메뉴 건너뛰기




Volumn 8, Issue 11, 2008, Pages 861-873

Cross-regulation between herpesviruses and the TNF superfamily members

Author keywords

[No Author keywords available]

Indexed keywords

BETA INTERFERON; CASPASE; DEATH RECEPTOR; HEPARAN SULFATE; HERPESVIRUS ENTRY MEDIATOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MEMBRANE PROTEIN; NECTIN 1; NECTIN 2; PROTEIN K15; PROTEIN LMP1; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RECEPTOR; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND RECEPTOR; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN;

EID: 54949093178     PISSN: 14741733     EISSN: None     Source Type: Journal    
DOI: 10.1038/nri2434     Document Type: Review
Times cited : (61)

References (169)
  • 1
    • 33645054794 scopus 로고    scopus 로고
    • Topics in herpesvirus genomics and evolution
    • McGeoch, D. J., Rixon, F. J. & Davison, A. J. Topics in herpesvirus genomics and evolution. Virus Res. 117, 90-104 (2006).
    • (2006) Virus Res , vol.117 , pp. 90-104
    • McGeoch, D.J.1    Rixon, F.J.2    Davison, A.J.3
  • 2
    • 2942579946 scopus 로고    scopus 로고
    • Escape of mutant double-stranded DNA virus from innate immune control
    • French, A. R. et al. Escape of mutant double-stranded DNA virus from innate immune control. Immunity 20, 747-756 (2004).
    • (2004) Immunity , vol.20 , pp. 747-756
    • French, A.R.1
  • 3
    • 34250212068 scopus 로고    scopus 로고
    • Early diversification of the TNF superfamily in teleosts: Genomic characterization and expression analysis
    • Glenney, G. W. & Wiens, G. D. Early diversification of the TNF superfamily in teleosts: genomic characterization and expression analysis. J. Immunol. 178, 7955-7973 (2007).
    • (2007) J. Immunol , vol.178 , pp. 7955-7973
    • Glenney, G.W.1    Wiens, G.D.2
  • 4
    • 0242669384 scopus 로고    scopus 로고
    • All in the family: Evolutionary and functional relationships among death receptors
    • Bridgham, J. T., Wilder, J. A., Hollocher, H. & Johnson, A. L. All in the family: evolutionary and functional relationships among death receptors. Cell. Death Differ. 10, 19-25 (2003).
    • (2003) Cell. Death Differ , vol.10 , pp. 19-25
    • Bridgham, J.T.1    Wilder, J.A.2    Hollocher, H.3    Johnson, A.L.4
  • 5
    • 17644400505 scopus 로고    scopus 로고
    • Network communications: Lymphotoxins, LIGHT, and TNF
    • Ware, C. F. Network communications: lymphotoxins, LIGHT, and TNF. Annu. Rev. Immunol. 23, 787-819 (2005).
    • (2005) Annu. Rev. Immunol , vol.23 , pp. 787-819
    • Ware, C.F.1
  • 6
    • 33645788091 scopus 로고    scopus 로고
    • Modulation of tumor necrosis factor by microbial pathogens
    • Rahman, M. M. & McFadden, G. Modulation of tumor necrosis factor by microbial pathogens. PLoS Pathog. 2, e4 (2006).
    • (2006) PLoS Pathog , vol.2
    • Rahman, M.M.1    McFadden, G.2
  • 8
    • 0037290767 scopus 로고    scopus 로고
    • Death and survival: Viral regulation of TNF signaling pathways
    • Benedict, C. A., Banks, T. A. & Ware, C. F. Death and survival: viral regulation of TNF signaling pathways. Curr. Opin. Immunol. 15, 59-65 (2003).
    • (2003) Curr. Opin. Immunol , vol.15 , pp. 59-65
    • Benedict, C.A.1    Banks, T.A.2    Ware, C.F.3
  • 9
    • 0025880218 scopus 로고
    • Myxoma virus expresses a secreted protein with homology to the tumor necrosis factor receptor gene family that contributes to viral virulence
    • Upton, C., Macen, J., Schreiber, M. & McFadden, G. Myxoma virus expresses a secreted protein with homology to the tumor necrosis factor receptor gene family that contributes to viral virulence. Virology 184, 370-382 (1991).
    • (1991) Virology , vol.184 , pp. 370-382
    • Upton, C.1    Macen, J.2    Schreiber, M.3    McFadden, G.4
  • 10
    • 0141632878 scopus 로고    scopus 로고
    • Herpesvirus entry: An update
    • Spear, P. G. & Longnecker, R. Herpesvirus entry: an update. J. Virol. 77, 10179-10185 (2003).
    • (2003) J. Virol , vol.77 , pp. 10179-10185
    • Spear, P.G.1    Longnecker, R.2
  • 11
    • 0031801093 scopus 로고    scopus 로고
    • Epstein-Barr virus uses different complexes of glycoproteins gH and gL to infect B lymphocytes and epithelial cells
    • Wang, X., Kenyon, W. J., Li, Q., Mullberg, J. & Hutt-Fletcher, L. M. Epstein-Barr virus uses different complexes of glycoproteins gH and gL to infect B lymphocytes and epithelial cells. J. Virol. 72, 5552-5558 (1998).
    • (1998) J. Virol , vol.72 , pp. 5552-5558
    • Wang, X.1    Kenyon, W.J.2    Li, Q.3    Mullberg, J.4    Hutt-Fletcher, L.M.5
  • 12
    • 29144522907 scopus 로고    scopus 로고
    • Human cytomegalovirus virion protein complex required for epithelial and endothelial cell tropism
    • Wang, D. & Shenk, T. Human cytomegalovirus virion protein complex required for epithelial and endothelial cell tropism. Proc. Natl Acad. Sci USA 102, 18153-18158 (2005).
    • (2005) Proc. Natl Acad. Sci USA , vol.102 , pp. 18153-18158
    • Wang, D.1    Shenk, T.2
  • 13
    • 37149049377 scopus 로고    scopus 로고
    • Herpes simplex virus type 2 glycoprotein G is targeted by the sulfated oligo- and polysaccharide inhibitors of virus attachment to cells
    • Adamiak, B., Ekblad, M., Bergstrom, T., Ferro, V. & Trybala, E. Herpes simplex virus type 2 glycoprotein G is targeted by the sulfated oligo- and polysaccharide inhibitors of virus attachment to cells. J. Virol. 81, 13424-13434 (2007).
    • (2007) J. Virol , vol.81 , pp. 13424-13434
    • Adamiak, B.1    Ekblad, M.2    Bergstrom, T.3    Ferro, V.4    Trybala, E.5
  • 14
    • 0034883314 scopus 로고    scopus 로고
    • Herpesviruses and heparan sulfate: An intimate relationship in aid of viral entry
    • Shukla, D. & Spear, P. G. Herpesviruses and heparan sulfate: an intimate relationship in aid of viral entry. J. Clin. Invest. 108, 503-510 (2001).
    • (2001) J. Clin. Invest , vol.108 , pp. 503-510
    • Shukla, D.1    Spear, P.G.2
  • 15
    • 1842850945 scopus 로고    scopus 로고
    • Herpes simplex virus: Receptors and ligands for cell entry
    • Spear, P. G. Herpes simplex virus: receptors and ligands for cell entry. Cell. Microbiol. 6, 401-410 (2004).
    • (2004) Cell. Microbiol , vol.6 , pp. 401-410
    • Spear, P.G.1
  • 16
    • 40749106962 scopus 로고    scopus 로고
    • PILRα is a herpes simplex virus-1 entry co-receptor that associates with glycoprotein B
    • This recent paper indicates that PILRα is a new entry factor for HSV-1 and shows that the viral glycoprotein gB can also mediate specific viral attachment to host cells
    • Satoh, T. et al. PILRα is a herpes simplex virus-1 entry co-receptor that associates with glycoprotein B. Cell 132, 935-944 (2008). This recent paper indicates that PILRα is a new entry factor for HSV-1 and shows that the viral glycoprotein gB can also mediate specific viral attachment to host cells.
    • (2008) Cell , vol.132 , pp. 935-944
    • Satoh, T.1
  • 17
    • 28644433999 scopus 로고    scopus 로고
    • Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry
    • Krummenacher, C. et al. Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry. EMBO J. 24, 4144-4153 (2005).
    • (2005) EMBO J , vol.24 , pp. 4144-4153
    • Krummenacher, C.1
  • 18
    • 0031797729 scopus 로고    scopus 로고
    • The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cells
    • Cocchi, F., Menotti, L., Mirandola, P., Lopez, M. & Campadelli-Fiume, G. The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cells. J. Virol. 72, 9992-10002 (1998).
    • (1998) J. Virol , vol.72 , pp. 9992-10002
    • Cocchi, F.1    Menotti, L.2    Mirandola, P.3    Lopez, M.4    Campadelli-Fiume, G.5
  • 19
    • 0030298375 scopus 로고    scopus 로고
    • Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family
    • This report identifies HVEM as the entry receptor for HSV-1
    • Montgomery, R. I., Warner, M. S., Lum, B. J. & Spear, P. G. Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. Cell 87, 427-436 (1996). This report identifies HVEM as the entry receptor for HSV-1.
    • (1996) Cell , vol.87 , pp. 427-436
    • Montgomery, R.I.1    Warner, M.S.2    Lum, B.J.3    Spear, P.G.4
  • 20
    • 20744443183 scopus 로고    scopus 로고
    • Nectin-1/HveC mediates herpes simplex virus type 1 entry into primary human sensory neurons and fibroblasts
    • Simpson, S. A. et al. Nectin-1/HveC mediates herpes simplex virus type 1 entry into primary human sensory neurons and fibroblasts. J. Neurovirol. 11, 208-218 (2005).
