메뉴 건너뛰기




Volumn 34, Issue 1, 2009, Pages 25-32

Tinkering with a viral ribonucleotide reductase

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; PROTEIN SUBUNIT; RECEPTOR INTERACTING PROTEIN 1; RIBONUCLEOTIDE REDUCTASE; UNCLASSIFIED DRUG; VIRUS DNA; VIRUS RNA;

EID: 58149279459     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2008.09.008     Document Type: Review
Times cited : (70)

References (54)
  • 1
    • 0017771466 scopus 로고
    • Evolution and tinkering
    • Jacob F. Evolution and tinkering. Science 196 (1977) 1161-1166
    • (1977) Science , vol.196 , pp. 1161-1166
    • Jacob, F.1
  • 2
    • 42949111649 scopus 로고    scopus 로고
    • Inhibition of proinflammatory and innate immune signaling pathways by a cytomegalovirus RIP1-interacting protein
    • Mack C., et al. Inhibition of proinflammatory and innate immune signaling pathways by a cytomegalovirus RIP1-interacting protein. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 3094-3099
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 3094-3099
    • Mack, C.1
  • 3
    • 47749133767 scopus 로고    scopus 로고
    • Cytomegalovirus M45 cell death suppression requires receptor-interacting protein (RIP) homotypic interaction motif (RHIM)-dependent interaction with RIP1
    • Upton J.W., et al. Cytomegalovirus M45 cell death suppression requires receptor-interacting protein (RIP) homotypic interaction motif (RHIM)-dependent interaction with RIP1. J. Biol. Chem. 283 (2008) 16966-16970
    • (2008) J. Biol. Chem. , vol.283 , pp. 16966-16970
    • Upton, J.W.1
  • 4
    • 36349022047 scopus 로고    scopus 로고
    • The family of Herpesviridae: a brief introduction
    • Knipe D.M., and Howley P.M. (Eds), Lippincott Williams & Wilkins
    • Pellet P.E., and Roizman B. The family of Herpesviridae: a brief introduction. In: Knipe D.M., and Howley P.M. (Eds). Fields Virology. 5th edn (2007), Lippincott Williams & Wilkins 2479-2499
    • (2007) Fields Virology. 5th edn , pp. 2479-2499
    • Pellet, P.E.1    Roizman, B.2
  • 5
    • 0028557489 scopus 로고
    • Ribonucleotide reductase of herpesviruses
    • Conner J., et al. Ribonucleotide reductase of herpesviruses. Rev. Med. Virol. 4 (1994) 25-34
    • (1994) Rev. Med. Virol. , vol.4 , pp. 25-34
    • Conner, J.1
  • 6
    • 0023880185 scopus 로고
    • Herpes simplex virus type 1-induced ribonucleotide reductase activity is dispensable for virus growth and DNA synthesis: isolation and characterization of an ICP6 lacZ insertion mutant
    • Goldstein D.J., and Weller S.K. Herpes simplex virus type 1-induced ribonucleotide reductase activity is dispensable for virus growth and DNA synthesis: isolation and characterization of an ICP6 lacZ insertion mutant. J. Virol. 62 (1988) 196-205
    • (1988) J. Virol. , vol.62 , pp. 196-205
    • Goldstein, D.J.1    Weller, S.K.2
  • 7
    • 0023739821 scopus 로고
    • Ribonucleotide reductase encoded by herpes simplex virus is a determinant of the pathogenicity of the virus in mice and a valid antiviral target
    • Cameron J.M., et al. Ribonucleotide reductase encoded by herpes simplex virus is a determinant of the pathogenicity of the virus in mice and a valid antiviral target. J. Gen. Virol. 69 (1988) 2607-2612
    • (1988) J. Gen. Virol. , vol.69 , pp. 2607-2612
    • Cameron, J.M.1
  • 8
    • 0024464324 scopus 로고
    • A herpes simplex virus ribonucleotide reductase deletion mutant is defective for productive acute and reactivatable latent infections of mice and for replication in mouse cells
