메뉴 건너뛰기




Volumn 79, Issue 8, 2005, Pages 4744-4754

Vaccinia virus H2 protein is an essential component of a complex involved in virus entry and cell-cell fusion

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN H2; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 16244373979     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.8.4744-4754.2005     Document Type: Article
Times cited : (76)

References (46)
  • 1
    • 0026532308 scopus 로고
    • Regulated expression of foreign genes in vaccinia virus under the control of bacteriophage T7 RNA polymerase and the Escherichia coli lac repressor
    • Alexander, W. A., B. Moss, and T. R. Fuerst. 1992. Regulated expression of foreign genes in vaccinia virus under the control of bacteriophage T7 RNA polymerase and the Escherichia coli lac repressor. J. Virol. 66:2934-2942.
    • (1992) J. Virol. , vol.66 , pp. 2934-2942
    • Alexander, W.A.1    Moss, B.2    Fuerst, T.R.3
  • 3
    • 0026625607 scopus 로고
    • Role of cell-associated enveloped vaccinia virus in cell-to-cell spread
    • Blasco, R., and B. Moss. 1992. Role of cell-associated enveloped vaccinia virus in cell-to-cell spread. J. Virol. 66:4170-4179.
    • (1992) J. Virol. , vol.66 , pp. 4170-4179
    • Blasco, R.1    Moss, B.2
  • 4
    • 0017071608 scopus 로고
    • Further investigations on the mode of entry of vaccinia virus into cells
    • Chang, A., and D. H. Metz. 1976. Further investigations on the mode of entry of vaccinia virus into cells. J. Gen. Virol. 32:275-282.
    • (1976) J. Gen. Virol. , vol.32 , pp. 275-282
    • Chang, A.1    Metz, D.H.2
  • 5
    • 0031906150 scopus 로고    scopus 로고
    • A27L protein mediates vaccinia virus interaction with cell surface heparan sulfate
    • Chung, C.-S., J.-C. Hsiao, Y.-S. Chang, and W. Chang. 1998. A27L protein mediates vaccinia virus interaction with cell surface heparan sulfate. J. Virol. 72:1577-1585.
    • (1998) J. Virol. , vol.72 , pp. 1577-1585
    • Chung, C.-S.1    Hsiao, J.-C.2    Chang, Y.-S.3    Chang, W.4
  • 7
    • 0026540962 scopus 로고
    • Identification and characterization of vaccinia virus genes encoding proteins that are highly antigenic in animals and are immunodominant in vaccinated humans
    • Demkowicz, W. E., J. S. Maa, and M. Esteban. 1992. Identification and characterization of vaccinia virus genes encoding proteins that are highly antigenic in animals and are immunodominant in vaccinated humans. J. Virol. 66:386-398.
    • (1992) J. Virol. , vol.66 , pp. 386-398
    • Demkowicz, W.E.1    Maa, J.S.2    Esteban, M.3
  • 8
    • 0025151572 scopus 로고
    • Fusion of intra- and extracellular forms of vaccinia virus with the cell membrane
    • Doms, R. W., R. Blumenthal, and B. Moss. 1990. Fusion of intra- and extracellular forms of vaccinia virus with the cell membrane. J. Virol. 64:4884-4892.
    • (1990) J. Virol. , vol.64 , pp. 4884-4892
    • Doms, R.W.1    Blumenthal, R.2    Moss, B.3
  • 9
    • 85025432190 scopus 로고    scopus 로고
    • Generation of recombinant vaccinia viruses
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Strahl (ed.), Greene Publishing Associates & Wiley Interscience, New York, N.Y.
    • Earl, P. L., B. Moss, L. S. Wyatt, and M. W. Carroll. 1998. Generation of recombinant vaccinia viruses, p. 16.17.1-16.17.19. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Strahl (ed.), Current protocols in molecular biology, vol. 2. Greene Publishing Associates & Wiley Interscience, New York, N.Y.
    • (1998) Current Protocols in Molecular Biology , vol.2 , pp. 16171-161719
    • Earl, P.L.1    Moss, B.2    Wyatt, L.S.3    Carroll, M.W.4
  • 10
    • 0025193184 scopus 로고
    • Vaccinia virus induces cell fusion at acid pH and this activity is mediated by the N-terminus of the 14-kDa virus envelope protein
    • Gong, S. C., C. F. Lai, and M. Esteban. 1990. Vaccinia virus induces cell fusion at acid pH and this activity is mediated by the N-terminus of the 14-kDa virus envelope protein. Virology 178:81-91.
