Natural compounds inhibiting the replication of Porcine reproductive and respiratory syndrome virus
    • Karuppannan A.K., Wu K.X., Qiang J., Chu J.J., Kwang J. Natural compounds inhibiting the replication of Porcine reproductive and respiratory syndrome virus. Antivir. Res. 2012, 94:188-194.
    • (2012) Antivir. Res. , vol.94 , pp. 188-194
    • Karuppannan, A.K.1    Wu, K.X.2    Qiang, J.3    Chu, J.J.4    Kwang, J.5
  • 41
    • 0037169362 scopus 로고    scopus 로고
    • Structure of the reovirus membrane-penetration protein, m1, in a complex with its protector protein, s3
    • Liemann S., Chandran K., Baker T.S., Nibert M.L., Harrison S.C. Structure of the reovirus membrane-penetration protein, m1, in a complex with its protector protein, s3. Cell 2002, 108:283-295.
    • (2002) Cell , vol.108 , pp. 283-295
    • Liemann, S.1    Chandran, K.2    Baker, T.S.3    Nibert, M.L.4    Harrison, S.C.5
  • 42
    • 0034623226 scopus 로고    scopus 로고
    • Ouabain interaction with cardiac Na+/K+-ATPase initiates signal cascades independent of changes in intracellular Na+ and Ca2+ concentrations
    • Liu J., Tian J., Haas M., Shapiro J.I., Askari A., Xie Z. Ouabain interaction with cardiac Na+/K+-ATPase initiates signal cascades independent of changes in intracellular Na+ and Ca2+ concentrations. J. Biol. Chem. 2000, 275:27838-27844.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27838-27844
    • Liu, J.1    Tian, J.2    Haas, M.3    Shapiro, J.I.4    Askari, A.5    Xie, Z.6
  • 45
    • 0027296972 scopus 로고
    • Reovirus M2 gene is associated with chromium release from mouse L cells
    • Lucia-Jandris P., Hooper J.W., Fields B.N. Reovirus M2 gene is associated with chromium release from mouse L cells. J. Virol. 1993, 67:5339-5345.
    • (1993) J. Virol. , vol.67 , pp. 5339-5345
    • Lucia-Jandris, P.1    Hooper, J.W.2    Fields, B.N.3
  • 46
    • 84861306230 scopus 로고    scopus 로고
    • Cell entry-associated conformational changes in reovirus particles are controlled by host protease activity
    • Madren J.A., Sarkar P., Danthi P. Cell entry-associated conformational changes in reovirus particles are controlled by host protease activity. J. Virol. 2012, 86:3466-3473.
    • (2012) J. Virol. , vol.86 , pp. 3466-3473
    • Madren, J.A.1    Sarkar, P.2    Danthi, P.3
  • 47
    • 41149103877 scopus 로고    scopus 로고
    • NPXY motifs in the beta1 integrin cytoplasmic tail are required for functional reovirus entry
    • Maginnis M.S., Mainou B.A., Derdowski A., Johnson E.M., Zent R., Dermody T.S. NPXY motifs in the beta1 integrin cytoplasmic tail are required for functional reovirus entry. J. Virol. 2008, 82:3181-3191.
    • (2008) J. Virol. , vol.82 , pp. 3181-3191
    • Maginnis, M.S.1    Mainou, B.A.2    Derdowski, A.3    Johnson, E.M.4    Zent, R.5    Dermody, T.S.6
  • 48
    • 79952606400 scopus 로고    scopus 로고
    • Src kinase mediates productive endocytic sorting of reovirus during cell entry
    • Mainou B.A., Dermody T.S. Src kinase mediates productive endocytic sorting of reovirus during cell entry. J. Virol. 2011, 85:3203-3213.
    • (2011) J. Virol. , vol.85 , pp. 3203-3213
    • Mainou, B.A.1    Dermody, T.S.2
  • 49
    • 84865101799 scopus 로고    scopus 로고
    • Transport to late endosomes is required for efficient reovirus infection
    • Mainou B.A., Dermody T.S. Transport to late endosomes is required for efficient reovirus infection. J. Virol. 2012, 86:8346-8358.
    • (2012) J. Virol. , vol.86 , pp. 8346-8358
    • Mainou, B.A.1    Dermody, T.S.2
  • 50
    • 0029655850 scopus 로고    scopus 로고
    • The entry of reovirus into L cells is dependent on vacuolar proton-ATPase activity
    • Martinez C.G., Guinea R., Benavente J., Carrasco L. The entry of reovirus into L cells is dependent on vacuolar proton-ATPase activity. J. Virol. 1996, 70:576-579.