    • Jacobson J.G., et al. A herpes simplex virus ribonucleotide reductase deletion mutant is defective for productive acute and reactivatable latent infections of mice and for replication in mouse cells. Virology 173 (1989) 276-283
    • (1989) Virology , vol.173 , pp. 276-283
    • Jacobson, J.G.1
  • 9
    • 0027471728 scopus 로고
    • Ribonucleotide reductase-deficient mutants of pseudorabies virus are avirulent for pigs and induce partial protective immunity
    • de Wind N., et al. Ribonucleotide reductase-deficient mutants of pseudorabies virus are avirulent for pigs and induce partial protective immunity. J. Gen. Virol. 74 (1993) 351-359
    • (1993) J. Gen. Virol. , vol.74 , pp. 351-359
    • de Wind, N.1
  • 10
    • 0028333801 scopus 로고
    • Deletion of the varicella-zoster virus large subunit of ribonucleotide reductase impairs growth of virus in vitro
    • Heineman T.C., and Cohen J.I. Deletion of the varicella-zoster virus large subunit of ribonucleotide reductase impairs growth of virus in vitro. J. Virol. 68 (1994) 3317-3323
    • (1994) J. Virol. , vol.68 , pp. 3317-3323
    • Heineman, T.C.1    Cohen, J.I.2
  • 11
    • 57649157806 scopus 로고    scopus 로고
    • Virus replication strategies
    • Knipe D.M., and Howley P.M. (Eds), Lippincott Williams & Wilkins
    • Ball A.L. Virus replication strategies. In: Knipe D.M., and Howley P.M. (Eds). Fields Virology. 5th edn (2007), Lippincott Williams & Wilkins 119-139
    • (2007) Fields Virology. 5th edn , pp. 119-139
    • Ball, A.L.1
  • 12
    • 4644337964 scopus 로고    scopus 로고
    • The evolution of large DNA viruses: combining genomic information of viruses and their hosts
    • Shackelton L.A., and Holmes E.C. The evolution of large DNA viruses: combining genomic information of viruses and their hosts. Trends Microbiol. 12 (2004) 458-465
    • (2004) Trends Microbiol. , vol.12 , pp. 458-465
    • Shackelton, L.A.1    Holmes, E.C.2
  • 13
    • 33645054794 scopus 로고    scopus 로고
    • Topics in herpesvirus genomics and evolution
    • McGeoch D.J., et al. Topics in herpesvirus genomics and evolution. Virus Res. 117 (2006) 90-104
    • (2006) Virus Res. , vol.117 , pp. 90-104
    • McGeoch, D.J.1
  • 14
    • 1842299978 scopus 로고
    • The role of herpes simplex virus thymidine kinase expression in pathogenesis and latency
    • Becker Y., and Darai G. (Eds), Springer
    • Tenser R.B. The role of herpes simplex virus thymidine kinase expression in pathogenesis and latency. In: Becker Y., and Darai G. (Eds). Pathogenesis of Human Herpes Viruses Due to Specific Pathogenicity Genes (1994), Springer 68-86
    • (1994) Pathogenesis of Human Herpes Viruses Due to Specific Pathogenicity Genes , pp. 68-86
    • Tenser, R.B.1
  • 15
    • 0036851310 scopus 로고    scopus 로고
    • Identification of new herpesvirus gene homologs in the human genome
    • Holzerlandt R., et al. Identification of new herpesvirus gene homologs in the human genome. Genome Res. 12 (2002) 1739-1748
    • (2002) Genome Res. , vol.12 , pp. 1739-1748
    • Holzerlandt, R.1
  • 16
    • 0032853635 scopus 로고    scopus 로고
    • The U28 ORF of human herpesvirus-7 does not encode a functional ribonucleotide reductase R1 subunit
    • Sun Y., and Conner J. The U28 ORF of human herpesvirus-7 does not encode a functional ribonucleotide reductase R1 subunit. J. Gen. Virol. 80 (1999) 2713-2718
    • (1999) J. Gen. Virol. , vol.80 , pp. 2713-2718
    • Sun, Y.1    Conner, J.2
  • 17
    • 10744221040 scopus 로고    scopus 로고
    • The human cytomegalovirus UL45 gene product is a late, virion-associated protein and influences virus growth at low multiplicities of infection