    • (2005) J. Neurovirol , vol.11 , pp. 208-218
    • Simpson, S.A.1
  • 21
    • 4344584510 scopus 로고    scopus 로고
    • Mutations in herpes simplex virus glycoprotein D that prevent cell entry via nectins and alter cell tropism
    • Manoj, S., Jogger, C. R., Myscofski, D., Yoon, M. & Spear, P. G. Mutations in herpes simplex virus glycoprotein D that prevent cell entry via nectins and alter cell tropism. Proc. Natl Acad. Sci. USA 101, 12414-12421 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 12414-12421
    • Manoj, S.1    Jogger, C.R.2    Myscofski, D.3    Yoon, M.4    Spear, P.G.5
  • 22
    • 34347344995 scopus 로고    scopus 로고
    • Alternative entry receptors for herpes simplex virus and their roles in disease
    • This recent report is the first to show the specific contributions of each HSV-2 entry receptor in vivo, indicating that although either HVEM or nectin-1 can mediate infection, nectin-1 is mainly responsible for the formation of external lesions and neuronal infection
    • Taylor, J. M. et al. Alternative entry receptors for herpes simplex virus and their roles in disease. Cell Host Microbe 2, 19-28 (2007). This recent report is the first to show the specific contributions of each HSV-2 entry receptor in vivo, indicating that although either HVEM or nectin-1 can mediate infection, nectin-1 is mainly responsible for the formation of external lesions and neuronal infection.
    • (2007) Cell Host Microbe , vol.2 , pp. 19-28
    • Taylor, J.M.1
  • 23
    • 33745865949 scopus 로고    scopus 로고
    • The DARC conspiracy - virus invasion tactics
    • Kinkade, A. & Ware, C. F. The DARC conspiracy - virus invasion tactics. Trends Immunol. 27, 362-367 (2006).
    • (2006) Trends Immunol , vol.27 , pp. 362-367
    • Kinkade, A.1    Ware, C.F.2
  • 24
    • 23844431675 scopus 로고    scopus 로고
    • The nectin-1α transmembrane domain, but not the cytoplasmic tail, influences cell fusion induced by HSV-1 glycoproteins
    • Subramanian, R. P., Dunn, J. E. & Geraghty, R. J. The nectin-1α transmembrane domain, but not the cytoplasmic tail, influences cell fusion induced by HSV-1 glycoproteins. Virology 339, 176-191 (2005).
    • (2005) Virology , vol.339 , pp. 176-191
    • Subramanian, R.P.1    Dunn, J.E.2    Geraghty, R.J.3
  • 25
    • 0030793175 scopus 로고    scopus 로고
    • Glycoprotein D of herpes simplex virus (HSV) binds directly to HVEM, a member of the tumor necrosis factor receptor superfamily and a mediator of HSV entry
    • Whitbeck, J. C. et al. Glycoprotein D of herpes simplex virus (HSV) binds directly to HVEM, a member of the tumor necrosis factor receptor superfamily and a mediator of HSV entry. J. Virol. 71, 6083-6093 (1997).
    • (1997) J. Virol , vol.71 , pp. 6083-6093
    • Whitbeck, J.C.1
  • 26
    • 0031907988 scopus 로고    scopus 로고
    • LIGHT, a new member of the TNF superfamily, and lymphotoxin α are ligands for herpesvirus entry mediator
    • Mauri, D. N. et al. LIGHT, a new member of the TNF superfamily, and lymphotoxin α are ligands for herpesvirus entry mediator. Immunity 8, 21-30 (1998).
    • (1998) Immunity , vol.8 , pp. 21-30
    • Mauri, D.N.1
  • 27
    • 19944433635 scopus 로고    scopus 로고
    • B and T lymphocyte attenuator regulates T cell activation through interaction with herpesvirus entry mediator
    • Sedy, J. R. et al. B and T lymphocyte attenuator regulates T cell activation through interaction with herpesvirus entry mediator. Nature Immunol. 6, 90-98 (2005).
    • (2005) Nature Immunol , vol.6 , pp. 90-98
    • Sedy, J.R.1
  • 28
    • 38349149016 scopus 로고    scopus 로고
    • + T cells through interaction with herpesvirus entry mediator
    • + T cells through interaction with herpesvirus entry mediator. Nature Immunol. 9, 176-185 (2008).
    • (2008) Nature Immunol , vol.9 , pp. 176-185
    • Cai, G.1
  • 29
    • 9644302462 scopus 로고    scopus 로고
    • Lymphotoxin and LIGHT signaling pathways and target genes
    • Schneider, K., Potter, K. G. & Ware, C. F. Lymphotoxin and LIGHT signaling pathways and target genes. Immunol. Rev. 202, 49-66 (2004).
    • (2004) Immunol. Rev , vol.202 , pp. 49-66
    • Schneider, K.1    Potter, K.G.2    Ware, C.F.3
  • 30
    • 33748088535 scopus 로고    scopus 로고
    • Balancing co-stimulation and inhibition with BTLA and HVEM
    • Murphy, K. M., Nelson, C. A. & Sedy, J. R. Balancing co-stimulation and inhibition with BTLA and HVEM. Nature Rev. Immunol. 6, 671-681 (2006).
    • (2006) Nature Rev. Immunol , vol.6 , pp. 671-681
    • Murphy, K.M.1    Nelson, C.A.2    Sedy, J.R.3
  • 31
    • 0035936797 scopus 로고    scopus 로고
    • The TNF and TNF receptor superfamilies: Integrating mammalian biology
    • Locksley, R. M., Killeen, N. & Lenardo, M. J. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 104, 487-501 (2001).
    • (2001) Cell , vol.104 , pp. 487-501
    • Locksley, R.M.1    Killeen, N.2    Lenardo, M.J.3
  • 32
    • 0036162436 scopus 로고    scopus 로고
    • The molecular architecture of the TNF superfamily
    • Bodmer, J. L., Schneider, P. & Tschopp, J. The molecular architecture of the TNF superfamily. Trends Biochem. Sci. 27, 19-26 (2002).
    • (2002) Trends Biochem. Sci , vol.27 , pp. 19-26
    • Bodmer, J.L.1    Schneider, P.2    Tschopp, J.3
  • 33
    • 28244498658 scopus 로고    scopus 로고
    • Attenuating lymphocyte activity: The crystal structure of the BTLA-HVEM complex
    • Compaan, D. M. et al. Attenuating lymphocyte activity: the crystal structure of the BTLA-HVEM complex. J. Biol. Chem. 280, 39553-39561 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 39553-39561
    • Compaan, D.M.1
  • 34
    • 12844268068 scopus 로고    scopus 로고
    • Gonzalez, L. C. et al. A coreceptor interaction between the CD28 and TNF receptor family members B and T lymphocyte attenuator and herpesvirus entry mediator. Proc. Natl Acad. Sci. USA 102, 1116-1121 (2005). This study, together with reference 27, identifies BTLA as the natural ligand for HVEM and shows that HVEM ligation of T-cell-expressed BTLA results in inhibition of T-cell activation.
    • Gonzalez, L. C. et al. A coreceptor interaction between the CD28 and TNF receptor family members B and T lymphocyte attenuator and herpesvirus entry mediator. Proc. Natl Acad. Sci. USA 102, 1116-1121 (2005). This study, together with reference 27, identifies BTLA as the natural ligand for HVEM and shows that HVEM ligation of T-cell-expressed BTLA results in inhibition of T-cell activation.
  • 35
    • 24944486256 scopus 로고    scopus 로고
    • Cheung, T. C. et al. Evolutionarily divergent herpesviruses modulate T cell activation by targeting the herpesvirus entry mediator cosignaling pathway. Proc. Natl Acad. Sci. USA 102, 13218-13223 (2005). In this study, the authors show that the CMV homologue of HVEM UL144 selectively interacts with the HVEM ligand BTLA and that UL144 can inhibit T-cell responses.
    • Cheung, T. C. et al. Evolutionarily divergent herpesviruses modulate T cell activation by targeting the herpesvirus entry mediator cosignaling pathway. Proc. Natl Acad. Sci. USA 102, 13218-13223 (2005). In this study, the authors show that the CMV homologue of HVEM UL144 selectively interacts with the HVEM ligand BTLA and that UL144 can inhibit T-cell responses.
  • 36
    • 0034892857 scopus 로고    scopus 로고
    • Herpes simplex virus glycoprotein D bound to the human receptor HveA
    • Carfi, A. et al. Herpes simplex virus glycoprotein D bound to the human receptor HveA. Mol. Cell 8, 169-179 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 169-179
    • Carfi, A.1
  • 37
    • 1242343695 scopus 로고    scopus 로고
    • Activation of natural killer cells and dendritic cells upon recognition of a novel CD99-like ligand by paired immunoglobulin-like type 2 receptor
    • Shiratori, I., Ogasawara, K., Saito, T., Lanier, L. L. & Arase, H. Activation of natural killer cells and dendritic cells upon recognition of a novel CD99-like ligand by paired immunoglobulin-like type 2 receptor. J. Exp. Med. 199, 525-533 (2004).
    • (2004) J. Exp. Med , vol.199 , pp. 525-533
    • Shiratori, I.1    Ogasawara, K.2    Saito, T.3    Lanier, L.L.4    Arase, H.5
  • 38
    • 0034254317 scopus 로고    scopus 로고
    • FDF03, a novel inhibitory receptor of the immunoglobulin superfamily, is expressed by human dendritic and myeloid cells
    • Fournier, N. et al. FDF03, a novel inhibitory receptor of the immunoglobulin superfamily, is expressed by human dendritic and myeloid cells. J. Immunol. 165, 1197-1209 (2000).
    • (2000) J. Immunol , vol.165 , pp. 1197-1209
    • Fournier, N.1
  • 39
    • 0034635222 scopus 로고    scopus 로고
    • PILRα, a novel immunoreceptor tyrosine-based inhibitory motif-bearing protein, recruits SHP-1 upon tyrosine phosphorylation and is paired with the truncated counterpart PILRβ
    • Mousseau, D. D., Banville, D., L'Abbe, D., Bouchard, P. & Shen, S. H. PILRα, a novel immunoreceptor tyrosine-based inhibitory motif-bearing protein, recruits SHP-1 upon tyrosine phosphorylation and is paired with the truncated counterpart PILRβ. J. Biol. Chem. 275, 4467-4474 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 4467-4474
    • Mousseau, D.D.1    Banville, D.2    L'Abbe, D.3    Bouchard, P.4    Shen, S.H.5
  • 40
    • 21744442561 scopus 로고    scopus 로고
    • Rapid divergency of rodent CD99 orthologs: Implications for the evolution of the pseudoautosomal region
    • Park, S. H. et al. Rapid divergency of rodent CD99 orthologs: implications for the evolution of the pseudoautosomal region. Gene 353, 177-188 (2005).