    • (1990) Virology , vol.178 , pp. 81-91
    • Gong, S.C.1    Lai, C.F.2    Esteban, M.3
  • 11
    • 0022211611 scopus 로고
    • Golgi-derived membranes that contain an acylated viral polypeptide are used for vaccinia virus envelopment
    • Hiller, G., and K. Weber. 1985. Golgi-derived membranes that contain an acylated viral polypeptide are used for vaccinia virus envelopment. J. Virol. 55:651-659.
    • (1985) J. Virol. , vol.55 , pp. 651-659
    • Hiller, G.1    Weber, K.2
  • 12
    • 0032935036 scopus 로고    scopus 로고
    • Vaccinia virus intracellular mature virions contain only one lipid membrane
    • Hollinshead, M., A. Vanderplasschen, G. L. Smith, and D. J. Vaux. 1999. Vaccinia virus intracellular mature virions contain only one lipid membrane. J. Virol. 73:1503-1517.
    • (1999) J. Virol. , vol.73 , pp. 1503-1517
    • Hollinshead, M.1    Vanderplasschen, A.2    Smith, G.L.3    Vaux, D.J.4
  • 13
    • 0031661314 scopus 로고    scopus 로고
    • Cell surface proteoglycans are necessary for A27L protein- mediated cell fusion: Identification of the N-terminal region of A27L protein as the glycosaminoglycan-binding domain
    • Hsiao, J. C., C. S. Chung, and W. Chang. 1998. Cell surface proteoglycans are necessary for A27L protein- mediated cell fusion: identification of the N-terminal region of A27L protein as the glycosaminoglycan-binding domain. J. Virol. 72:8374-8379.
    • (1998) J. Virol. , vol.72 , pp. 8374-8379
    • Hsiao, J.C.1    Chung, C.S.2    Chang, W.3
  • 14
    • 0032844237 scopus 로고    scopus 로고
    • Vaccinia virus envelope D8L protein binds to cell surface chondroitin sulfate and mediates the adsorption of intracellular mature virions to cells
    • Hsiao, J. C., C. S. Chung, and W. Chang. 1999. Vaccinia virus envelope D8L protein binds to cell surface chondroitin sulfate and mediates the adsorption of intracellular mature virions to cells. J. Virol. 73:8750-8761.
    • (1999) J. Virol. , vol.73 , pp. 8750-8761
    • Hsiao, J.C.1    Chung, C.S.2    Chang, W.3
  • 15
    • 0029881572 scopus 로고    scopus 로고
    • Extracellular enveloped vaccinia virus escapes neutralization
    • Ichihashi, Y. 1996. Extracellular enveloped vaccinia virus escapes neutralization. Virology 217:478-485.
    • (1996) Virology , vol.217 , pp. 478-485
    • Ichihashi, Y.1
  • 16
    • 0029892864 scopus 로고    scopus 로고
    • Neutralizing epitopes on penetration protein of vaccinia virus
    • Ichihashi, Y., and M. Oie. 1996. Neutralizing epitopes on penetration protein of vaccinia virus. Virology 220:491-494.
    • (1996) Virology , vol.220 , pp. 491-494
    • Ichihashi, Y.1    Oie, M.2
  • 17
    • 0023193166 scopus 로고
    • Studies on the mechanism of entry of vaccinia virus into animal cells
    • Janeczko, R. A., J. F. Rodriguez, and M. Esteban. 1987. Studies on the mechanism of entry of vaccinia virus into animal cells. Arch. Virol. 92:135-150.
    • (1987) Arch. Virol. , vol.92 , pp. 135-150
    • Janeczko, R.A.1    Rodriguez, J.F.2    Esteban, M.3
  • 18
    • 0035983248 scopus 로고    scopus 로고
    • Inhibition of vaccinia virus replication by adenosine in BSC-40 cells: Involvement of A(2) receptor-mediated PKA activation
    • Leao-Ferreira, L. R., R. Paes-De-Carvalho, F. G. De Mello, and N. Moussatche. 2002. Inhibition of vaccinia virus replication by adenosine in BSC-40 cells: involvement of A(2) receptor-mediated PKA activation. Arch. Virol. 147:1407-1423.
    • (2002) Arch. Virol. , vol.147 , pp. 1407-1423
    • Leao-Ferreira, L.R.1    Paes-De-Carvalho, R.2    De Mello, F.G.3    Moussatche, N.4
  • 19
    • 0034012233 scopus 로고    scopus 로고
    • Vaccinia virus envelope H3L protein binds to cell surface heparan sulfate and is important for intracellular mature virion morphogenesis and virus infection in vitro and in vivo
    • Lin, C. L., C. S. Chung, H. G. Heine, and W. Chang. 2000. Vaccinia virus envelope H3L protein binds to cell surface heparan sulfate and is important for intracellular mature virion morphogenesis and virus infection in vitro and in vivo. J. Virol. 74:3353-3365.