    • (1996) J. Virol. , vol.70 , pp. 576-579
    • Martinez, C.G.1    Guinea, R.2    Benavente, J.3    Carrasco, L.4
  • 51
    • 0017867024 scopus 로고
    • Effect of ouabain on sindbis virus replication in ouabain-sensitive and ouabain-resistant Aedes albopictus cells (Singh)
    • Mento S.J., Stollar V. Effect of ouabain on sindbis virus replication in ouabain-sensitive and ouabain-resistant Aedes albopictus cells (Singh). Virology 1978, 87:58-65.
    • (1978) Virology , vol.87 , pp. 58-65
    • Mento, S.J.1    Stollar, V.2
  • 52
    • 34147164393 scopus 로고    scopus 로고
    • Thermostabilizing mutations in reovirus outer-capsid protein m1 selected by heat inactivation of infectious subvirion particles
    • Middleton J.K., Agosto M.A., Severson T.F., Yin J., Nibert M.L. Thermostabilizing mutations in reovirus outer-capsid protein m1 selected by heat inactivation of infectious subvirion particles. Virology 2007, 361:412-425.
    • (2007) Virology , vol.361 , pp. 412-425
    • Middleton, J.K.1    Agosto, M.A.2    Severson, T.F.3    Yin, J.4    Nibert, M.L.5
  • 53
    • 0036149374 scopus 로고    scopus 로고
    • Thermostability of reovirus disassembly intermediates (ISVPs) correlates with genetic, biochemical, and thermodynamic properties of major surface protein mu1
    • Middleton J.K., Severson T.F., Chandran K., Gillian A.L., Yin J., Nibert M.L. Thermostability of reovirus disassembly intermediates (ISVPs) correlates with genetic, biochemical, and thermodynamic properties of major surface protein mu1. J. Virol. 2002, 76:1051-1061.
    • (2002) J. Virol. , vol.76 , pp. 1051-1061
    • Middleton, J.K.1    Severson, T.F.2    Chandran, K.3    Gillian, A.L.4    Yin, J.5    Nibert, M.L.6
  • 54
    • 0015290604 scopus 로고
    • Inhibition of virus growth by ouabain: effect of ouabain on the growth of HVJ in chick embryo cells
    • Nagai Y., Maeno K., Iinuma M., Yoshida T., Matsumoto T. Inhibition of virus growth by ouabain: effect of ouabain on the growth of HVJ in chick embryo cells. J. Virol. 1972, 9:234-243.
    • (1972) J. Virol. , vol.9 , pp. 234-243
    • Nagai, Y.1    Maeno, K.2    Iinuma, M.3    Yoshida, T.4    Matsumoto, T.5
  • 55
    • 0029058860 scopus 로고
    • Infectious subvirion particles of reovirus type 3 Dearing exhibit a loss in infectivity and contain a cleaved sigma 1 protein
    • Nibert M.L., Chappell J.D., Dermody T.S. Infectious subvirion particles of reovirus type 3 Dearing exhibit a loss in infectivity and contain a cleaved sigma 1 protein. J. Virol. 1995, 69:5057-5067.
    • (1995) J. Virol. , vol.69 , pp. 5057-5067
    • Nibert, M.L.1    Chappell, J.D.2    Dermody, T.S.3
  • 56
    • 9644268149 scopus 로고    scopus 로고
    • Putative autocleavage of reovirus m1 protein in concert with outer-capsid disassembly and activation for membrane permeabilization
    • Nibert M.L., Odegard A.L., Agosto M.A., Chandran K., Schiff L.A. Putative autocleavage of reovirus m1 protein in concert with outer-capsid disassembly and activation for membrane permeabilization. J. Mol. Biol. 2005, 345:461-474.
    • (2005) J. Mol. Biol. , vol.345 , pp. 461-474
    • Nibert, M.L.1    Odegard, A.L.2    Agosto, M.A.3    Chandran, K.4    Schiff, L.A.5
  • 57
    • 84856870292 scopus 로고    scopus 로고
    • Impact of host proteases on reovirus infection in the respiratory tract
    • Nygaard R.M., Golden J.W., Schiff L.A. Impact of host proteases on reovirus infection in the respiratory tract. J. Virol. 2012, 86:1238-1243.