    • (2005) Gene , vol.353 , pp. 177-188
    • Park, S.H.1
  • 41
    • 0032129268 scopus 로고    scopus 로고
    • Herpes simplex type 1 induction of persistent NF-κB nuclear translocation increases the efficiency of virus replication
    • Patel, A. et al. Herpes simplex type 1 induction of persistent NF-κB nuclear translocation increases the efficiency of virus replication. Virology 247, 212-222 (1998).
    • (1998) Virology , vol.247 , pp. 212-222
    • Patel, A.1
  • 42
    • 33646372984 scopus 로고    scopus 로고
    • Herpes simplex virus disrupts NF-κB regulation by blocking its recruitment on the IκBα promoter and directing the factor on viral genes
    • Amici, C. et al. Herpes simplex virus disrupts NF-κB regulation by blocking its recruitment on the IκBα promoter and directing the factor on viral genes. J. Biol. Chem. 281, 7110-7117 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 7110-7117
    • Amici, C.1
  • 43
    • 6344256840 scopus 로고    scopus 로고
    • Cells lacking NF-κB or in which NF-κB is not activated vary with respect to ability to sustain herpes simplex virus 1 replication and are not susceptible to apoptosis induced by a replication-incompetent mutant virus
    • Taddeo, B., Zhang, W., Lakeman, F. & Roizman, B. Cells lacking NF-κB or in which NF-κB is not activated vary with respect to ability to sustain herpes simplex virus 1 replication and are not susceptible to apoptosis induced by a replication-incompetent mutant virus. J. Virol. 78, 11615-11621 (2004).
    • (2004) J. Virol , vol.78 , pp. 11615-11621
    • Taddeo, B.1    Zhang, W.2    Lakeman, F.3    Roizman, B.4
  • 44
    • 0141704330 scopus 로고    scopus 로고
    • Protection by herpes simplex virus glycoprotein D against Fas-mediated apoptosis: Role of nuclear factor κB
    • Medici, M. A. et al. Protection by herpes simplex virus glycoprotein D against Fas-mediated apoptosis: role of nuclear factor κB. J. Biol. Chem. 278, 36059-36067 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 36059-36067
    • Medici, M.A.1
  • 45
    • 34247219205 scopus 로고    scopus 로고
    • Signaling pathway used by HSV-1 to induce NF-κB activation: Possible role of herpes virus entry receptor A
    • Sciortino, M. T. et al. Signaling pathway used by HSV-1 to induce NF-κB activation: possible role of herpes virus entry receptor A. Ann. N.Y. Acad. Sci. 1096, 89-96 (2007).
    • (2007) Ann. N.Y. Acad. Sci , vol.1096 , pp. 89-96
    • Sciortino, M.T.1
  • 46
    • 24744464366 scopus 로고    scopus 로고
    • Focal adhesion kinase plays a pivotal role in herpes simplex virus entry
    • Cheshenko, N., Liu, W., Satlin, L. M. & Herold, B. C. Focal adhesion kinase plays a pivotal role in herpes simplex virus entry. J. Biol. Chem. 280, 31116-31125 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 31116-31125
    • Cheshenko, N.1    Liu, W.2    Satlin, L.M.3    Herold, B.C.4
  • 47
    • 34547735905 scopus 로고    scopus 로고
    • Multiple receptor interactions trigger release of membrane and intracellular calcium stores critical for herpes simplex virus entry
    • Cheshenko, N., Liu, W., Satlin, L. M. & Herold, B. C. Multiple receptor interactions trigger release of membrane and intracellular calcium stores critical for herpes simplex virus entry. Mol. Biol. Cell 18, 3119-3130 (2007).
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3119-3130
    • Cheshenko, N.1    Liu, W.2    Satlin, L.M.3    Herold, B.C.4
  • 48
    • 38449099587 scopus 로고    scopus 로고
    • HVEM signaling in monocytes is mediated by intracellular calcium mobilization
    • Heo, S. K. et al. HVEM signaling in monocytes is mediated by intracellular calcium mobilization. J. Immunol. 179, 6305-6310 (2007).
    • (2007) J. Immunol , vol.179 , pp. 6305-6310
    • Heo, S.K.1
  • 49
    • 0037637670 scopus 로고    scopus 로고
    • La, S., Kim, J., Kwon, B. S. & Kwon, B. Herpes simplex virus type 1 glycoprotein D inhibits T-cell proliferation. Mol. Cells 14, 398-403 (2002).
    • La, S., Kim, J., Kwon, B. S. & Kwon, B. Herpes simplex virus type 1 glycoprotein D inhibits T-cell proliferation. Mol. Cells 14, 398-403 (2002).
  • 50
    • 31144453873 scopus 로고    scopus 로고
    • Inhibition of TCR signaling by herpes simplex virus
    • Sloan, D. D. et al. Inhibition of TCR signaling by herpes simplex virus. J. Immunol. 176, 1825-1833 (2006).
    • (2006) J. Immunol , vol.176 , pp. 1825-1833
    • Sloan, D.D.1
  • 51
    • 0028301850 scopus 로고
    • + T-cell clones recovered from recurrent genital herpes simplex virus type 2 lesions
    • + T-cell clones recovered from recurrent genital herpes simplex virus type 2 lesions. J. Virol. 68, 2803-2810 (1994).
    • (1994) J. Virol , vol.68 , pp. 2803-2810
    • Koelle, D.M.1
  • 52
    • 0001585502 scopus 로고    scopus 로고
    • Clearance of HSV-2 from recurrent genital lesions correlates with infiltration of HSV-specific cytotoxic T lymphocytes
    • Koelle, D. M. et al. Clearance of HSV-2 from recurrent genital lesions correlates with infiltration of HSV-specific cytotoxic T lymphocytes. J. Clin. Invest. 101, 1500-1508 (1998).
    • (1998) J. Clin. Invest , vol.101 , pp. 1500-1508
    • Koelle, D.M.1
  • 53
    • 33947424353 scopus 로고    scopus 로고
    • + T cells accumulate near sensory nerve endings in genital skin during subclinical HSV-2 reactivation
    • + T cells accumulate near sensory nerve endings in genital skin during subclinical HSV-2 reactivation. J. Exp. Med. 204, 595-603 (2007).
    • (2007) J. Exp. Med , vol.204 , pp. 595-603
    • Zhu, J.1
  • 54
    • 0037271850 scopus 로고    scopus 로고
    • Viral mimicry of cytokines, chemokines and their receptors
    • Alcami, A. Viral mimicry of cytokines, chemokines and their receptors. Nature Rev. Immunol. 3, 36-50 (2003).
    • (2003) Nature Rev. Immunol , vol.3 , pp. 36-50
    • Alcami, A.1
  • 55
    • 0013098971 scopus 로고    scopus 로고
    • Poxviruses and immune evasion
    • Seet, B. T. et al. Poxviruses and immune evasion. Annu. Rev. Immunol. 21, 377-423 (2003).
    • (2003) Annu. Rev. Immunol , vol.21 , pp. 377-423
    • Seet, B.T.1
  • 56
    • 34147136559 scopus 로고    scopus 로고
    • Myxoma virus in the European rabbit: Interactions between the virus and its susceptible host
    • Stanford, M. M., Werden, S. J. & McFadden, G. Myxoma virus in the European rabbit: interactions between the virus and its susceptible host. Vet. Res. 38, 299-318 (2007).
    • (2007) Vet. Res , vol.38 , pp. 299-318
    • Stanford, M.M.1    Werden, S.J.2    McFadden, G.3
  • 57
    • 0037333399 scopus 로고    scopus 로고
    • Transmembrane domains 1 and 2 of the latent membrane protein 1 of Epstein-Barr virus contain a lipid raft targeting signal and play a critical role in cytostasis
    • Coffin, W. F. 3rd, Geiger, T. R. & Martin, J. M. Transmembrane domains 1 and 2 of the latent membrane protein 1 of Epstein-Barr virus contain a lipid raft targeting signal and play a critical role in cytostasis. J. Virol. 77, 3749-3758 (2003).
    • (2003) J. Virol , vol.77 , pp. 3749-3758
    • Coffin 3rd, W.F.1    Geiger, T.R.2    Martin, J.M.3
  • 58
    • 0037938602 scopus 로고    scopus 로고
    • LMP1, a viral relative of the TNF receptor family, signals principally from intracellular compartments
    • Lam, N. & Sugden, B. LMP1, a viral relative of the TNF receptor family, signals principally from intracellular compartments. EMBO J. 22, 3027-3038 (2003).
    • (2003) EMBO J , vol.22 , pp. 3027-3038
    • Lam, N.1    Sugden, B.2
  • 59
    • 33646161719 scopus 로고    scopus 로고
    • Regulation of intracellular signalling by the terminal membrane proteins of members of the gammaherpesvirinae
    • Brinkmann, M. M. & Schulz, T. F. Regulation of intracellular signalling by the terminal membrane proteins of members of the gammaherpesvirinae. J. Gen. Virol. 87, 1047-1074 (2006).
    • (2006) J. Gen. Virol , vol.87 , pp. 1047-1074
    • Brinkmann, M.M.1    Schulz, T.F.2
  • 60
    • 84934436278 scopus 로고    scopus 로고
    • LMP1 TRAFficking activates growth and survival pathways
    • Soni, V., Cahir-McFarland, E. & Kieff, E. LMP1 TRAFficking activates growth and survival pathways. Adv. Exp. Med. Biol. 597, 173-187 (2007).
    • (2007) Adv. Exp. Med. Biol , vol.597 , pp. 173-187
    • Soni, V.1    Cahir-McFarland, E.2    Kieff, E.3
  • 61
    • 1542313888 scopus 로고    scopus 로고
    • Requirement for TRAF3 in signaling by LMP1 but not CD40 in B lymphocytes
    • Xie, P., Hostager, B. S. & Bishop, G. A. Requirement for TRAF3 in signaling by LMP1 but not CD40 in B lymphocytes. J. Exp. Med. 199, 661-671 (2004).
    • (2004) J. Exp. Med , vol.199 , pp. 661-671
    • Xie, P.1    Hostager, B.S.2    Bishop, G.A.3
  • 62
    • 6344272092 scopus 로고    scopus 로고
    • Roles of TNF receptor-associated factor 3 in signaling to B lymphocytes by carboxyl-terminal activating regions 1 and 2 of the EBV-encoded oncoprotein latent membrane protein 1
    • Xie, P. & Bishop, G. A. Roles of TNF receptor-associated factor 3 in signaling to B lymphocytes by carboxyl-terminal activating regions 1 and 2 of the EBV-encoded oncoprotein latent membrane protein 1. J. Immunol. 173, 5546-5555 (2004).
