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Gene Review

UL48  -  transactivates immediate early genes

Human herpesvirus 1

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Disease relevance of UL48


High impact information on UL48

  • We have discovered a ubiquitin (Ub)-specific cysteine protease encoded within the N-terminal approximately 500 residues of the UL36 gene product, the largest (3164 aa) tegument protein of herpes simplex virus 1 (HSV-1) [5].
  • Herpes simplex virus-1 (HSV-1) virions are large, complex enveloped particles containing a proteinaceous tegument layer connected to an icosahedral capsid [6].
  • Nuclear transport of the viral tegument protein VP16, transport of viral capsids to the nuclear pore, and downstream events (including expression of immediate-early genes and viral plaque formation) were substantially reduced in cells transfected with dominant-negative mutants of FAK or small interfering RNA designed to inhibit FAK expression [7].
  • CD4(+) T cell clones were isolated that recognized and had high binding affinities to epitopes in HSV-2 tegument proteins [8].
  • Images were obtained of 1) the intact, enveloped virus; 2) the underlying capsid with associated tegument proteins along with fragments of the membrane; 3) the capsomeres composing the capsid and their surface arrangement; 4) damaged and partially degraded capsids with missing capsomeres; and 5) the DNA extruded from damaged virions [9].

Chemical compound and disease context of UL48

  • Identification of a 709-Amino-Acid Internal Nonessential Region within the Essential Conserved Tegument Protein (p)UL36 of Pseudorabies Virus [10].
  • The protein kinase associated with purified herpes simplex virus 1 and 2 virions partitioned with the capsid-tegument structures and was not solubilized by non-ionic detergents and low, non-inhibitory concentrations of urea [11].

Biological context of UL48


Anatomical context of UL48

  • The UL11 gene of herpes simplex virus type 1 encodes a 96-amino-acid tegument protein that is myristylated, palmitylated, and phosphorylated and is found on the cytoplasmic faces of nuclear, Golgi apparatus-derived, and plasma membranes of infected cells [16].
  • We have previously shown (G. E. Lee, G. A. Church, and D. W. Wilson, J. Virol. 77:2038-2045, 2003) that the virion host shutoff (Vhs) tegument protein is largely insoluble in HSV-infected cells and is also stably associated with membranes [17].
  • After contact of infectious virus with the cell plasma membrane, discernible changes of the envelope and tegument could be seen by electron microscopy [18].
  • In this study, we have tested the hypothesis that latent infection of sensory neurons results from the failure of alpha TIF, a tegument protein, to be transported from the nerve endings to the nucleus of the sensory neuron [19].
  • After intranuclear assembly, nucleocapsids bud at the inner leaflet of the nuclear membrane, resulting in enveloped particles in the perinuclear space that contain a sharply bordered rim of tegument and a smooth envelope surface [20].

Associations of UL48 with chemical compounds

  • We have identified an interaction between VP22, an abundant tegument protein and the cytoplasmic tail of glycoprotein E (gE) [3].

Other interactions of UL48

  • The interaction of UL46-UL48 was verified using an in vitro pull-down assay [21].
  • Marek's disease virus (MDV) homologues of herpes simplex virus type 1 UL49 (VP22) and UL48 (VP16) genes: high-level expression and characterization of MDV-1 VP22 and VP16 [22].
  • Moreover, analysis of isolated intracellular capsids showed that both phosphorylated and unphosphorylated forms of the US10 product were also associated with the capsid/tegument [23].
  • From studies on the resultant virus recombinant using a monoclonal antibody that recognizes the inserted epitope we find that, contrary to a previous report, the UL37 protein is a structural component of both virions and L particles and is present in the tegument of virus particles [24].

