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Gene Review

US9  -  type 2 membrane protein; tegument...

Human herpesvirus 1

 
 
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Disease relevance of US9

  • Herpes simplex virus type 1 glycoprotein e is required for axonal localization of capsid, tegument, and membrane glycoproteins [1].
  • Their ability to deliver functional proteins into cells was compared to that of virions by testing the biological activities of two tegument proteins which are present in both types of particle [2].
  • L-particles are noninfectious virion-related particles that lack the nucleocapsid but do contain tegument and envelope [2].
  • The ORF 3 encoded a predicted protein of 601 aa (M(r) 67.5 kDa) which exhibited limited homology (18% overall identity) with the UL47 protein (major tegument protein) of HSV-1 [3].
  • Particularly striking was the addition of a large amount of tegument material to ILTV capsids in the cytoplasm [4].
 

High impact information on US9

  • 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 [5].
  • 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 [6].
  • It is required, however, for RNA degradation activity of tegument-derived vhs and wild-type replication and virulence in mice [7].
  • Herpes simplex virus tegument protein VP22 contains overlapping domains for cytoplasmic localization, microtubule interaction, and chromatin binding [8].
  • 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 [4].
 

Chemical compound and disease context of US9

  • 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 [9].
  • 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 [10].
 

Biological context of US9

  • The only polypeptide known to map entirely within the HSV genome region defined by pMC1 was identified as the major tegument species Vmw65 [11].
  • The equine herpesvirus 1 (EHV-1) homolog of the herpes simplex virus type 1 (HSV-1) tegument phosphoprotein, alpha TIF (Vmw65; VP16), was identified previously as the product of open reading frame 12 (ORF12) and shown to transactivate immediate early (IE) gene promoters [12].
  • Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument [13].
  • Furthermore, MDV ICP27 upstream sequences contain four copies of consensus sequence elements similar to the tegument protein target sequence TAATGARAT [14].
  • To confirm more directly that NA induces apoptosis, the NA of clone 7a and A/Fiji was expressed fused to the Herpes simplex virus tegument coat protein VP22, transfected into HeLa cells and the level of apoptosis determined [15].
 

Anatomical context of US9

  • After contact of infectious virus with the cell plasma membrane, discernible changes of the envelope and tegument could be seen by electron microscopy [16].
  • 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 [17].
  • Differences in the intracellular localization and fate of herpes simplex virus tegument proteins early in the infection of Vero cells [18].
  • Immunolocalization studies on purified virions indicate that the antigen can be detected only in virions without membranes, and is located outside the capsid, most probably in the tegument [19].
  • 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 [20].
 

Associations of US9 with chemical compounds

  • We have identified an interaction between VP22, an abundant tegument protein and the cytoplasmic tail of glycoprotein E (gE) [9].
 

Analytical, diagnostic and therapeutic context of US9

  • 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 [12].
  • 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].

References

  1. Herpes simplex virus type 1 glycoprotein e is required for axonal localization of capsid, tegument, and membrane glycoproteins. Wang, F., Tang, W., McGraw, H.M., Bennett, J., Enquist, L.W., Friedman, H.M. J. Virol. (2005) [Pubmed]
  2. Noninfectious L-particles supply functions which can facilitate infection by HSV-1. McLauchlan, J., Addison, C., Craigie, M.C., Rixon, F.J. Virology (1992) [Pubmed]
  3. Nucleotide sequence analysis of an infectious laryngotracheitis virus gene corresponding to the US3 of HSV-1 and a unique gene encoding a 67 kDa protein. Kongsuwan, K., Prideaux, C.T., Johnson, M.A., Sheppard, M., Rhodes, S. Arch. Virol. (1995) [Pubmed]
  4. Egress of alphaherpesviruses: comparative ultrastructural study. Granzow, H., Klupp, B.G., Fuchs, W., Veits, J., Osterrieder, N., Mettenleiter, T.C. J. Virol. (2001) [Pubmed]
  5. 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]
  6. 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]
  7. Role of the VP16-binding domain of vhs in viral growth, host shutoff activity, and pathogenesis. Strand, S.S., Leib, D.A. J. Virol. (2004) [Pubmed]
  8. Herpes simplex virus tegument protein VP22 contains overlapping domains for cytoplasmic localization, microtubule interaction, and chromatin binding. Martin, A., O'Hare, P., McLauchlan, J., Elliott, G. J. Virol. (2002) [Pubmed]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. Identification and characterization of Marek's disease virus genes homologous to ICP27 and glycoprotein K of herpes simplex virus-1. Ren, D., Lee, L.F., Coussens, P.M. Virology (1994) [Pubmed]
  15. Exploitation of the Herpes simplex virus translocating protein VP22 to carry influenza virus proteins into cells for studies of apoptosis: direct confirmation that neuraminidase induces apoptosis and indications that other proteins may have a role. Morris, S.J., Smith, H., Sweet, C. Arch. Virol. (2002) [Pubmed]
  16. 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]
  17. 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]
  18. 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]
  19. A 165 kd protein of the herpes simplex virion shares a common epitope with the regulatory protein, ICP4. Bibor-Hardy, V., Sakr, F. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
  20. 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]
  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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