    • (2004) J. Immunol , vol.173 , pp. 5546-5555
    • Xie, P.1    Bishop, G.A.2
  • 63
    • 25844450231 scopus 로고    scopus 로고
    • LMP1 protein from the Epstein-Barr virus is a structural CD40 decoy in B lymphocytes for binding to TRAF3
    • Wu, S. et al. LMP1 protein from the Epstein-Barr virus is a structural CD40 decoy in B lymphocytes for binding to TRAF3. J. Biol. Chem. 280, 33620-33626 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 33620-33626
    • Wu, S.1
  • 64
    • 37349127804 scopus 로고    scopus 로고
    • EBV latent membrane protein 1 activates Akt, NFκB, and Stat3 in B cell lymphomas
    • Shair, K. H. et al. EBV latent membrane protein 1 activates Akt, NFκB, and Stat3 in B cell lymphomas. PLoS Pathog. 3, e166 (2007).
    • (2007) PLoS Pathog , vol.3
    • Shair, K.H.1
  • 65
    • 40049106893 scopus 로고    scopus 로고
    • Latent membrane protein 1 of EBV activates phosphatidylinositol 3-kinase to induce production of IL-10
    • Lambert, S. L. & Martinez, O. M. Latent membrane protein 1 of EBV activates phosphatidylinositol 3-kinase to induce production of IL-10. J. Immunol. 179, 8225-8234 (2007).
    • (2007) J. Immunol , vol.179 , pp. 8225-8234
    • Lambert, S.L.1    Martinez, O.M.2
  • 66
    • 0035496101 scopus 로고    scopus 로고
    • Epstein-Barr virus: Exploiting the immune system
    • Thorley-Lawson, D. A. Epstein-Barr virus: exploiting the immune system. Nature Rev. Immunol. 1, 75-82 (2001).
    • (2001) Nature Rev. Immunol , vol.1 , pp. 75-82
    • Thorley-Lawson, D.A.1
  • 67
    • 0035887040 scopus 로고    scopus 로고
    • TRAF6 is a critical mediator of signal transduction by the viral oncogene latent membrane protein 1
    • Schultheiss, U. et al. TRAF6 is a critical mediator of signal transduction by the viral oncogene latent membrane protein 1. EMBO J. 20, 5678-5691 (2001).
    • (2001) EMBO J , vol.20 , pp. 5678-5691
    • Schultheiss, U.1
  • 68
    • 9144240523 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 1 activation of NF-κB through IRAK1 and TRAF6
    • Luftig, M. et al. Epstein-Barr virus latent membrane protein 1 activation of NF-κB through IRAK1 and TRAF6. Proc. Natl Acad. Sci. USA 100, 15595-15600 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 15595-15600
    • Luftig, M.1
  • 69
    • 0347065357 scopus 로고    scopus 로고
    • Latent membrane protein 1 of Epstein-Barr virus stimulates processing of NF-κB2 p100 to p52
    • Atkinson, P. G., Coope, H. J., Rowe, M. & Ley, S. C. Latent membrane protein 1 of Epstein-Barr virus stimulates processing of NF-κB2 p100 to p52. J. Biol. Chem. 278, 51134-51142 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 51134-51142
    • Atkinson, P.G.1    Coope, H.J.2    Rowe, M.3    Ley, S.C.4
  • 70
    • 33644555508 scopus 로고    scopus 로고
    • Song, Y. J., Jen, K. Y., Soni, V., Kieff, E. & Cahir-McFarland, E. IL-1 receptor-associated kinase 1 is critical for latent membrane protein 1-induced p65/RelA serine 536 phosphorylation and NF-κB activation. Proc. Natl Acad. Sci. USA 103, 2689-2694 (2006).
    • Song, Y. J., Jen, K. Y., Soni, V., Kieff, E. & Cahir-McFarland, E. IL-1 receptor-associated kinase 1 is critical for latent membrane protein 1-induced p65/RelA serine 536 phosphorylation and NF-κB activation. Proc. Natl Acad. Sci. USA 103, 2689-2694 (2006).
  • 71
    • 0347719385 scopus 로고    scopus 로고
    • Epstein-Barr virus latent infection membrane protein 1 TRAF-binding site induces NIK/IKK α-dependent noncanonical NF-κB activation
    • Luftig, M. et al. Epstein-Barr virus latent infection membrane protein 1 TRAF-binding site induces NIK/IKK α-dependent noncanonical NF-κB activation. Proc. Natl Acad. Sci. USA 101, 141-146 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 141-146
    • Luftig, M.1
  • 72
    • 0037229329 scopus 로고    scopus 로고
    • TRAF1 is a critical regulator of JNK signaling by the TRAF-binding domain of the Epstein-Barr virus-encoded latent infection membrane protein 1 but not CD40
    • Eliopoulos, A. G. et al. TRAF1 is a critical regulator of JNK signaling by the TRAF-binding domain of the Epstein-Barr virus-encoded latent infection membrane protein 1 but not CD40. J. Virol. 77, 1316-1328 (2003).
    • (2003) J. Virol , vol.77 , pp. 1316-1328
    • Eliopoulos, A.G.1
  • 73
    • 33645994488 scopus 로고    scopus 로고
    • Cooperation between TNF receptor-associated factors 1 and 2 in CD40 signaling
    • Xie, P., Hostager, B. S., Munroe, M. E., Moore, C. R. & Bishop, G. A. Cooperation between TNF receptor-associated factors 1 and 2 in CD40 signaling. J. Immunol. 176, 5388-5400 (2006).
    • (2006) J. Immunol , vol.176 , pp. 5388-5400
    • Xie, P.1    Hostager, B.S.2    Munroe, M.E.3    Moore, C.R.4    Bishop, G.A.5
  • 74
    • 10744228735 scopus 로고    scopus 로고
    • Elucidation of the c-Jun N-terminal kinase pathway mediated by Estein-Barr virus-encoded latent membrane protein 1
    • Wan, J. et al. Elucidation of the c-Jun N-terminal kinase pathway mediated by Estein-Barr virus-encoded latent membrane protein 1. Mol. Cell. Biol. 24, 192-199 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 192-199
    • Wan, J.1
  • 75
    • 33646359441 scopus 로고    scopus 로고
    • TAK1 is a component of the Epstein-Barr virus LMP1 complex and is essential for activation of JNK but not of NF-κB
    • Uemura, N. et al. TAK1 is a component of the Epstein-Barr virus LMP1 complex and is essential for activation of JNK but not of NF-κB. J. Biol. Chem. 281, 7863-7872 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 7863-7872
    • Uemura, N.1
  • 76
    • 0037423201 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 1 (LMP1) activates the phosphatidylinositol 3-kinase/Akt pathway to promote cell survival and induce actin filament remodeling
    • Dawson, C. W., Tramountanis, G., Eliopoulos, A. G. & Young, L. S. Epstein-Barr virus latent membrane protein 1 (LMP1) activates the phosphatidylinositol 3-kinase/Akt pathway to promote cell survival and induce actin filament remodeling. J. Biol. Chem. 278, 3694-3704 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 3694-3704
    • Dawson, C.W.1    Tramountanis, G.2    Eliopoulos, A.G.3    Young, L.S.4
  • 77
    • 0034969241 scopus 로고    scopus 로고
    • Immunoreceptor tyrosine-based activation motif-dependent signaling by Kaposi's sarcoma-associated herpesvirus K1 protein: Effects on lytic viral replication
    • Lagunoff, M., Lukac, D. M. & Ganem, D. Immunoreceptor tyrosine-based activation motif-dependent signaling by Kaposi's sarcoma-associated herpesvirus K1 protein: effects on lytic viral replication. J. Virol. 75, 5891-5898 (2001).
    • (2001) J. Virol , vol.75 , pp. 5891-5898
    • Lagunoff, M.1    Lukac, D.M.2    Ganem, D.3
  • 78
    • 0033545865 scopus 로고    scopus 로고
    • Deregulated signal transduction by the K1 gene product of Kaposi's sarcoma-associated herpesvirus
    • Lagunoff, M., Majeti, R., Weiss, A. & Ganem, D. Deregulated signal transduction by the K1 gene product of Kaposi's sarcoma-associated herpesvirus. Proc. Natl Acad. Sci. USA 96, 5704-5709 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 5704-5709
    • Lagunoff, M.1    Majeti, R.2    Weiss, A.3    Ganem, D.4
  • 79
    • 25144462103 scopus 로고    scopus 로고
    • Characterization of the Kaposi's sarcoma-associated herpesvirus K1 signalosome
    • Lee, B. S. et al. Characterization of the Kaposi's sarcoma-associated herpesvirus K1 signalosome. J. Virol. 79, 12173-12184 (2005).
    • (2005) J. Virol , vol.79 , pp. 12173-12184
    • Lee, B.S.1
  • 80
    • 0842304506 scopus 로고    scopus 로고
    • The K1 protein of Kaposi's sarcoma-associated herpesvirus activates the Akt signaling pathway
    • Tomlinson, C. C. & Damania, B. The K1 protein of Kaposi's sarcoma-associated herpesvirus activates the Akt signaling pathway. J. Virol. 78, 1918-1927 (2004).
    • (2004) J. Virol , vol.78 , pp. 1918-1927
    • Tomlinson, C.C.1    Damania, B.2
  • 81
    • 20844453394 scopus 로고    scopus 로고
    • Activation of Src kinase Lyn by the Kaposi sarcoma-associated herpesvirus K1 protein: Implications for lymphomagenesis
    • Prakash, O. et al. Activation of Src kinase Lyn by the Kaposi sarcoma-associated herpesvirus K1 protein: implications for lymphomagenesis. Blood 105, 3987-3994 (2005).
    • (2005) Blood , vol.105 , pp. 3987-3994
    • Prakash, O.1
  • 82
    • 0031813291 scopus 로고    scopus 로고
    • Identification of an immunoreceptor tyrosine-based activation motif of K1 transforming protein of Kaposi's sarcoma-associated herpesvirus
    • Lee, H. et al. Identification of an immunoreceptor tyrosine-based activation motif of K1 transforming protein of Kaposi's sarcoma-associated herpesvirus. Mol. Cell. Biol. 18, 5219-5228 (1998).