    • Patrone M., et al. The human cytomegalovirus UL45 gene product is a late, virion-associated protein and influences virus growth at low multiplicities of infection. J. Gen. Virol. 84 (2003) 3359-3370
    • (2003) J. Gen. Virol. , vol.84 , pp. 3359-3370
    • Patrone, M.1
  • 18
    • 1842588435 scopus 로고    scopus 로고
    • The ribonucleotide reductase R1 homolog of murine cytomegalovirus is not a functional enzyme subunit but is required for pathogenesis
    • Lembo D., et al. The ribonucleotide reductase R1 homolog of murine cytomegalovirus is not a functional enzyme subunit but is required for pathogenesis. J. Virol. 78 (2004) 4278-4288
    • (2004) J. Virol. , vol.78 , pp. 4278-4288
    • Lembo, D.1
  • 19
    • 3142528493 scopus 로고    scopus 로고
    • Evidence that the human cytomegalovirus 46-kDa UL72 protein is not an active dUTPase but a late protein dispensable for replication in fibroblasts
    • Caposio P., et al. Evidence that the human cytomegalovirus 46-kDa UL72 protein is not an active dUTPase but a late protein dispensable for replication in fibroblasts. Virology 325 (2004) 264-276
    • (2004) Virology , vol.325 , pp. 264-276
    • Caposio, P.1
  • 20
    • 0025344377 scopus 로고
    • Analysis of the protein-coding content of the sequence of human cytomegalovirus strain AD169
    • Chee M.S., et al. Analysis of the protein-coding content of the sequence of human cytomegalovirus strain AD169. Curr. Top. Microbiol. Immunol. 154 (1990) 125-169
    • (1990) Curr. Top. Microbiol. Immunol. , vol.154 , pp. 125-169
    • Chee, M.S.1
  • 21
    • 0029981145 scopus 로고    scopus 로고
    • Analysis of the complete DNA sequence of murine cytomegalovirus
    • Rawlinson W.D., et al. Analysis of the complete DNA sequence of murine cytomegalovirus. J. Virol. 70 (1996) 8833-8849
    • (1996) J. Virol. , vol.70 , pp. 8833-8849
    • Rawlinson, W.D.1
  • 22
    • 0035958740 scopus 로고    scopus 로고
    • In silico structural and functional analysis of the human cytomegalovirus (HHV5) genome
    • Novotny J., et al. In silico structural and functional analysis of the human cytomegalovirus (HHV5) genome. J. Mol. Biol. 310 (2001) 1151-1166
    • (2001) J. Mol. Biol. , vol.310 , pp. 1151-1166
    • Novotny, J.1
  • 24
    • 0031458253 scopus 로고    scopus 로고
    • Sequences of the ribonucleotide reductase-encoding genes of felid herpesvirus 1 and molecular phylogenetic analysis
    • Willoughby K., et al. Sequences of the ribonucleotide reductase-encoding genes of felid herpesvirus 1 and molecular phylogenetic analysis. Virus Genes 15 (1997) 203-218
    • (1997) Virus Genes , vol.15 , pp. 203-218
    • Willoughby, K.1
  • 25
    • 0038362228 scopus 로고    scopus 로고
    • The human cytomegalovirus
    • Landolfo S., et al. The human cytomegalovirus. Pharmacol. Ther. 98 (2003) 269-297
    • (2003) Pharmacol. Ther. , vol.98 , pp. 269-297
    • Landolfo, S.1
  • 26
    • 36348950198 scopus 로고    scopus 로고
    • The S phase of the cell cycle and its perturbation by human cytomegalovirus
    • Bain M., and Sinclair J. The S phase of the cell cycle and its perturbation by human cytomegalovirus. Rev. Med. Virol. 17 (2007) 423-434
    • (2007) Rev. Med. Virol. , vol.17 , pp. 423-434
    • Bain, M.1    Sinclair, J.2
  • 28
    • 53749101697 scopus 로고    scopus 로고
    • Cell cycle independent expression of immediate early gene 3 results in a G1 and G2 arrest in MCMV-infected cells
    • Wiebusch L., et al. Cell cycle independent expression of immediate early gene 3 results in a G1 and G2 arrest in MCMV-infected cells. J. Virol. 82 (2008) 10188-10198
