Gillian Elliott

Summary

Affiliation: Marie Curie Research Institute
Country: UK

Publications

  1. ncbi request reprint Phosphorylation of the herpes simplex virus type 1 tegument protein VP22
    G Elliott
    Marie Curie Research Institute, The Chart, Oxteo, Surrey, United Kingdom
    Virology 226:140-5. 1996
  2. pmc Deletion of the herpes simplex virus VP22-encoding gene (UL49) alters the expression, localization, and virion incorporation of ICP0
    Gillian Elliott
    Marie Curie Research Institute, Oxted, Surrey, UK
    J Virol 79:9735-45. 2005
  3. pmc Cytoplasm-to-nucleus translocation of a herpesvirus tegument protein during cell division
    G Elliott
    Virus Assembly Group, Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, United Kingdom
    J Virol 74:2131-41. 2000
  4. pmc Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22
    G Elliott
    Virus Assembly Group, Marie Curie Research Institute, Oxted, Surrey RH1 OTL, United Kingdom
    J Virol 73:6203-6. 1999
  5. pmc Live-cell analysis of a green fluorescent protein-tagged herpes simplex virus infection
    G Elliott
    Marie Curie Research Institute, The Chart, Oxted, Surrey RH1 0TL, United Kingdom
    J Virol 73:4110-9. 1999
  6. pmc Herpes simplex virus type 1 tegument protein VP22 induces the stabilization and hyperacetylation of microtubules
    G Elliott
    Marie Curie Research Institute, Oxted, Surrey RH8 OTL, United Kingdom
    J Virol 72:6448-55. 1998
  7. pmc RNA binding by the herpes simplex virus type 1 nucleocytoplasmic shuttling protein UL47 is mediated by an N-terminal arginine-rich domain that also functions as its nuclear localization signal
    Michelle Donnelly
    Virus Assembly Group, Marie Curie Research Institute, Oxted, Surrey RH8 OTL, United Kingdom
    J Virol 81:2283-96. 2007
  8. pmc Sequential localization of two herpes simplex virus tegument proteins to punctate nuclear dots adjacent to ICP0 domains
    Ian Hutchinson
    Virus Assembly Group, Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, UK
    J Virol 76:10365-73. 2002
  9. pmc Phosphorylation of the herpes simplex virus tegument protein VP22 has no effect on incorporation of VP22 into the virus but is involved in optimal expression and virion packaging of ICP0
    Corinne Potel
    Virus Assembly Group, Marie Curie Research Institute, Oxted, Surrey, United Kingdom
    J Virol 79:14057-68. 2005
  10. pmc Herpes simplex virus tegument protein VP22 contains an internal VP16 interaction domain and a C-terminal domain that are both required for VP22 assembly into the virus particle
    Wali Hafezi
    Marie Curie Research Institute, Oxted, Surrey, UK
    J Virol 79:13082-93. 2005

Collaborators

  • John McLauchlan
  • H M Browne
  • Janneke Verhagen
  • Michelle Donnelly
  • Ian Hutchinson
  • Paul Williams
  • Corinne Potel
  • Wali Hafezi
  • Ana Martin
  • Emmanuelle Bernard
  • Rachelle Cook
  • Alison Whiteley
  • Peter O'Hare

