Skip to main content
Log in

HSV-2 ICP34.5 protein modulates herpes simplex virus glycoprotein processing

  • Brief Report
  • Published:
Archives of Virology Aims and scope Submit manuscript

Abstract

The ICP34.5 gene from HSV-2 strain 333 was cloned and, when expressed in Vero cells, enhanced the efficiency and extent of glycoprotein processing of glycoprotein C (gC1), a representative viral glycoprotein, during infection with HSV-1 SP7. The ICP34.5 from HSV-1 SP7 limits the extent and efficiency of viral glycoprotein processing. The ability of the HSV-2 ICP34.5 protein to enhance the efficiency and extent of HSV-1 SP7 glycoprotein processing indicates that modulation of viral glycoprotein processing is also a property of the HSV-2 ICP34.5 protein.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1

References

  1. Brown SM, Harland J, MacLean AR, Podlech J, Clements JB (1994) Cell type and cell state determine differential in vivo growth of non-neurovirulent ICP34.5-negative herpes simplex virus types 1 and 2. J Gen Virol 75:2367–2377

    Article  PubMed  CAS  Google Scholar 

  2. Chou J, Roizman B (1994) Differential response of human cells to deletions and stop codons in the gamma 1 34.5 gene of herpes simplex virus. J Virol 68(12):8304–8311

    PubMed  CAS  Google Scholar 

  3. Chou J, Roizman B (1992) The Gamma 1 34.5 gene of herpes simplex virus 1 precludes neuroblastoma cells from triggering total shutoff of protein synthesis characteristic of programed cell death in neuronal cells. PNAS 89(8):3266–3270

    Article  PubMed  CAS  Google Scholar 

  4. Orvedahl A, Alexander D, Talloczy Z, Sun Q, Wei Y, Wei Z, Burns D, Leib DA, Levine B (2007) HSV-1 ICP34.5 confers neurovirulence by targeting the beclin 1 autophagy protein. Cell Host Microbe 1:23–35

    Article  PubMed  CAS  Google Scholar 

  5. Bower JR, Mao H, Durishin C, Rozenbom E, Detwiler M, Rempinski D, Karban TL, Rosenthal KS (1999) Intrastrain variants of herpes simplex virus type 1 isolated from a neonate with fatal disseminated infection differ in the ICP34.5 gene, glycoprotein processing, and neuroinvasive disease. J Virol 73(5):3843–3853

    PubMed  CAS  Google Scholar 

  6. Mao H, Rosenthal KS (2003) Strain-dependent structural variants of herpes simplex virus type 1 ICP34.5 determine viral plaque size, efficiency of glycoprotein processing, and viral release and neuroinvasive disease potential. J Virol 77(6):3409–3417

    Article  PubMed  CAS  Google Scholar 

  7. Chou J, Roizman B (1986) The terminal a sequence of the herpes simplex virus genome contains the promoter of a gene located in the repeat sequences of the l component. J Virol 57(2):629–637

    PubMed  CAS  Google Scholar 

  8. He B, Gross M, Roizman B (1998) The gamma-1 34.5 protein of herpes simplex virus has the structural and functional attributes of a protein phosphatase 1 regulatory subunit and is present in high molecular weight complex with the enzyme in infected cells. J Biol Chem 273:20737–20743

    Article  PubMed  CAS  Google Scholar 

  9. He B, Gross M, Roizman B (1997) The gamma 1 34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1 alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. PNAS 94:843–848

    Article  PubMed  CAS  Google Scholar 

  10. Verpooten D, Ma Y, Hou S, Yan Z, He B (2009) Control of TANK binding kinase 1 mediated signaling by the gamma-1 34.5 protein of herpes simplex virus 1. J Biol Chem 284:1097–1105. http://www.jbc.org/cgl/doi/10.107/jbc.M805905200

    Article  PubMed  CAS  Google Scholar 

  11. Dolan A, Jamieson FE, Cunningham C, Barnett BC, McGeoch DJ (1998) The genome sequence of herpes simplex virus type 2. J Virol 72(3):2010–2021

    PubMed  CAS  Google Scholar 

  12. Tirabassi RS, Enquist LW (2000) Role of the pseudorabies virus gI cytoplasmic domain in neuroinvasion, virulence, and posttranslational N-linked glycosylation. J Virol 74(8):3505–3516

    Article  PubMed  CAS  Google Scholar 

  13. Tirabassi RS, Townley RA, Eldridge MG, Enquist LW (1997) Characterization of pseudorabies virus mutants expressing carboxy-terminal truncations of gE: evidence for envelope incorporation, virulence, and neurotropism domains. J Virol 71(9):6455–6464

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Kenneth Steven Rosenthal.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Chatterjee, S., Wang, J.W., Cismowski, M.J. et al. HSV-2 ICP34.5 protein modulates herpes simplex virus glycoprotein processing. Arch Virol 154, 661–663 (2009). https://doi.org/10.1007/s00705-009-0341-9

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00705-009-0341-9

Keywords

Navigation