    • (1998) Mol. Cell. Biol , vol.18 , pp. 5219-5228
    • Lee, H.1
  • 83
    • 3543092018 scopus 로고    scopus 로고
    • Expression in a recombinant murid herpesvirus 4 reveals the in vivo transforming potential of the K1 open reading frame of Kaposi's sarcoma-associated herpesvirus
    • Douglas, J., Dutia, B., Rhind, S., Stewart, J. P. & Talbot, S. J. Expression in a recombinant murid herpesvirus 4 reveals the in vivo transforming potential of the K1 open reading frame of Kaposi's sarcoma-associated herpesvirus. J. Virol. 78, 8878-8884 (2004).
    • (2004) J. Virol , vol.78 , pp. 8878-8884
    • Douglas, J.1    Dutia, B.2    Rhind, S.3    Stewart, J.P.4    Talbot, S.J.5
  • 84
    • 0041387452 scopus 로고    scopus 로고
    • Activation of mitogenactivated protein kinase and NF-κB pathways by a Kaposi's sarcoma-associated herpesvirus K15 membrane protein
    • Brinkmann, M. M. et al. Activation of mitogenactivated protein kinase and NF-κB pathways by a Kaposi's sarcoma-associated herpesvirus K15 membrane protein. J. Virol. 77, 9346-9358 (2003).
    • (2003) J. Virol , vol.77 , pp. 9346-9358
    • Brinkmann, M.M.1
  • 85
    • 33845736881 scopus 로고    scopus 로고
    • Modulation of host gene expression by the K15 protein of Kaposi's sarcoma-associated herpesvirus
    • Brinkmann, M. M., Pietrek, M., Dittrich-Breiholz, O., Kracht, M. & Schulz, T. F. Modulation of host gene expression by the K15 protein of Kaposi's sarcoma-associated herpesvirus. J. Virol. 81, 42-58 (2007).
    • (2007) J. Virol , vol.81 , pp. 42-58
    • Brinkmann, M.M.1    Pietrek, M.2    Dittrich-Breiholz, O.3    Kracht, M.4    Schulz, T.F.5
  • 86
    • 34247611854 scopus 로고    scopus 로고
    • Immune evasion by Kaposi's sarcoma-associated herpesvirus
    • Coscoy, L. Immune evasion by Kaposi's sarcoma-associated herpesvirus. Nature Rev. Immunol. 7, 391-401 (2007).
    • (2007) Nature Rev. Immunol , vol.7 , pp. 391-401
    • Coscoy, L.1
  • 87
    • 0033564340 scopus 로고    scopus 로고
    • Cutting Edge: A novel viral TNF receptor superfamily member in virulent strains of human cytomegalovirus
    • Benedict, C. A. et al. Cutting Edge: a novel viral TNF receptor superfamily member in virulent strains of human cytomegalovirus. J. Immunol. 162, 6967-6970 (1999).
    • (1999) J. Immunol , vol.162 , pp. 6967-6970
    • Benedict, C.A.1
  • 88
    • 0032752996 scopus 로고    scopus 로고
    • Human cytomegalovirus UL144 open reading frame: Sequence hypervariability in low-passage clinical isolates
    • Lurain, N. S. et al. Human cytomegalovirus UL144 open reading frame: sequence hypervariability in low-passage clinical isolates. J. Virol. 73, 10040-10050 (1999).
    • (1999) J. Virol , vol.73 , pp. 10040-10050
    • Lurain, N.S.1
  • 89
    • 0029655755 scopus 로고    scopus 로고
    • Human cytomegalovirus clinical isolates carry at least 19 genes not found in laboratory strains
    • Cha, T. A. et al. Human cytomegalovirus clinical isolates carry at least 19 genes not found in laboratory strains. J. Virol. 70, 78-83 (1996).
    • (1996) J. Virol , vol.70 , pp. 78-83
    • Cha, T.A.1
  • 90
    • 33748947656 scopus 로고    scopus 로고
    • The UL144 gene product of human cytomegalovirus activates NFκB via a TRAF6-dependent mechanism
    • Poole, E., King, C. A., Sinclair, J. H. & Alcami, A. The UL144 gene product of human cytomegalovirus activates NFκB via a TRAF6-dependent mechanism. EMBO J. 25, 4390-4399 (2006).
    • (2006) EMBO J , vol.25 , pp. 4390-4399
    • Poole, E.1    King, C.A.2    Sinclair, J.H.3    Alcami, A.4
  • 92
    • 33646856912 scopus 로고    scopus 로고
    • B and T lymphocyte attenuator-mediated signal transduction provides a potent inhibitory signal to primary human CD4 T cells that can be initiated by multiple phosphotyrosine motifs
    • Chemnitz, J. M., Lanfranco, A. R., Braunstein, I. & Riley, J. L. B and T lymphocyte attenuator-mediated signal transduction provides a potent inhibitory signal to primary human CD4 T cells that can be initiated by multiple phosphotyrosine motifs. J. Immunol. 176, 6603-6614 (2006).
    • (2006) J. Immunol , vol.176 , pp. 6603-6614
    • Chemnitz, J.M.1    Lanfranco, A.R.2    Braunstein, I.3    Riley, J.L.4
  • 93
    • 40449086741 scopus 로고    scopus 로고
    • Nelson, C. A. et al. Structural determinants of herpesvirus entry mediator recognition by murine B and T lymphocyte attenuator. J. Immunol. 180, 940-947 (2008). This paper, together with references 17, 33 and 36, presents the known structural information about HVEM and its viral and cellular ligands gD and BTLA, showing that HVEM binds to both ligands in a similar manner and that gD undergoes a conformational change following HVEM binding.
    • Nelson, C. A. et al. Structural determinants of herpesvirus entry mediator recognition by murine B and T lymphocyte attenuator. J. Immunol. 180, 940-947 (2008). This paper, together with references 17, 33 and 36, presents the known structural information about HVEM and its viral and cellular ligands gD and BTLA, showing that HVEM binds to both ligands in a similar manner and that gD undergoes a conformational change following HVEM binding.
  • 94
    • 0842304537 scopus 로고    scopus 로고
    • Selective induction of Th2-attracting chemokines CCL17 and CCL22 in human B cells by latent membrane protein 1 of Epstein-Barr virus
    • Nakayama, T. et al. Selective induction of Th2-attracting chemokines CCL17 and CCL22 in human B cells by latent membrane protein 1 of Epstein-Barr virus. J. Virol. 78, 1665-1674 (2004).
    • (2004) J. Virol , vol.78 , pp. 1665-1674
    • Nakayama, T.1
  • 95
    • 38849171171 scopus 로고    scopus 로고
    • The inhibitory HVEM-BTLA pathway counter regulates lymphotoxin receptor signaling to achieve homeostasis of dendritic cells
    • De Trez, C. et al. The inhibitory HVEM-BTLA pathway counter regulates lymphotoxin receptor signaling to achieve homeostasis of dendritic cells. J. Immunol. 180, 238-248 (2008).
    • (2008) J. Immunol , vol.180 , pp. 238-248
    • De Trez, C.1
  • 96
    • 33846636409 scopus 로고    scopus 로고
    • Differential antigen processing by dendritic cell subsets in vivo
    • Dudziak, D. et al. Differential antigen processing by dendritic cell subsets in vivo. Science 315, 107-111 (2007).
    • (2007) Science , vol.315 , pp. 107-111
    • Dudziak, D.1
  • 98
    • 0037089402 scopus 로고    scopus 로고
    • Human cytomegalovirus inhibits maturation and impairs function of monocyte-derived dendritic cells
    • Moutaftsi, M., Mehl, A. M., Borysiewicz, L. K. & Tabi, Z. Human cytomegalovirus inhibits maturation and impairs function of monocyte-derived dendritic cells. Blood 99, 2913-2921 (2002).
    • (2002) Blood , vol.99 , pp. 2913-2921
    • Moutaftsi, M.1    Mehl, A.M.2    Borysiewicz, L.K.3    Tabi, Z.4
  • 99
    • 0033565590 scopus 로고    scopus 로고
    • IFN-γ mediates a novel antiviral activity through dynamic modulation of TRAIL and TRAIL receptor expression
    • Sedger, L. M. et al. IFN-γ mediates a novel antiviral activity through dynamic modulation of TRAIL and TRAIL receptor expression. J. Immunol. 163, 920-926 (1999).
    • (1999) J. Immunol , vol.163 , pp. 920-926
    • Sedger, L.M.1
  • 100
    • 27744572593 scopus 로고    scopus 로고
    • + T cells requires γ interferon and either perforin- or Fas-mediated cytolytic mechanisms
    • + T cells requires γ interferon and either perforin- or Fas-mediated cytolytic mechanisms. J. Virol. 79, 14546-14554 (2005).
    • (2005) J. Virol , vol.79 , pp. 14546-14554
    • Dobbs, M.E.1    Strasser, J.E.2    Chu, C.F.3    Chalk, C.4    Milligan, G.N.5
  • 101
    • 0346365288 scopus 로고    scopus 로고
    • Epstein-Barr virus immediate-early protein BZLF1 inhibits tumor necrosis factor α-induced signaling and apoptosis by downregulating tumor necrosis factor receptor 1
    • Morrison, T. E., Mauser, A., Klingelhutz, A. & Kenney, S. C. Epstein-Barr virus immediate-early protein BZLF1 inhibits tumor necrosis factor α-induced signaling and apoptosis by downregulating tumor necrosis factor receptor 1. J. Virol. 78, 544-549 (2004).
    • (2004) J. Virol , vol.78 , pp. 544-549
    • Morrison, T.E.1    Mauser, A.2    Klingelhutz, A.3    Kenney, S.C.4
  • 102
    • 0038279763 scopus 로고    scopus 로고
    • Human cytomegalovirus infection inhibits tumor necrosis factor α (TNF-α) signaling by targeting the 55-kilodalton TNF-α receptor
    • Baillie, J., Sahlender, D. A. & Sinclair, J. H. Human cytomegalovirus infection inhibits tumor necrosis factor α (TNF-α) signaling by targeting the 55-kilodalton TNF-α receptor. J. Virol. 77, 7007-7016 (2003).