    • (2012) J. Virol. , vol.86 , pp. 1238-1243
    • Nygaard, R.M.1    Golden, J.W.2    Schiff, L.A.3
  • 58
    • 3543115472 scopus 로고    scopus 로고
    • Putative autocleavage of outer capsid protein m1, allowing release of myristoylated peptide m1N during particle uncoating, is critical for cell entry by reovirus
    • Odegard A.L., Chandran K., Zhang X., Parker J.S., Baker T.S., Nibert M.L. Putative autocleavage of outer capsid protein m1, allowing release of myristoylated peptide m1N during particle uncoating, is critical for cell entry by reovirus. J. Virol. 2004, 78:8732-8745.
    • (2004) J. Virol. , vol.78 , pp. 8732-8745
    • Odegard, A.L.1    Chandran, K.2    Zhang, X.3    Parker, J.S.4    Baker, T.S.5    Nibert, M.L.6
  • 59
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma S., Poole B. Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc. Natl. Acad. Sci. USA 1978, 75:3327-3331.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 61
    • 0022559211 scopus 로고
    • ATP-driven H+ pumping into intracellular organelles
    • Rudnick G. ATP-driven H+ pumping into intracellular organelles. Annu. Rev. Physiol. 1986, 48:403-413.
    • (1986) Annu. Rev. Physiol. , vol.48 , pp. 403-413
    • Rudnick, G.1
  • 62
    • 78649431782 scopus 로고    scopus 로고
    • Determinants of strain-specific differences in efficiency of reovirus entry
    • Sarkar P., Danthi P. Determinants of strain-specific differences in efficiency of reovirus entry. J. Virol. 2010, 84:12723-12732.
    • (2010) J. Virol. , vol.84 , pp. 12723-12732
    • Sarkar, P.1    Danthi, P.2
  • 63
    • 84888020607 scopus 로고    scopus 로고
    • The mu1 72-96 loop controls conformational transitions during reovirus cell entry
    • Sarkar P., Danthi P. The mu1 72-96 loop controls conformational transitions during reovirus cell entry. J. Virol. 2013, 87:13532-13542.
    • (2013) J. Virol. , vol.87 , pp. 13532-13542
    • Sarkar, P.1    Danthi, P.2
  • 65
    • 44949231424 scopus 로고    scopus 로고
    • Analyzing real-time PCR data by the comparative C(T) method
    • Schmittgen T.D., Livak K.J. Analyzing real-time PCR data by the comparative C(T) method. Nat. Protoc. 2008, 3:1101-1108.
    • (2008) Nat. Protoc. , vol.3 , pp. 1101-1108
    • Schmittgen, T.D.1    Livak, K.J.2
  • 66
    • 84869216032 scopus 로고    scopus 로고
    • Reovirus uses multiple endocytic pathways for cell entry
    • Schulz W.L., Haj A.K., Schiff L.A. Reovirus uses multiple endocytic pathways for cell entry. J. Virol. 2012, 86:12665-12675.
    • (2012) J. Virol. , vol.86 , pp. 12665-12675
    • Schulz, W.L.1    Haj, A.K.2    Schiff, L.A.3
  • 67
  • 68
    • 0014627613 scopus 로고
    • Polypeptide components of virions, top component and cores of reovirus type 3
    • Smith R.E., Zweerink H.J., Joklik W.K. Polypeptide components of virions, top component and cores of reovirus type 3. Virology 1969, 39:791-810.
    • (1969) Virology , vol.39 , pp. 791-810
    • Smith, R.E.1    Zweerink, H.J.2    Joklik, W.K.3
  • 69
    • 0023194972 scopus 로고
    • Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle
    • Sturzenbecker L.J., Nibert M.L., Furlong D.B., Fields B.N. Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle. J. Virol. 1987, 61:2351-2361.
    • (1987) J. Virol. , vol.61 , pp. 2351-2361
    • Sturzenbecker, L.J.1    Nibert, M.L.2    Furlong, D.B.3    Fields, B.N.4
  • 71
    • 0020105628 scopus 로고
    • Rapid acidification of endocytic vesicles containing alpha-2 macroglobulin
    • Tycko B., Maxfield F.R. Rapid acidification of endocytic vesicles containing alpha-2 macroglobulin. Cell 1982, 28:643-651.