Detail Information

Publications14

  1. ncbi request reprint Phosphorylation of the herpes simplex virus type 1 tegument protein VP22
    G Elliott
    Marie Curie Research Institute, The Chart, Oxteo, Surrey, United Kingdom
    Virology 226:140-5. 1996
    ..This kinase also phosphorylates VP22 at the N-terminus in intact capsid-tegument structures. Casein kinase II is therefore likely to be the major kinase of VP22 during infection...
  2. pmc Deletion of the herpes simplex virus VP22-encoding gene (UL49) alters the expression, localization, and virion incorporation of ICP0
    Gillian Elliott
    Marie Curie Research Institute, Oxted, Surrey, UK
    J Virol 79:9735-45. 2005
    ..This report provides the first direct evidence that VP22 influences virus assembly...
  3. pmc Cytoplasm-to-nucleus translocation of a herpesvirus tegument protein during cell division
    G Elliott
    Virus Assembly Group, Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, United Kingdom
    J Virol 74:2131-41. 2000
    ..Thus, VP22 utilizes an unusual pathway for nuclear targeting in cells expressing the protein which differs from the nuclear targeting pathway used during intercellular trafficking...
  4. pmc Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22
    G Elliott
    Virus Assembly Group, Marie Curie Research Institute, Oxted, Surrey RH1 OTL, United Kingdom
    J Virol 73:6203-6. 1999
    ..Furthermore, we show that a mutant of VP22 which has both sites altered is unable to incorporate phosphate in vivo, confirming that there are no other phosphorylation sites within VP22...
  5. pmc Live-cell analysis of a green fluorescent protein-tagged herpes simplex virus infection
    G Elliott
    Marie Curie Research Institute, The Chart, Oxted, Surrey RH1 0TL, United Kingdom
    J Virol 73:4110-9. 1999
    ..In this way, we have for the first time visualized the trafficking of a herpesvirus structural component within live, infected cells...
  6. pmc Herpes simplex virus type 1 tegument protein VP22 induces the stabilization and hyperacetylation of microtubules
    G Elliott
    Marie Curie Research Institute, Oxted, Surrey RH8 OTL, United Kingdom
    J Virol 72:6448-55. 1998
    ..Taken together, these results suggest that VP22 exhibits the properties of a classical microtubule-associated protein (MAP) during both transfection and infection. This is the first demonstration of a MAP encoded by an animal virus...
  7. pmc RNA binding by the herpes simplex virus type 1 nucleocytoplasmic shuttling protein UL47 is mediated by an N-terminal arginine-rich domain that also functions as its nuclear localization signal
    Michelle Donnelly
    Virus Assembly Group, Marie Curie Research Institute, Oxted, Surrey RH8 OTL, United Kingdom
    J Virol 81:2283-96. 2007
    ..Using RNA immunoprecipitations, we demonstrate that hUL47 is also bound in vivo to at least one viral transcript, the ICP0 mRNA. Taken together, these results suggest that hUL47 may play a role in RNA biogenesis in the infected cell...
  8. pmc Sequential localization of two herpes simplex virus tegument proteins to punctate nuclear dots adjacent to ICP0 domains
    Ian Hutchinson
    Virus Assembly Group, Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, UK
    J Virol 76:10365-73. 2002
    ..Hence, these tegument proteins join a growing number of proteins that are targeted to discrete nuclear domains in the herpesvirus-infected cell nucleus...
  9. pmc Phosphorylation of the herpes simplex virus tegument protein VP22 has no effect on incorporation of VP22 into the virus but is involved in optimal expression and virion packaging of ICP0
    Corinne Potel
    Virus Assembly Group, Marie Curie Research Institute, Oxted, Surrey, United Kingdom
    J Virol 79:14057-68. 2005
    ..Taken together, these results suggest an important role for VP22 phosphorylation in its relationship with ICP0...
  10. pmc Herpes simplex virus tegument protein VP22 contains an internal VP16 interaction domain and a C-terminal domain that are both required for VP22 assembly into the virus particle
    Wali Hafezi
    Marie Curie Research Institute, Oxted, Surrey, UK
    J Virol 79:13082-93. 2005
    ....
  11. pmc Characterization of a novel transferable CRM-1-independent nuclear export signal in a herpesvirus tegument protein that shuttles between the nucleus and cytoplasm
    Janneke Verhagen
    Virus Assembly Group, Marie Curie Research Institute, Oxted, United Kingdom
    J Virol 80:10021-35. 2006
    ..As this new sequence bears little similarity to other export signals so far defined, we suggest it may be involved in bUL47 export from the nucleus via a novel cellular receptor...
  12. pmc Herpes simplex virus tegument protein VP22 contains overlapping domains for cytoplasmic localization, microtubule interaction, and chromatin binding
    Ana Martin
    Virus Assembly Group, Marie Curie Research Institute, Oxted, Surrey RH8 0TL, United Kingdom
    J Virol 76:4961-70. 2002
    ..Hence, the signals involved in dictating the complex localization patterns of VP22 are present in overlapping regions of the protein...
  13. pmc Nucleocytoplasmic shuttling of bovine herpesvirus 1 UL47 protein in infected cells
    Janneke Verhagen
    Virus Assembly Group, Marie Curie Research Institute, Oxted, Surrey RH8 OTL, United Kingdom
    J Virol 80:1059-63. 2006
    ..Furthermore, we demonstrate that actinomycin D inhibits the reaccumulation of UL47 in the nuclei of infected cells. These results suggest that UL47 exhibits behavior similar to that of previously characterized RNA-transporting proteins...
  14. pmc Characterization of a CRM1-dependent nuclear export signal in the C terminus of herpes simplex virus type 1 tegument protein UL47
    Paul Williams
    Department of Virology, Faculty of Medicine, Imperial College London, London, United Kingdom
    J Virol 82:10946-52. 2008
    ..Finally, we show that the hUL47 NES is sensitive to the inhibitor of CRM1-mediated nuclear export leptomycin B. Hence, hUL47 joins a growing list of virus-encoded RNA-binding proteins that use CRM1 to exit the nucleus...