    • (2003) J. Virol , vol.77 , pp. 7007-7016
    • Baillie, J.1    Sahlender, D.A.2    Sinclair, J.H.3
  • 103
    • 0035194167 scopus 로고    scopus 로고
    • Altered cellular mRNA levels in human cytomegalovirus-infected fibroblasts: Viral block to the accumulation of antiviral mRNAs
    • Browne, E. P., Wing, B., Coleman, D. & Shenk, T. Altered cellular mRNA levels in human cytomegalovirus-infected fibroblasts: viral block to the accumulation of antiviral mRNAs. J. Virol. 75, 12319-12330 (2001).
    • (2001) J. Virol , vol.75 , pp. 12319-12330
    • Browne, E.P.1    Wing, B.2    Coleman, D.3    Shenk, T.4
  • 104
    • 33344461472 scopus 로고    scopus 로고
    • EBV latency III immortalization program sensitizes B cells to induction of CD95-mediated apoptosis via LMP1: Role of NF-κB, STAT1, and p53
    • Le Clorennec, C. et al. EBV latency III immortalization program sensitizes B cells to induction of CD95-mediated apoptosis via LMP1: role of NF-κB, STAT1, and p53. Blood 107, 2070-2078 (2006).
    • (2006) Blood , vol.107 , pp. 2070-2078
    • Le Clorennec, C.1
  • 105
    • 0035696024 scopus 로고    scopus 로고
    • Targeting the function of mature dendritic cells by human cytomegalovirus: A multilayered viral defense strategy
    • Raftery, M. J. et al. Targeting the function of mature dendritic cells by human cytomegalovirus: a multilayered viral defense strategy. Immunity 15, 997-1009 (2001).
    • (2001) Immunity , vol.15 , pp. 997-1009
    • Raftery, M.J.1
  • 106
    • 0035478299 scopus 로고    scopus 로고
    • Up-regulation of Fas ligand expression by human cytomegalovirus immediate-early gene product 2: A novel mechanism in cytomegalovirus-induced apoptosis in human retina
    • Chiou, S. H. et al. Up-regulation of Fas ligand expression by human cytomegalovirus immediate-early gene product 2: a novel mechanism in cytomegalovirus-induced apoptosis in human retina. J. Immunol. 167, 4098-4103 (2001).
    • (2001) J. Immunol , vol.167 , pp. 4098-4103
    • Chiou, S.H.1
  • 107
    • 0030970013 scopus 로고    scopus 로고
    • Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors
    • Thome, M. et al. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature 386, 517-521 (1997).
    • (1997) Nature , vol.386 , pp. 517-521
    • Thome, M.1
  • 108
    • 0035496099 scopus 로고    scopus 로고
    • Regulation of lymphocyte proliferation and death by FLIP
    • Thome, M. & Tschopp, J. Regulation of lymphocyte proliferation and death by FLIP. Nature Rev. Immunol. 1, 50-58 (2001).
    • (2001) Nature Rev. Immunol , vol.1 , pp. 50-58
    • Thome, M.1    Tschopp, J.2
  • 109
    • 33750716875 scopus 로고    scopus 로고
    • The FLIP-side of Fas signaling
    • Hyer, M. L., Samuel, T. & Reed, J. C. The FLIP-side of Fas signaling. Clin. Cancer Res. 12, 5929-5931 (2006).
    • (2006) Clin. Cancer Res , vol.12 , pp. 5929-5931
    • Hyer, M.L.1    Samuel, T.2    Reed, J.C.3
  • 111
    • 33747803613 scopus 로고    scopus 로고
    • EBV can protect latently infected B cell lymphomas from death receptor-induced apoptosis
    • Snow, A. L. et al. EBV can protect latently infected B cell lymphomas from death receptor-induced apoptosis. J. Immunol. 177, 3283-3293 (2006).
    • (2006) J. Immunol , vol.177 , pp. 3283-3293
    • Snow, A.L.1
  • 112
    • 33750322789 scopus 로고    scopus 로고
    • The immediate early 2 protein of human cytomegalovirus (HCMV) mediates the apoptotic control in HCMV retinitis through up-regulation of the cellular FLICE-inhibitory protein expression
    • Chiou, S. H. et al. The immediate early 2 protein of human cytomegalovirus (HCMV) mediates the apoptotic control in HCMV retinitis through up-regulation of the cellular FLICE-inhibitory protein expression. J. Immunol. 177, 6199-6206 (2006).
    • (2006) J. Immunol , vol.177 , pp. 6199-6206
    • Chiou, S.H.1
  • 113
    • 0034933686 scopus 로고    scopus 로고
    • A cytomegalovirus-encoded inhibitor of apoptosis that suppresses caspase-8 activation
    • Skaletskaya, A. et al. A cytomegalovirus-encoded inhibitor of apoptosis that suppresses caspase-8 activation. Proc. Natl Acad. Sci. USA 98, 7829-7834 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 7829-7834
    • Skaletskaya, A.1
  • 114
    • 0344982847 scopus 로고    scopus 로고
    • Differential function and expression of the viral inhibitor of caspase 8-induced apoptosis (vICA) and the viral mitochondria-localized inhibitor of apoptosis (vMIA) cell death suppressors conserved in primate and rodent cytomegaloviruses
    • McCormick, A. L., Skaletskaya, A., Barry, P. A., Mocarski, E. S. & Goldmacher, V. S. Differential function and expression of the viral inhibitor of caspase 8-induced apoptosis (vICA) and the viral mitochondria-localized inhibitor of apoptosis (vMIA) cell death suppressors conserved in primate and rodent cytomegaloviruses. Virology 316, 221-233 (2003).
    • (2003) Virology , vol.316 , pp. 221-233
    • McCormick, A.L.1    Skaletskaya, A.2    Barry, P.A.3    Mocarski, E.S.4    Goldmacher, V.S.5
  • 115
    • 42949111649 scopus 로고    scopus 로고
    • Inhibition of proinflammatory and innate immune signaling pathways by a cytomegalovirus RIP1-interacting protein
    • Mack, C., Sickmann, A., Lembo, D. & Brune, W. Inhibition of proinflammatory and innate immune signaling pathways by a cytomegalovirus RIP1-interacting protein. Proc. Natl Acad. Sci. USA 105, 3094-3099 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 3094-3099
    • Mack, C.1    Sickmann, A.2    Lembo, D.3    Brune, W.4
  • 116
    • 0037369240 scopus 로고    scopus 로고
    • The human herpes virus 8-encoded viral FLICE inhibitory protein protects against growth factor withdrawal-induced apoptosis via NF-κB activation
    • Sun, Q., Matta, H. & Chaudhary, P. M. The human herpes virus 8-encoded viral FLICE inhibitory protein protects against growth factor withdrawal-induced apoptosis via NF-κB activation. Blood 101, 1956-1961 (2003).
    • (2003) Blood , vol.101 , pp. 1956-1961
    • Sun, Q.1    Matta, H.2    Chaudhary, P.M.3
  • 117
    • 33645744753 scopus 로고    scopus 로고
    • The KSHV oncoprotein vFLIP contains a TRAF-interacting motif and requires TRAF2 and TRAF3 for signalling
    • 114-119
    • Guasparri, I., Wu, H. & Cesarman, E. The KSHV oncoprotein vFLIP contains a TRAF-interacting motif and requires TRAF2 and TRAF3 for signalling. EMBO Rep. 7, 114-119 (2006).
    • (2006) EMBO Rep , vol.7
    • Guasparri, I.1    Wu, H.2    Cesarman, E.3
  • 118
    • 0141502126 scopus 로고    scopus 로고
    • KSHV vFLIP binds to IKK-γ to activate IKK
    • Field, N. et al. KSHV vFLIP binds to IKK-γ to activate IKK. J. Cell Sci. 116, 3721-3728 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 3721-3728
    • Field, N.1
  • 119
    • 3042689762 scopus 로고    scopus 로고
    • Activation of alternative NF-κB pathway by human herpes virus 8-encoded Fas-associated death domain-like IL-1 β-converting enzyme inhibitory protein (vFLIP)
    • Matta, H. & Chaudhary, P. M. Activation of alternative NF-κB pathway by human herpes virus 8-encoded Fas-associated death domain-like IL-1 β-converting enzyme inhibitory protein (vFLIP). Proc. Natl Acad. Sci. USA 101, 9399-9404 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 9399-9404
    • Matta, H.1    Chaudhary, P.M.2
  • 120
    • 1842631466 scopus 로고    scopus 로고
    • KSHV vFLIP is essential for the survival of infected lymphoma cells
    • Guasparri, I., Keller, S. A. & Cesarman, E. KSHV vFLIP is essential for the survival of infected lymphoma cells. J. Exp. Med. 199, 993-1003 (2004).
    • (2004) J. Exp. Med , vol.199 , pp. 993-1003
    • Guasparri, I.1    Keller, S.A.2    Cesarman, E.3
  • 121
    • 33947114420 scopus 로고    scopus 로고
    • Induction of spindle cell morphology in human vascular endothelial cells by human herpesvirus 8-encoded viral FLICE inhibitory protein K13
    • Matta, H. et al. Induction of spindle cell morphology in human vascular endothelial cells by human herpesvirus 8-encoded viral FLICE inhibitory protein K13. Oncogene 26, 1656-1660 (2007).
    • (2007) Oncogene , vol.26 , pp. 1656-1660
    • Matta, H.1
  • 122
    • 24644491664 scopus 로고    scopus 로고
    • Constitutive NF-κB activation, normal Fas-induced apoptosis, and increased incidence of lymphoma in human herpes virus 8 K13 transgenic mice
    • Chugh, P. et al. Constitutive NF-κB activation, normal Fas-induced apoptosis, and increased incidence of lymphoma in human herpes virus 8 K13 transgenic mice. Proc. Natl Acad. Sci. USA 102, 12885-12890 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 12885-12890
    • Chugh, P.1
  • 123
    • 33847369549 scopus 로고    scopus 로고
    • K1 protein of human herpesvirus 8 suppresses lymphoma cell Fas-mediated apoptosis
    • Wang, S. et al. K1 protein of human herpesvirus 8 suppresses lymphoma cell Fas-mediated apoptosis. Blood 109, 2174-2182 (2007).