Analytical, diagnostic and therapeutic context of UL48


  1. DNA sequence of the herpes simplex virus type 1 gene whose product is responsible for transcriptional activation of immediate early promoters. Dalrymple, M.A., McGeoch, D.J., Davison, A.J., Preston, C.M. Nucleic Acids Res. (1985) [Pubmed]
  2. Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument. Morrison, E.E., Wang, Y.F., Meredith, D.M. J. Virol. (1998) [Pubmed]
  3. A conserved region of the herpes simplex virus type 1 tegument protein VP22 facilitates interaction with the cytoplasmic tail of glycoprotein E (gE). O'regan, K.J., Bucks, M.A., Murphy, M.A., Wills, J.W., Courtney, R.J. Virology (2007) [Pubmed]
  4. Antigenic and protein sequence homology between VP13/14, a herpes simplex virus type 1 tegument protein, and gp10, a glycoprotein of equine herpesvirus 1 and 4. Whittaker, G.R., Riggio, M.P., Halliburton, I.W., Killington, R.A., Allen, G.P., Meredith, D.M. J. Virol. (1991) [Pubmed]
  5. A deubiquitinating enzyme encoded by HSV-1 belongs to a family of cysteine proteases that is conserved across the family Herpesviridae. Kattenhorn, L.M., Korbel, G.A., Kessler, B.M., Spooner, E., Ploegh, H.L. Mol. Cell (2005) [Pubmed]
  6. Structure of the herpesvirus major capsid protein. Bowman, B.R., Baker, M.L., Rixon, F.J., Chiu, W., Quiocho, F.A. EMBO J. (2003) [Pubmed]
  7. Focal adhesion kinase plays a pivotal role in herpes simplex virus entry. Cheshenko, N., Liu, W., Satlin, L.M., Herold, B.C. J. Biol. Chem. (2005) [Pubmed]
  8. T cell immunity to herpes simplex viruses in seronegative subjects: silent infection or acquired immunity? Posavad, C.M., Wald, A., Hosken, N., Huang, M.L., Koelle, D.M., Ashley, R.L., Corey, L. J. Immunol. (2003) [Pubmed]
  9. Rapid visualization at high resolution of pathogens by atomic force microscopy: structural studies of herpes simplex virus-1. Plomp, M., Rice, M.K., Wagner, E.K., McPherson, A., Malkin, A.J. Am. J. Pathol. (2002) [Pubmed]
  10. Identification of a 709-Amino-Acid Internal Nonessential Region within the Essential Conserved Tegument Protein (p)UL36 of Pseudorabies Virus. Böttcher, S., Klupp, B.G., Granzow, H., Fuchs, W., Michael, K., Mettenleiter, T.C. J. Virol. (2006) [Pubmed]
  11. Herpes simplex virus phosphoproteins. II. Characterization of the virion protein kinase and of the polypeptides phosphorylated in the virion. Lemaster, S., Roizman, B. J. Virol. (1980) [Pubmed]
  12. Post-translational modification of the tegument proteins (VP13 and VP14) of herpes simplex virus type 1 by glycosylation and phosphorylation. Meredith, D.M., Lindsay, J.A., Halliburton, I.W., Whittaker, G.R. J. Gen. Virol. (1991) [Pubmed]
  13. The UL48 tegument protein of pseudorabies virus is critical for intracytoplasmic assembly of infectious virions. Fuchs, W., Granzow, H., Klupp, B.G., Kopp, M., Mettenleiter, T.C. J. Virol. (2002) [Pubmed]
  14. Identification and characterization of a cDNA clone derived from the Marek's disease tumour cell line RPL1 encoding a homologue of alpha-transinducing factor (VP16) of HSV-1. Koptidesová, D., Kopácek, J., Zelník, V., Ross, N.L., Pastoreková, S., Pastorek, J. Arch. Virol. (1995) [Pubmed]
  15. Identification of herpes simplex virus DNA sequences which encode a trans-acting polypeptide responsible for stimulation of immediate early transcription. Campbell, M.E., Palfreyman, J.W., Preston, C.M. J. Mol. Biol. (1984) [Pubmed]
  16. Packaging Determinants in the UL11 Tegument Protein of Herpes Simplex Virus Type 1. Loomis, J.S., Courtney, R.J., Wills, J.W. J. Virol. (2006) [Pubmed]
  17. The amino terminus of the herpes simplex virus 1 protein vhs mediates membrane association and tegument incorporation. Mukhopadhyay, A., Lee, G.E., Wilson, D.W. J. Virol. (2006) [Pubmed]
  18. Herpes simplex virus type 1 entry through a cascade of virus-cell interactions requires different roles of gD and gH in penetration. Fuller, A.O., Lee, W.C. J. Virol. (1992) [Pubmed]
  19. Expression of the herpes simplex virus 1 alpha transinducing factor (VP16) does not induce reactivation of latent virus or prevent the establishment of latency in mice. Sears, A.E., Hukkanen, V., Labow, M.A., Levine, A.J., Roizman, B. J. Virol. (1991) [Pubmed]
  20. Egress of alphaherpesviruses: comparative ultrastructural study. Granzow, H., Klupp, B.G., Fuchs, W., Veits, J., Osterrieder, N., Mettenleiter, T.C. J. Virol. (2001) [Pubmed]
  21. Determination of interactions between tegument proteins of herpes simplex virus type 1. Vittone, V., Diefenbach, E., Triffett, D., Douglas, M.W., Cunningham, A.L., Diefenbach, R.J. J. Virol. (2005) [Pubmed]
  22. Marek's disease virus (MDV) homologues of herpes simplex virus type 1 UL49 (VP22) and UL48 (VP16) genes: high-level expression and characterization of MDV-1 VP22 and VP16. Dorange, F., El Mehdaoui, S., Pichon, C., Coursaget, P., Vautherot, J.F. J. Gen. Virol. (2000) [Pubmed]
  23. The product of the US10 gene of herpes simplex virus type 1 is a capsid/tegument-associated phosphoprotein which copurifies with the nuclear matrix. Yamada, H., Daikoku, T., Yamashita, Y., Jiang, Y.M., Tsurumi, T., Nishiyama, Y. J. Gen. Virol. (1997) [Pubmed]
  24. The herpes simplex virus type 1 UL37 gene product is a component of virus particles. McLauchlan, J., Liefkens, K., Stow, N.D. J. Gen. Virol. (1994) [Pubmed]
  25. Capsid structure of simian cytomegalovirus from cryoelectron microscopy: evidence for tegument attachment sites. Trus, B.L., Gibson, W., Cheng, N., Steven, A.C. J. Virol. (1999) [Pubmed]
  26. Evidence for Intercellular Trafficking of VP22 in Living Cells. Lemken, M.L., Wolf, C., Wybranietz, W.A., Schmidt, U., Smirnow, I., Bühring, H.J., Mack, A.F., Lauer, U.M., Bitzer, M. Mol. Ther. (2007) [Pubmed]
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