    • (1982) Cell , vol.28 , pp. 643-651
    • Tycko, B.1    Maxfield, F.R.2
  • 72
    • 0030337835 scopus 로고    scopus 로고
    • Acidification of lysosomes and endosomes
    • Van Dyke R.W. Acidification of lysosomes and endosomes. Subcell. Biochem. 1996, 27:331-360.
    • (1996) Subcell. Biochem. , vol.27 , pp. 331-360
    • Van Dyke, R.W.1
  • 73
    • 2342424240 scopus 로고    scopus 로고
    • Ouabain assembles signaling cascades through the caveolar Na+/K+-ATPase
    • Wang H., Haas M., Liang M., Cai T., Tian J., Li S., Xie Z. Ouabain assembles signaling cascades through the caveolar Na+/K+-ATPase. J. Biol. Chem. 2004, 279:17250-17259.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17250-17259
    • Wang, H.1    Haas, M.2    Liang, M.3    Cai, T.4    Tian, J.5    Li, S.6    Xie, Z.7
  • 74
    • 0027463283 scopus 로고
    • Isolation and genetic characterization of ethanol-resistant reovirus mutants
    • Wessner D.R., Fields B.N. Isolation and genetic characterization of ethanol-resistant reovirus mutants. J. Virol. 1993, 67:2442-2447.
    • (1993) J. Virol. , vol.67 , pp. 2442-2447
    • Wessner, D.R.1    Fields, B.N.2
  • 75
    • 0019069749 scopus 로고
    • Fusion of Semliki forest virus with the plasma membrane can be induced by low pH
    • White J., Kartenbeck J., Helenius A. Fusion of Semliki forest virus with the plasma membrane can be induced by low pH. J. Cell Biol. 1980, 87:264-272.
    • (1980) J. Cell Biol. , vol.87 , pp. 264-272
    • White, J.1    Kartenbeck, J.2    Helenius, A.3
  • 76
    • 0019870337 scopus 로고
    • Cell fusion by Semliki Forest, influenza, and vesicular stomatitis viruses
    • White J., Matlin K., Helenius A. Cell fusion by Semliki Forest, influenza, and vesicular stomatitis viruses. J. Cell Biol. 1981, 89:674-679.
    • (1981) J. Cell Biol. , vol.89 , pp. 674-679
    • White, J.1    Matlin, K.2    Helenius, A.3
  • 77
    • 84877898099 scopus 로고    scopus 로고
    • Virus entry at a glance
    • Yamauchi Y., Helenius A. Virus entry at a glance. J. Cell Sci. 2013, 126:1289-1295.
    • (2013) J. Cell Sci. , vol.126 , pp. 1289-1295
    • Yamauchi, Y.1    Helenius, A.2
  • 78
    • 0025925091 scopus 로고
    • Bafilomycin A1, a specific inhibitor of vacuolar-type H(+)-ATPase, inhibits acidification and protein degradation in lysosomes of cultured cells
    • Yoshimori T., Yamamoto A., Moriyama Y., Futai M., Tashiro Y. Bafilomycin A1, a specific inhibitor of vacuolar-type H(+)-ATPase, inhibits acidification and protein degradation in lysosomes of cultured cells. J. Biol. Chem. 1991, 266:17707-17712.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17707-17712
    • Yoshimori, T.1    Yamamoto, A.2    Moriyama, Y.3    Futai, M.4    Tashiro, Y.5
  • 79
    • 33845419956 scopus 로고    scopus 로고
    • Reovirus m1 structural rearrangements that mediate membrane penetration
    • Zhang L., Chandran K., Nibert M.L., Harrison S.C. Reovirus m1 structural rearrangements that mediate membrane penetration. J. Virol. 2006, 80:12367-12376.
    • (2006) J. Virol. , vol.80 , pp. 12367-12376
    • Zhang, L.1    Chandran, K.2    Nibert, M.L.3    Harrison, S.C.4
  • 80
    • 26444511104 scopus 로고    scopus 로고
    • Features of reovirus outer capsid protein m1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0Å resolution
    • Zhang X., Ji Y., Zhang L., Harrison S.C., Marinescu D.C., Nibert M.L., Baker T.S. Features of reovirus outer capsid protein m1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0Å resolution. Structure 2005, 13:1545-1557.
    • (2005) Structure , vol.13 , pp. 1545-1557
    • Zhang, X.1    Ji, Y.2    Zhang, L.3    Harrison, S.C.4    Marinescu, D.C.5    Nibert, M.L.6    Baker, T.S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.