    • (2008) J. Virol. , vol.82 , pp. 10188-10198
    • Wiebusch, L.1
  • 29
    • 0035846920 scopus 로고    scopus 로고
    • A ribonucleotide reductase homolog of cytomegalovirus and endothelial cell tropism
    • Brune W., et al. A ribonucleotide reductase homolog of cytomegalovirus and endothelial cell tropism. Science 291 (2001) 303-305
    • (2001) Science , vol.291 , pp. 303-305
    • Brune, W.1
  • 30
    • 14744299357 scopus 로고    scopus 로고
    • The RIP kinases: crucial integrators of cellular stress
    • Meylan E., and Tschopp J. The RIP kinases: crucial integrators of cellular stress. Trends Biochem. Sci. 30 (2005) 151-159
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 151-159
    • Meylan, E.1    Tschopp, J.2
  • 31
    • 33847051539 scopus 로고    scopus 로고
    • RIP1, a kinase on the crossroads of a cell's decision to live or die
    • Festjens N., et al. RIP1, a kinase on the crossroads of a cell's decision to live or die. Cell Death Differ. 14 (2007) 400-410
    • (2007) Cell Death Differ. , vol.14 , pp. 400-410
    • Festjens, N.1
  • 32
    • 2442642691 scopus 로고    scopus 로고
    • RIP1 is an essential mediator of Toll-like receptor 3-induced NF-κ B activation
    • Meylan E., et al. RIP1 is an essential mediator of Toll-like receptor 3-induced NF-κ B activation. Nat. Immunol. 5 (2004) 503-507
    • (2004) Nat. Immunol. , vol.5 , pp. 503-507
    • Meylan, E.1
  • 33
    • 0037114185 scopus 로고    scopus 로고
    • Cutting edge: a novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-β promoter in the Toll-like receptor signaling
    • Yamamoto M., et al. Cutting edge: a novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-β promoter in the Toll-like receptor signaling. J. Immunol. 169 (2002) 6668-6672
    • (2002) J. Immunol. , vol.169 , pp. 6668-6672
    • Yamamoto, M.1
  • 34
    • 17144413785 scopus 로고    scopus 로고
    • Apoptosis induced by the toll-like receptor adaptor TRIF is dependent on its receptor interacting protein homotypic interaction motif
    • Kaiser W.J., and Offermann M.K. Apoptosis induced by the toll-like receptor adaptor TRIF is dependent on its receptor interacting protein homotypic interaction motif. J. Immunol. 174 (2005) 4942-4952
    • (2005) J. Immunol. , vol.174 , pp. 4942-4952
    • Kaiser, W.J.1    Offermann, M.K.2
  • 35
    • 0036720530 scopus 로고    scopus 로고
    • The human cytomegalovirus ribonucleotide reductase homolog UL45 is dispensable for growth in endothelial cells, as determined by a BAC-cloned clinical isolate of human cytomegalovirus with preserved wild-type characteristics
    • Hahn G., et al. The human cytomegalovirus ribonucleotide reductase homolog UL45 is dispensable for growth in endothelial cells, as determined by a BAC-cloned clinical isolate of human cytomegalovirus with preserved wild-type characteristics. J. Virol. 76 (2002) 9551-9555
    • (2002) J. Virol. , vol.76 , pp. 9551-9555
    • Hahn, G.1
  • 36
    • 0030752881 scopus 로고    scopus 로고
    • The large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) is associated with the virion tegument and has PK activity
    • Smith C.C., and Aurelian L. The large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) is associated with the virion tegument and has PK activity. Virology 234 (1997) 235-242
    • (1997) Virology , vol.234 , pp. 235-242
    • Smith, C.C.1    Aurelian, L.2
  • 37
    • 0031916707 scopus 로고    scopus 로고
    • The R1 subunit of herpes simplex virus ribonucleotide reductase is a good substrate for host cell protein kinases but is not itself a protein kinase