    • (2007) Blood , vol.109 , pp. 2174-2182
    • Wang, S.1
  • 124
    • 25144457575 scopus 로고    scopus 로고
    • Epstein-Barr virus-encoded poly(A)- RNA confers resistance to apoptosis mediated through Fas by blocking the PKR pathway in human epithelial intestine 407 cells
    • Nanbo, A., Yoshiyama, H. & Takada, K. Epstein-Barr virus-encoded poly(A)- RNA confers resistance to apoptosis mediated through Fas by blocking the PKR pathway in human epithelial intestine 407 cells. J. Virol. 79, 12280-12285 (2005).
    • (2005) J. Virol , vol.79 , pp. 12280-12285
    • Nanbo, A.1    Yoshiyama, H.2    Takada, K.3
  • 125
    • 34249871137 scopus 로고    scopus 로고
    • Complex I binding by a virally encoded RNA regulates mitochondria-induced cell death
    • Reeves, M. B., Davies, A. A., McSharry, B. P., Wilkinson, G. W. & Sinclair, J. H. Complex I binding by a virally encoded RNA regulates mitochondria-induced cell death. Science 316, 1345-1348 (2007).
    • (2007) Science , vol.316 , pp. 1345-1348
    • Reeves, M.B.1    Davies, A.A.2    McSharry, B.P.3    Wilkinson, G.W.4    Sinclair, J.H.5
  • 126
    • 0033427047 scopus 로고    scopus 로고
    • OX40-deficient mice are defective in Th cell proliferation but are competent in generating B cell and CTL responses after virus infection
    • Kopf, M. et al. OX40-deficient mice are defective in Th cell proliferation but are competent in generating B cell and CTL responses after virus infection. Immunity 11, 699-708 (1999).
    • (1999) Immunity , vol.11 , pp. 699-708
    • Kopf, M.1
  • 127
    • 0141609073 scopus 로고    scopus 로고
    • Co-stimulatory members of the TNFR family: Keys to effective T-cell immunity?
    • Croft, M. Co-stimulatory members of the TNFR family: keys to effective T-cell immunity? Nature Rev. Immunol. 3, 609-620 (2003).
    • (2003) Nature Rev. Immunol , vol.3 , pp. 609-620
    • Croft, M.1
  • 128
    • 17644389199 scopus 로고    scopus 로고
    • Watts, T. H. TNF/TNFR family members in costimulation of T cell responses. Annu. Rev. Immunol. 23, 23-68 (2005).
    • Watts, T. H. TNF/TNFR family members in costimulation of T cell responses. Annu. Rev. Immunol. 23, 23-68 (2005).
  • 129
    • 27744446078 scopus 로고    scopus 로고
    • Evaluation of OX40 ligand as a costimulator of human antiviral memory CD8 T cell responses: Comparison with B7.1 and 4-1BBL
    • Serghides, L. et al. Evaluation of OX40 ligand as a costimulator of human antiviral memory CD8 T cell responses: comparison with B7.1 and 4-1BBL. J. Immunol. 175, 6368-6377 (2005).
    • (2005) J. Immunol , vol.175 , pp. 6368-6377
    • Serghides, L.1
  • 130
    • 33749128681 scopus 로고    scopus 로고
    • Functional dichotomy between OX40 and 4-1BB in modulating effector CD8 T cell responses
    • Lee, S. W. et al. Functional dichotomy between OX40 and 4-1BB in modulating effector CD8 T cell responses. J. Immunol. 177, 4464-4472 (2006).
    • (2006) J. Immunol , vol.177 , pp. 4464-4472
    • Lee, S.W.1
  • 131
    • 33847779175 scopus 로고    scopus 로고
    • Expression and function of the OX40/ OX40L costimulatory pair during herpes stromal keratitis
    • Lepisto, A. J., Xu, M., Yagita, H., Weinberg, A. D. & Hendricks, R. L. Expression and function of the OX40/ OX40L costimulatory pair during herpes stromal keratitis. J. Leukoc. Biol. 81, 766-774 (2007).
    • (2007) J. Leukoc. Biol , vol.81 , pp. 766-774
    • Lepisto, A.J.1    Xu, M.2    Yagita, H.3    Weinberg, A.D.4    Hendricks, R.L.5
  • 132
    • 32144453848 scopus 로고    scopus 로고
    • + T regulatory cell inhibition
    • + T regulatory cell inhibition. J. Immunol. 176, 2486-2495 (2006).
    • (2006) J. Immunol , vol.176 , pp. 2486-2495
    • Yu, Q.1
  • 133
    • 34848849793 scopus 로고    scopus 로고
    • OX40 costimulation promotes persistence of cytomegalovirus-specific CD8 T cells: A CD4-dependent mechanism
    • Humphreys, I. R. et al. OX40 costimulation promotes persistence of cytomegalovirus-specific CD8 T cells: a CD4-dependent mechanism. J. Immunol. 179, 2195-2202 (2007).
    • (2007) J. Immunol , vol.179 , pp. 2195-2202
    • Humphreys, I.R.1
  • 134
    • 34249103845 scopus 로고    scopus 로고
    • Humphreys, I. R. et al. Cytomegalovirus exploits IL-10-mediated immune regulation in the salivary glands. J. Exp. Med. 204, 1217-1225 (2007). References 133 and 134 show that OX40 controls MCMV infection by co-stimulating antigen-specific T-cell responses, and that stimulating OX40 increases IFNγ production and decreases IL-10 production in the salivary glands.
    • Humphreys, I. R. et al. Cytomegalovirus exploits IL-10-mediated immune regulation in the salivary glands. J. Exp. Med. 204, 1217-1225 (2007). References 133 and 134 show that OX40 controls MCMV infection by co-stimulating antigen-specific T-cell responses, and that stimulating OX40 increases IFNγ production and decreases IL-10 production in the salivary glands.
  • 136
    • 34247872819 scopus 로고    scopus 로고
    • Cellular responses to viral infection in humans: Lessons from Epstein-Barr virus
    • Hislop, A. D., Taylor, G. S., Sauce, D. & Rickinson, A. B. Cellular responses to viral infection in humans: lessons from Epstein-Barr virus. Annu. Rev. Immunol. 25, 587-617 (2007).
    • (2007) Annu. Rev. Immunol , vol.25 , pp. 587-617
    • Hislop, A.D.1    Taylor, G.S.2    Sauce, D.3    Rickinson, A.B.4
  • 137
    • 3142683548 scopus 로고    scopus 로고
    • TLR9-dependent recognition of MCMV by IPC and DC generates coordinated cytokine responses that activate antiviral NK cell function
    • Krug, A. et al. TLR9-dependent recognition of MCMV by IPC and DC generates coordinated cytokine responses that activate antiviral NK cell function. Immunity 21, 107-119 (2004).
    • (2004) Immunity , vol.21 , pp. 107-119
    • Krug, A.1
  • 138
    • 30444450839 scopus 로고    scopus 로고
    • Recognition of cytosolic DNA activates an IRF3-dependent innate immune response
    • Stetson, D. B. & Medzhitov, R. Recognition of cytosolic DNA activates an IRF3-dependent innate immune response. Immunity 24, 93-103 (2006).
    • (2006) Immunity , vol.24 , pp. 93-103
    • Stetson, D.B.1    Medzhitov, R.2
  • 139
    • 34748827433 scopus 로고    scopus 로고
    • Genetic analysis of resistance to viral infection
    • Beutler, B. et al. Genetic analysis of resistance to viral infection. Nature Rev. Immunol. 7, 753-766 (2007).
    • (2007) Nature Rev. Immunol , vol.7 , pp. 753-766
    • Beutler, B.1
  • 140
    • 34547143110 scopus 로고    scopus 로고
    • DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response
    • Takaoka, A. et al. DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response. Nature 448, 501-505 (2007).
    • (2007) Nature , vol.448 , pp. 501-505
    • Takaoka, A.1
  • 141
    • 34548699323 scopus 로고    scopus 로고
    • TLR3 deficiency in patients with herpes simplex encephalitis
    • Zhang, S. Y. et al. TLR3 deficiency in patients with herpes simplex encephalitis. Science 317, 1522-1527 (2007).
    • (2007) Science , vol.317 , pp. 1522-1527
    • Zhang, S.Y.1
  • 142
    • 0034749494 scopus 로고    scopus 로고
    • Lymphotoxins and cytomegalovirus cooperatively induce interferon-β, establishing host-virus detente
    • Benedict, C. A. et al. Lymphotoxins and cytomegalovirus cooperatively induce interferon-β, establishing host-virus detente. Immunity 15, 617-626 (2001).
    • (2001) Immunity , vol.15 , pp. 617-626
    • Benedict, C.A.1
  • 143
    • 21044440573 scopus 로고    scopus 로고
    • A lymphotoxin-IFN-β axis essential for lymphocyte survival revealed during cytomegalovirus infection
    • Banks, T. A. et al. A lymphotoxin-IFN-β axis essential for lymphocyte survival revealed during cytomegalovirus infection. J. Immunol. 174, 7217-7225 (2005).
    • (2005) J. Immunol , vol.174 , pp. 7217-7225
    • Banks, T.A.1
  • 144
    • 38849112479 scopus 로고    scopus 로고
    • Lymphotoxin-mediated crosstalk between B cells and splenic stroma promotes the initial type I interferon response to cytomegalovirus
    • References 142 and 144 describe a mechanism by which LTβR cooperates with CMV in infected cells to induce the production of IFN, and show that B cells are the source of the initial lymphotoxin
    • Schneider, K. et al. Lymphotoxin-mediated crosstalk between B cells and splenic stroma promotes the initial type I interferon response to cytomegalovirus. Cell Host Microbe 3, 67-76 (2008). References 142 and 144 describe a mechanism by which LTβR cooperates with CMV in infected cells to induce the production of IFN, and show that B cells are the source of the initial lymphotoxin.
    • (2008) Cell Host Microbe , vol.3 , pp. 67-76
    • Schneider, K.1
  • 145
    • 28244439891 scopus 로고    scopus 로고
    • Human NK cells inhibit cytomegalovirus replication through a noncytolytic mechanism involving lymphotoxin-dependent induction of IFN-β
    • Iversen, A. C., Norris, P. S., Ware, C. F. & Benedict, C. A. Human NK cells inhibit cytomegalovirus replication through a noncytolytic mechanism involving lymphotoxin-dependent induction of IFN-β. J. Immunol. 175, 7568-7574 (2005).