    • (2000) J. Virol. , vol.74 , pp. 3353-3365
    • Lin, C.L.1    Chung, C.S.2    Heine, H.G.3    Chang, W.4
  • 20
    • 0033930060 scopus 로고    scopus 로고
    • Entry of the two infectious forms of vaccinia virus at the plasma membrane is signaling-dependent for the IMV but not the EEV
    • Locker, J. K., A. Kuehn, S. Schleich, G. Rutter, H. Hohenberg, R. Wepf, and G. Griffiths. 2000. Entry of the two infectious forms of vaccinia virus at the plasma membrane is signaling-dependent for the IMV but not the EEV. Mol. Biol. Cell 11:2497-2511.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2497-2511
    • Locker, J.K.1    Kuehn, A.2    Schleich, S.3    Rutter, G.4    Hohenberg, H.5    Wepf, R.6    Griffiths, G.7
  • 21
    • 0141570574 scopus 로고    scopus 로고
    • Plasma membrane budding as an alternative release mechanism of the extracellular enveloped form of vaccinia virus from HeLa cells
    • Meiser, A., C. Sancho, and J. Krijnse Locker. 2003. Plasma membrane budding as an alternative release mechanism of the extracellular enveloped form of vaccinia virus from HeLa cells. J. Virol. 77:9931-9942.
    • (2003) J. Virol. , vol.77 , pp. 9931-9942
    • Meiser, A.1    Sancho, C.2    Krijnse Locker, J.3
  • 22
    • 0001142643 scopus 로고    scopus 로고
    • Poxviridae: The viruses and their replication
    • D. M. Knipe and P. M. Howley (ed.), Lippincott Williams & Wilkins, Philadelphia, Pa.
    • Moss, B. 2001. Poxviridae: the viruses and their replication, p. 2849-2883. In D. M. Knipe and P. M. Howley (ed.), Fields virology, 4th ed., vol. 2. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology, 4th Ed. , vol.2 , pp. 2849-2883
    • Moss, B.1
  • 23
    • 0035736250 scopus 로고    scopus 로고
    • High-speed mass transit for poxviruses on microtubules
    • Moss, B., and B. M. Ward. 2001. High-speed mass transit for poxviruses on microtubules. Nat. Cell Biol. 3:E245-E246.
    • (2001) Nat. Cell Biol. , vol.3
    • Moss, B.1    Ward, B.M.2
  • 24
    • 0019199323 scopus 로고
    • Significance of extracellular virus in the in vitro and in vivo dissemination of vaccinia virus
    • Payne, L. G. 1980. Significance of extracellular virus in the in vitro and in vivo dissemination of vaccinia virus. J. Gen. Virol. 50:89-100.
    • (1980) J. Gen. Virol. , vol.50 , pp. 89-100
    • Payne, L.G.1
  • 25
    • 0028227884 scopus 로고
    • Characterization of the vaccinia virus L1R myristylprotein as a component of the intracellular virion envelope
    • Ravanello, M. P., and D. E. Hruby. 1994. Characterization of the vaccinia virus L1R myristylprotein as a component of the intracellular virion envelope. J. Gen. Virol. 75:1479-1483.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1479-1483
    • Ravanello, M.P.1    Hruby, D.E.2
  • 26
    • 0027968128 scopus 로고
    • Conditional lethal expression of the vaccinia virus L1R myristylated protein reveals a role in virus assembly
    • Ravanello, M. P., and D. E. Hruby. 1994. Conditional lethal expression of the vaccinia virus L1R myristylated protein reveals a role in virus assembly. J. Virol. 68:6401-6410.
    • (1994) J. Virol. , vol.68 , pp. 6401-6410
    • Ravanello, M.P.1    Hruby, D.E.2
  • 27
    • 0036149942 scopus 로고    scopus 로고
    • Endoplasmic reticulum-Golgi intermediate compartment membranes and vimentin filaments participate in vaccinia virus assembly
    • Risco, C., J. R. Rodriguez, C. Lopez-Iglesias, J. L. Carrascosa, M. Esteban, and D. Rodriguez. 2002. Endoplasmic reticulum-Golgi intermediate compartment membranes and vimentin filaments participate in vaccinia virus assembly. J. Virol. 76:1839-1855.