    • Langelier Y., et al. The R1 subunit of herpes simplex virus ribonucleotide reductase is a good substrate for host cell protein kinases but is not itself a protein kinase. J. Biol. Chem. 273 (1998) 1435-1443
    • (1998) J. Biol. Chem. , vol.273 , pp. 1435-1443
    • Langelier, Y.1
  • 38
    • 0037526521 scopus 로고    scopus 로고
    • The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone-like activity similar to Hsp27
    • Chabaud S., et al. The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone-like activity similar to Hsp27. FEBS Lett. 545 (2003) 213-218
    • (2003) FEBS Lett. , vol.545 , pp. 213-218
    • Chabaud, S.1
  • 39
    • 0036843525 scopus 로고    scopus 로고
    • The R1 subunit of herpes simplex virus ribonucleotide reductase protects cells against apoptosis at, or upstream of, caspase-8 activation
    • Langelier Y., et al. The R1 subunit of herpes simplex virus ribonucleotide reductase protects cells against apoptosis at, or upstream of, caspase-8 activation. J. Gen. Virol. 83 (2002) 2779-2789
    • (2002) J. Gen. Virol. , vol.83 , pp. 2779-2789
    • Langelier, Y.1
  • 40
    • 0037228190 scopus 로고    scopus 로고
    • The herpes simplex virus type 2 R1 protein kinase (ICP10 PK) functions as a dominant regulator of apoptosis in hippocampal neurons involving activation of the ERK survival pathway and upregulation of the antiapoptotic protein Bag-1
    • Perkins D., et al. The herpes simplex virus type 2 R1 protein kinase (ICP10 PK) functions as a dominant regulator of apoptosis in hippocampal neurons involving activation of the ERK survival pathway and upregulation of the antiapoptotic protein Bag-1. J. Virol. 77 (2003) 1292-1305
    • (2003) J. Virol. , vol.77 , pp. 1292-1305
    • Perkins, D.1
  • 41
    • 0036120791 scopus 로고    scopus 로고
    • Expression of herpes simplex virus type 2 protein ICP10 PK rescues neurons from apoptosis due to serum deprivation or genetic defects
    • Perkins D., et al. Expression of herpes simplex virus type 2 protein ICP10 PK rescues neurons from apoptosis due to serum deprivation or genetic defects. Exp. Neurol. 174 (2002) 118-122
    • (2002) Exp. Neurol. , vol.174 , pp. 118-122
    • Perkins, D.1
  • 42
    • 33846520504 scopus 로고    scopus 로고
    • The HSV-2 protein ICP10PK prevents neuronal apoptosis and loss of function in an in vivo model of neurodegeneration associated with glutamate excitotoxicity
    • Golembewski E.K., et al. The HSV-2 protein ICP10PK prevents neuronal apoptosis and loss of function in an in vivo model of neurodegeneration associated with glutamate excitotoxicity. Exp. Neurol. 203 (2007) 381-393
    • (2007) Exp. Neurol. , vol.203 , pp. 381-393
    • Golembewski, E.K.1
  • 43
    • 33846794626 scopus 로고    scopus 로고
    • The ribonucleotide reductase domain of the R1 subunit of herpes simplex virus type 2 ribonucleotide reductase is essential for R1 antiapoptotic function
    • Chabaud S., et al. The ribonucleotide reductase domain of the R1 subunit of herpes simplex virus type 2 ribonucleotide reductase is essential for R1 antiapoptotic function. J. Gen. Virol. 88 (2007) 384-394
    • (2007) J. Gen. Virol. , vol.88 , pp. 384-394
    • Chabaud, S.1
  • 44
    • 21344465226 scopus 로고    scopus 로고
    • Herpes simplex virus type 2 encodes a heat shock protein homologue with apoptosis regulatory functions
    • Gober M.D., et al. Herpes simplex virus type 2 encodes a heat shock protein homologue with apoptosis regulatory functions. Front. Biosci. 10 (2005) 2788-2803
    • (2005) Front. Biosci. , vol.10 , pp. 2788-2803
    • Gober, M.D.1
  • 45
    • 0028914853 scopus 로고