    • (2005) J. Immunol , vol.175 , pp. 7568-7574
    • Iversen, A.C.1    Norris, P.S.2    Ware, C.F.3    Benedict, C.A.4
  • 146
    • 33645966202 scopus 로고    scopus 로고
    • γ interferon blocks gammaherpesvirus reactivation from latency
    • Steed, A. L. et al. γ interferon blocks gammaherpesvirus reactivation from latency. J. Virol. 80, 192-200 (2006).
    • (2006) J. Virol , vol.80 , pp. 192-200
    • Steed, A.L.1
  • 147
    • 27644558111 scopus 로고    scopus 로고
    • Barton, E. S., Lutzke, M. L., Rochford, R. & Virgin, H. W. 4th. α/β interferons regulate murine gammaherpesvirus latent gene expression and reactivation from latency. J. Virol. 79, 14149-14160 (2005).
    • Barton, E. S., Lutzke, M. L., Rochford, R. & Virgin, H. W. 4th. α/β interferons regulate murine gammaherpesvirus latent gene expression and reactivation from latency. J. Virol. 79, 14149-14160 (2005).
  • 148
    • 33645796485 scopus 로고    scopus 로고
    • Specific remodeling of splenic architecture by cytomegalovirus
    • Benedict, C. A. et al. Specific remodeling of splenic architecture by cytomegalovirus. PLoS Pathog. 2, e16 (2006).
    • (2006) PLoS Pathog , vol.2
    • Benedict, C.A.1
  • 149
    • 34547782880 scopus 로고    scopus 로고
    • Regulation of homeostatic chemokine expression and cell trafficking during immune responses
    • Mueller, S. N. et al. Regulation of homeostatic chemokine expression and cell trafficking during immune responses. Science 317, 670-674 (2007).
    • (2007) Science , vol.317 , pp. 670-674
    • Mueller, S.N.1
  • 150
    • 44049100259 scopus 로고    scopus 로고
    • Restoration of lymphoid organ integrity through the interaction of lymphoid tissue-inducer cells with stroma of the T cell zone
    • Scandella, E. et al. Restoration of lymphoid organ integrity through the interaction of lymphoid tissue-inducer cells with stroma of the T cell zone. Nature Immunol. 9, 667-675 (2008).
    • (2008) Nature Immunol , vol.9 , pp. 667-675
    • Scandella, E.1
  • 152
    • 34248346700 scopus 로고    scopus 로고
    • Genome sequences of three koi herpesvirus isolates representing the expanding distribution of an emerging disease threatening koi and common carp worldwide
    • Aoki, T. et al. Genome sequences of three koi herpesvirus isolates representing the expanding distribution of an emerging disease threatening koi and common carp worldwide. J. Virol. 81, 5058-5065 (2007).
    • (2007) J. Virol , vol.81 , pp. 5058-5065
    • Aoki, T.1
  • 153
    • 33845487130 scopus 로고    scopus 로고
    • Costimulatory receptors in jawed vertebrates: Conserved CD28, odd CTLA4 and multiple BTLAs
    • Bernard, D. et al. Costimulatory receptors in jawed vertebrates: conserved CD28, odd CTLA4 and multiple BTLAs. Dev. Comp. Immunol. 31, 255-271 (2007).
    • (2007) Dev. Comp. Immunol , vol.31 , pp. 255-271
    • Bernard, D.1
  • 154
    • 38349133685 scopus 로고    scopus 로고
    • Mapping of equine lentivirus receptor 1 residues critical for equine infectious anemia virus envelope binding
    • Zhang, B., Sun, C., Jin, S., Cascio, M. & Montelaro, R. C. Mapping of equine lentivirus receptor 1 residues critical for equine infectious anemia virus envelope binding. J. Virol. 82, 1204-1213 (2008).
    • (2008) J. Virol , vol.82 , pp. 1204-1213
    • Zhang, B.1    Sun, C.2    Jin, S.3    Cascio, M.4    Montelaro, R.C.5
  • 156
    • 0032486317 scopus 로고    scopus 로고
    • Entry of alpha herpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor
    • Geraghty, R. J., Krummenacher, C., Cohen, G. H., Eisenberg, R. J. & Spear, P. G. Entry of alpha herpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. Science 280, 1618-1620 (1998).
    • (1998) Science , vol.280 , pp. 1618-1620
    • Geraghty, R.J.1    Krummenacher, C.2    Cohen, G.H.3    Eisenberg, R.J.4    Spear, P.G.5
  • 157
    • 0033215527 scopus 로고    scopus 로고
    • A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry
    • Shukla, D. et al. A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. Cell 99, 13-22 (1999).
    • (1999) Cell , vol.99 , pp. 13-22
    • Shukla, D.1
  • 158
    • 0028931933 scopus 로고
    • Infection of cells by varicella zoster virus: Inhibition of viral entry by mannose 6-phosphate and heparin
    • Zhu, Z., Gershon, M. D., Ambron, R., Gabel, C. & Gershon, A. A. Infection of cells by varicella zoster virus: inhibition of viral entry by mannose 6-phosphate and heparin. Proc. Natl Acad. Sci. USA 92, 3546-3550 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3546-3550
    • Zhu, Z.1    Gershon, M.D.2    Ambron, R.3    Gabel, C.4    Gershon, A.A.5
  • 159
    • 11144324373 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptor dependence of varicella zoster virus infection in vitro and in the epidermis during varicella and zoster
    • Chen, J. J., Zhu, Z., Gershon, A. A. & Gershon, M. D. Mannose 6-phosphate receptor dependence of varicella zoster virus infection in vitro and in the epidermis during varicella and zoster. Cell 119, 915-926 (2004).
    • (2004) Cell , vol.119 , pp. 915-926
    • Chen, J.J.1    Zhu, Z.2    Gershon, A.A.3    Gershon, M.D.4
  • 160
    • 33750006828 scopus 로고    scopus 로고
    • Insulin degrading enzyme is a cellular receptor mediating varicella-zoster virus infection and cell-to-cell spread
    • Li, Q., Ali, M. A. & Cohen, J. I. Insulin degrading enzyme is a cellular receptor mediating varicella-zoster virus infection and cell-to-cell spread. Cell 127, 305-316 (2006).
    • (2006) Cell , vol.127 , pp. 305-316
    • Li, Q.1    Ali, M.A.2    Cohen, J.I.3
  • 161
    • 0034634319 scopus 로고    scopus 로고
    • Epstein-Barr virus entry into cells
    • Speck, P., Haan, K. M. & Longnecker, R. Epstein-Barr virus entry into cells. Virology 277, 1-5 (2000).
    • (2000) Virology , vol.277 , pp. 1-5
    • Speck, P.1    Haan, K.M.2    Longnecker, R.3
  • 162
    • 0042265526 scopus 로고    scopus 로고
    • Epidermal growth factor receptor is a cellular receptor for human cytomegalovirus
    • Wang, X., Huong, S. M., Chiu, M. L., Raab-Traub, N. & Huang, E. S. Epidermal growth factor receptor is a cellular receptor for human cytomegalovirus. Nature 424, 456-461 (2003).
    • (2003) Nature , vol.424 , pp. 456-461
    • Wang, X.1    Huong, S.M.2    Chiu, M.L.3    Raab-Traub, N.4    Huang, E.S.5
  • 164
    • 0033598990 scopus 로고    scopus 로고
    • CD46 is a cellular receptor for human herpesvirus 6
    • Santoro, F. et al. CD46 is a cellular receptor for human herpesvirus 6. Cell 99, 817-827 (1999).
    • (1999) Cell , vol.99 , pp. 817-827
    • Santoro, F.1
  • 165
    • 0037830588 scopus 로고    scopus 로고
    • Interaction of glycoprotein H of human herpesvirus 6 with the cellular receptor CD46
    • Santoro, F. et al. Interaction of glycoprotein H of human herpesvirus 6 with the cellular receptor CD46. J. Biol. Chem. 278, 25964-25969 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 25964-25969
    • Santoro, F.1
  • 166
    • 0037383517 scopus 로고    scopus 로고
    • Human herpesvirus 6 variant A glycoprotein H-glycoprotein L-glycoprotein Q complex associates with human CD46
    • Mori, Y., Yang, X., Akkapaiboon, P., Okuno, T. & Yamanishi, K. Human herpesvirus 6 variant A glycoprotein H-glycoprotein L-glycoprotein Q complex associates with human CD46. J. Virol. 77, 4992-4999 (2003).
    • (2003) J. Virol , vol.77 , pp. 4992-4999
    • Mori, Y.1    Yang, X.2    Akkapaiboon, P.3    Okuno, T.4    Yamanishi, K.5
  • 167
    • 0028271684 scopus 로고
    • CD4 is a critical component of the receptor for human herpesvirus 7: Interference with human immunodeficiency virus
    • Lusso, P. et al. CD4 is a critical component of the receptor for human herpesvirus 7: interference with human immunodeficiency virus. Proc. Natl Acad. Sci. USA 91, 3872-3876 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3872-3876
    • Lusso, P.1
  • 168
    • 0036008473 scopus 로고    scopus 로고
    • Integrin α3β1 (CD 49c/29) is a cellular receptor for Kaposi's sarcoma-associated herpesvirus (KSHV/ HHV-8) entry into the target cells
    • Akula, S. M., Pramod, N. P., Wang, F. Z. & Chandran, B. Integrin α3β1 (CD 49c/29) is a cellular receptor for Kaposi's sarcoma-associated herpesvirus (KSHV/ HHV-8) entry into the target cells. Cell 108, 407-419 (2002).
    • (2002) Cell , vol.108 , pp. 407-419
    • Akula, S.M.1    Pramod, N.P.2    Wang, F.Z.3    Chandran, B.4
  • 169
    • 33645468403 scopus 로고    scopus 로고
    • Kaposi's sarcomaassociated herpesvirus fusion-entry receptor: Cystine transporter xCT
    • Kaleeba, J. A. & Berger, E. A. Kaposi's sarcomaassociated herpesvirus fusion-entry receptor: cystine transporter xCT. Science 311, 1921-1924 (2006).
    • (2006) Science , vol.311 , pp. 1921-1924
    • Kaleeba, J.A.1    Berger, E.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.