    • (2002) J. Virol. , vol.76 , pp. 1839-1855
    • Risco, C.1    Rodriguez, J.R.2    Lopez-Iglesias, C.3    Carrascosa, J.L.4    Esteban, M.5    Rodriguez, D.6
  • 28
    • 0022345294 scopus 로고
    • Isolation and characterization of neutralizing monoclonal antibodies to vaccinia virus
    • Rodriguez, J. F., R. Janeczko, and M. Esteban. 1985. Isolation and characterization of neutralizing monoclonal antibodies to vaccinia virus. J. Virol. 56:482-488.
    • (1985) J. Virol. , vol.56 , pp. 482-488
    • Rodriguez, J.F.1    Janeczko, R.2    Esteban, M.3
  • 29
    • 0023164849 scopus 로고
    • r envelope protein of vaccinia virus is involved in cell fusion and forms covalently linked trimers
    • r envelope protein of vaccinia virus is involved in cell fusion and forms covalently linked trimers. J. Virol. 61:395-404.
    • (1987) J. Virol. , vol.61 , pp. 395-404
    • Rodriguez, J.F.1    Paez, E.2    Esteban, M.3
  • 30
    • 0025001946 scopus 로고
    • IPTG-dependent vaccinia virus: Identification of a virus protein enabling virion envelopment by Golgi membrane and egress
    • Rodriguez, J. F., and G. L. Smith. 1990. IPTG-dependent vaccinia virus: identification of a virus protein enabling virion envelopment by Golgi membrane and egress. Nucleic Acids Res. 18:5347-5351.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5347-5351
    • Rodriguez, J.F.1    Smith, G.L.2
  • 31
    • 0028158628 scopus 로고
    • PHD - An automatic mail server for protein secondary structure prediction
    • Rost, B., C. Sander, and R. Schneider. 1994. PHD - an automatic mail server for protein secondary structure prediction. Comput. Appl. Biosci. 10:53-60.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 53-60
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 32
    • 0031806239 scopus 로고    scopus 로고
    • Roles of vaccinia virus EEV-specific proteins in intracellular actin tail formation and low pH-induced cell-cell fusion
    • Sanderson, C. M., F. Frischknecht, M. Way, M. Hollinshead, and G. L. Smith. 1998. Roles of vaccinia virus EEV-specific proteins in intracellular actin tail formation and low pH-induced cell-cell fusion. J. Gen. Virol. 79:1415-1425.
    • (1998) J. Gen. Virol. , vol.79 , pp. 1415-1425
    • Sanderson, C.M.1    Frischknecht, F.2    Way, M.3    Hollinshead, M.4    Smith, G.L.5
  • 33
    • 0028097957 scopus 로고
    • Assembly of vaccinia virus: The second wrapping cisterna is derived from the trans-Golgi network
    • Schmelz, M., B. Sodeik, M. Ericsson, E. J. Wolffe, H. Shida, G. Hilier, and G. Griffiths. 1994. Assembly of vaccinia virus: the second wrapping cisterna is derived from the trans-Golgi network. J. Virol. 68:130-147.
    • (1994) J. Virol. , vol.68 , pp. 130-147
    • Schmelz, M.1    Sodeik, B.2    Ericsson, M.3    Wolffe, E.J.4    Shida, H.5    Hilier, G.6    Griffiths, G.7
  • 34
    • 1242296981 scopus 로고    scopus 로고
    • Vaccinia virus A28L gene encodes an essential protein component of the virion membrane with intramolecular disulfide bonds formed by the viral cytoplasmic redox pathway
    • Senkevich, T. G., B. M. Ward, and B. Moss. 2004. Vaccinia virus A28L gene encodes an essential protein component of the virion membrane with intramolecular disulfide bonds formed by the viral cytoplasmic redox pathway. J. Virol. 78:2348-2356.
    • (2004) J. Virol. , vol.78 , pp. 2348-2356
    • Senkevich, T.G.1    Ward, B.M.2    Moss, B.3
  • 35
    • 1242342126 scopus 로고    scopus 로고
    • Vaccinia virus entry into cells is dependent on a virion surface protein encoded by the A28L gene
    • Senkevich, T. G., B. M. Ward, and B. Moss. 2004. Vaccinia virus entry into cells is dependent on a virion surface protein encoded by the A28L gene. J. Virol. 78:2357-2366.