    • Molecular phylogeny and evolutionary timescale for the family of mammalian herpesviruses
    • McGeoch D.J., et al. Molecular phylogeny and evolutionary timescale for the family of mammalian herpesviruses. J. Mol. Biol. 247 (1995) 443-458
    • (1995) J. Mol. Biol. , vol.247 , pp. 443-458
    • McGeoch, D.J.1
  • 46
    • 0032033132 scopus 로고    scopus 로고
    • The death domain kinase RIP mediates the TNF-induced NF-κB signal
    • Kelliher M.A., et al. The death domain kinase RIP mediates the TNF-induced NF-κB signal. Immunity 8 (1998) 297-303
    • (1998) Immunity , vol.8 , pp. 297-303
    • Kelliher, M.A.1
  • 47
    • 27744561393 scopus 로고    scopus 로고
    • Rip1 mediates the Trif-dependent toll-like receptor 3- and 4-induced NF-κB activation but does not contribute to interferon regulatory factor 3 activation
    • Cusson-Hermance N., et al. Rip1 mediates the Trif-dependent toll-like receptor 3- and 4-induced NF-κB activation but does not contribute to interferon regulatory factor 3 activation. J. Biol. Chem. 280 (2005) 36560-36566
    • (2005) J. Biol. Chem. , vol.280 , pp. 36560-36566
    • Cusson-Hermance, N.1
  • 48
    • 9244236078 scopus 로고    scopus 로고
    • A FADD-dependent innate immune mechanism in mammalian cells
    • Balachandran S., et al. A FADD-dependent innate immune mechanism in mammalian cells. Nature 432 (2004) 401-405
    • (2004) Nature , vol.432 , pp. 401-405
    • Balachandran, S.1
  • 49
    • 43049174990 scopus 로고    scopus 로고
    • TRADD protein is an essential component of the RIG-like helicase antiviral pathway
    • Michallet M.C., et al. TRADD protein is an essential component of the RIG-like helicase antiviral pathway. Immunity 28 (2008) 651-661
    • (2008) Immunity , vol.28 , pp. 651-661
    • Michallet, M.C.1
  • 50
    • 28944447430 scopus 로고    scopus 로고
    • PIDD mediates NF-κB activation in response to DNA damage
    • Janssens S., et al. PIDD mediates NF-κB activation in response to DNA damage. Cell 123 (2005) 1079-1092
    • (2005) Cell , vol.123 , pp. 1079-1092
    • Janssens, S.1
  • 51
    • 31344461659 scopus 로고    scopus 로고
    • Innate immune recognition of viral infection
    • Kawai T., and Akira S. Innate immune recognition of viral infection. Nat. Immunol. 7 (2006) 131-137
    • (2006) Nat. Immunol. , vol.7 , pp. 131-137
    • Kawai, T.1    Akira, S.2
  • 52
    • 0028050514 scopus 로고
    • Intron-containing T4 bacteriophage gene sunY encodes an anaerobic ribonucleotide reductase
    • Young P., et al. Intron-containing T4 bacteriophage gene sunY encodes an anaerobic ribonucleotide reductase. J. Biol. Chem. 269 (1994) 20229-20232
    • (1994) J. Biol. Chem. , vol.269 , pp. 20229-20232
    • Young, P.1
  • 53
    • 0027456546 scopus 로고
    • DNA sequence, structure and gene expression of mycobacteriophage L5: a phage system for mycobacterial genetics
    • Hatfull G.F., and Sarkis G.J. DNA sequence, structure and gene expression of mycobacteriophage L5: a phage system for mycobacterial genetics. Mol. Microbiol. 7 (1993) 395-405
    • (1993) Mol. Microbiol. , vol.7 , pp. 395-405
    • Hatfull, G.F.1    Sarkis, G.J.2
  • 54
    • 0033834072 scopus 로고    scopus 로고
    • Iridovirus homologues of cellular genes-implications for the molecular evolution of large DNA viruses
    • Tidona C.A., and Darai G. Iridovirus homologues of cellular genes-implications for the molecular evolution of large DNA viruses. Virus Genes 21 (2000) 77-81
    • (2000) Virus Genes , vol.21 , pp. 77-81
    • Tidona, C.A.1    Darai, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.