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Gene Review

UL46  -  modulates transactivating tegument protein...

Human herpesvirus 1

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Disease relevance of UL46

  • The gene products of herpes simplex virus type 1 UL46 and UL47 enhance the efficiency of alpha TIF (VP16)-mediated alpha gene expression through an unknown mechanism of action [1].
  • Purified virions were found to contain approximately 700 copies of the UL11 protein per particle, making it an abundant component of the tegument [2].
  • Herpes simplex virus type 1 (HSV-1) was labeled by the fusion of the green fluorescent protein to a structural protein of its tegument (VP11/12), the product of gene UL46 [3].
  • Current evidence suggests that viral glycoprotein tails play a role in the recruitment of tegument-coated capsids to the site of final envelopment; vesicles derived from the trans-Golgi network [4].
  • 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 [5].

High impact information on UL46

  • Of the three tegument proteins that package mRNA in herpes simplex virions, one (VP22) transports the mRNA to uninfected cells for expression prior to viral infection [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].
  • 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 [8].
  • Identification of a 709-Amino-Acid Internal Nonessential Region within the Essential Conserved Tegument Protein (p)UL36 of Pseudorabies Virus [9].
  • The interaction of UL46-UL48 was verified using an in vitro pull-down assay [10].

Chemical compound and disease context of UL46

  • 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 UL46


Anatomical context of UL46


Associations of UL46 with chemical compounds

  • We have identified an interaction between VP22, an abundant tegument protein and the cytoplasmic tail of glycoprotein E (gE) [4].

Other interactions of UL46


Analytical, diagnostic and therapeutic context of UL46

  • ETIF was localized to the viral tegument in Western blot assays of EHV-1 virions and subvirion fractions using polyclonal antiserum and monoclonal antibodies generated against a glutathione-S-transferase-ETIF fusion protein [15].
  • The intercellular trafficking property of the herpes simplex virus type 1 tegument protein VP22 makes it a promising tool for overcoming low transduction efficiencies in gene therapy [21].


  1. Herpes simplex virus type 1 UL46 and UL47 deletion mutants lack VP11 and VP12 or VP13 and VP14, respectively, and exhibit altered viral thymidine kinase expression. Zhang, Y., McKnight, J.L. J. Virol. (1993) [Pubmed]
  2. 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]
  3. Rapid directional translocations in virus replication. Willard, M. J. Virol. (2002) [Pubmed]
  4. 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]
  5. Egress of alphaherpesviruses: comparative ultrastructural study. Granzow, H., Klupp, B.G., Fuchs, W., Veits, J., Osterrieder, N., Mettenleiter, T.C. J. Virol. (2001) [Pubmed]
  6. Of the three tegument proteins that package mRNA in herpes simplex virions, one (VP22) transports the mRNA to uninfected cells for expression prior to viral infection. Sciortino, M.T., Taddeo, B., Poon, A.P., Mastino, A., Roizman, B. Proc. Natl. Acad. Sci. U.S.A. (2002) [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. 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]
  9. 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]
  10. 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]
  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. 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]
  14. 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]
  15. Structural and antigenic identification of the ORF12 protein (alpha TIF) of equine herpesvirus 1. Lewis, J.B., Thompson, Y.G., Feng, X., Holden, V.R., O'Callaghan, D., Caughman, G.B. Virology (1997) [Pubmed]
  16. 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]
  17. 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]
  18. 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]
  19. Intraocular T cells of patients with herpes simplex virus (HSV)-induced acute retinal necrosis recognize HSV tegument proteins VP11/12 and VP13/14. Verjans, G.M., Dings, M.E., McLauchlan, J., van Der Kooi, A., Hoogerhout, P., Brugghe, H.F., Timmermans, H.A., Baarsma, G.S., Osterhaus, A.D. J. Infect. Dis. (2000) [Pubmed]
  20. Differences in the intracellular localization and fate of herpes simplex virus tegument proteins early in the infection of Vero cells. Morrison, E.E., Stevenson, A.J., Wang, Y.F., Meredith, D.M. J. Gen. Virol. (1998) [Pubmed]
  21. 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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