    • (2004) J. Virol. , vol.78 , pp. 2357-2366
    • Senkevich, T.G.1    Ward, B.M.2    Moss, B.3
  • 36
    • 0037076339 scopus 로고    scopus 로고
    • Complete pathway for protein disulfide bond formation encoded by poxviruses
    • Senkevich, T. G., C. L. White, E. V. Koonin, and B. Moss. 2002. Complete pathway for protein disulfide bond formation encoded by poxviruses. Proc. Natl. Acad. Sci. USA 99:6667-6672.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6667-6672
    • Senkevich, T.G.1    White, C.L.2    Koonin, E.V.3    Moss, B.4
  • 38
    • 0017067118 scopus 로고
    • High-voltage electron microscope study of the release of vaccinia virus from whole cells
    • Stokes, G. V. 1976. High-voltage electron microscope study of the release of vaccinia virus from whole cells. J. Virol. 18:636-643.
    • (1976) J. Virol. , vol.18 , pp. 636-643
    • Stokes, G.V.1
  • 39
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 40
    • 0027530255 scopus 로고
    • Progeny vaccinia and human cytomegalovirus particles utilize early endosomal cisternae for their envelopes
    • Tooze, J., M. Hollinshead, B. Reis, K. Radsak, and H. Kern. 1993. Progeny vaccinia and human cytomegalovirus particles utilize early endosomal cisternae for their envelopes. Eur. J. Cell Biol. 60:163-178.
    • (1993) Eur. J. Cell Biol. , vol.60 , pp. 163-178
    • Tooze, J.1    Hollinshead, M.2    Reis, B.3    Radsak, K.4    Kern, H.5
  • 41
    • 0021034620 scopus 로고
    • Release of vaccinia virus from FL cells infected with the IHD-W strain
    • Tsutsui, K. 1983. Release of vaccinia virus from FL cells infected with the IHD-W strain. J. Electron Microsc. 32:125-140.
    • (1983) J. Electron. Microsc. , vol.32 , pp. 125-140
    • Tsutsui, K.1
  • 42
    • 0031949903 scopus 로고    scopus 로고
    • Intracellular and extracellular vaccinia virions enter cells by different mechanisms
    • Vanderplasschen, A., M. Hollinshead, and G. L. Smith. 1998. Intracellular and extracellular vaccinia virions enter cells by different mechanisms. J. Gen. Virol. 79:877-887.
    • (1998) J. Gen. Virol. , vol.79 , pp. 877-887
    • Vanderplasschen, A.1    Hollinshead, M.2    Smith, G.L.3
  • 43
    • 0345411634 scopus 로고    scopus 로고
    • Identification of functional domains in the 14-kilodalton envelope protein (A27L) of vaccinia virus
    • Vazquez, M. I., and M. Esteban. 1999. Identification of functional domains in the 14-kilodalton envelope protein (A27L) of vaccinia virus. J. Virol. 73:9098-9109.
    • (1999) J. Virol. , vol.73 , pp. 9098-9109
    • Vazquez, M.I.1    Esteban, M.2
  • 44
    • 1242274535 scopus 로고    scopus 로고
    • Vaccinia virus A36R membrane protein provides a direct link between intracellular enveloped virions and the microtubule motor kinesin
    • Ward, B. M., and B. Moss. 2004. Vaccinia virus A36R membrane protein provides a direct link between intracellular enveloped virions and the microtubule motor kinesin. J. Virol. 78:2486-2493.
    • (2004) J. Virol. , vol.78 , pp. 2486-2493
    • Ward, B.M.1    Moss, B.2
  • 45
    • 0027162408 scopus 로고
    • Deletion of the vaccinia virus B5R gene encoding a 42-kilodalton membrane glycoprotein inhibits extracellular virus envelope formation and dissemination
    • Wolffe, E. J., S. N. Isaacs, and B. Moss. 1993. Deletion of the vaccinia virus B5R gene encoding a 42-kilodalton membrane glycoprotein inhibits extracellular virus envelope formation and dissemination. J. Virol. 67:4732-4741.
    • (1993) J. Virol. , vol.67 , pp. 4732-4741
    • Wolffe, E.J.1    Isaacs, S.N.2    Moss, B.3
  • 46
    • 0029103360 scopus 로고
    • A myristylated membrane protein encoded by the vaccinia virus L1R open reading frame is the target of potent neutralizing monoclonal antibodies
    • Wolffe, E. J., S. Vijaya, and B. Moss. 1995. A myristylated membrane protein encoded by the vaccinia virus L1R open reading frame is the target of potent neutralizing monoclonal antibodies. Virology 211:53-63.
    • (1995) Virology , vol.211 , pp. 53-63
    • Wolffe, E.J.1    Vijaya, S.2    Moss, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.