Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • News & Views
  • Published:

New anti-HSV therapeutics target the helicase–primase complex

The only targets for clinical treatment of herpes simplex virus infections have been the viral enzymes thymidine kinase and DNA polymerase. Now, animal experiments show the healing benefits of new antiherpes drugs that act on the viral helicase–primase complex and appear superior to the standard treatment, acyclovir.

This is a preview of subscription content, access via your institution

Relevant articles

Open Access articles citing this article.

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Mechanism of DNA synthesis inhibition by acyclovir and the new drugs (modified from Boehmer and Lehman11).

Renee Lucas

References

  1. Elion, G.B. et al. Selectivity of action of an antiherpectic agent 9-(hydroxyethoxymethyl) guanine. Proc. Natl. Acad. Sci. USA 74, 5716–5720 (1977).

    Article  CAS  Google Scholar 

  2. Crute, J.J. et al. Herpes simplex virus helicase–primase inhibitors are active in animal models of human disease. Nature Med. 8, 386–391 (2002).

    Article  CAS  Google Scholar 

  3. Kleymann, G. et al. New helicase–primase inhibitors as drug candidates for the treatment of herpes simplex disease. Nature Med. 8, 392–398 (2002).

    Article  CAS  Google Scholar 

  4. Coen, D. & Schaffer, P. Two distinct loci confer resistance to acycloguanosine in herpes simplex virus type 1. Proc. Natl. Acad. Sci. USA 77, 2265–2269 (1980).

    Article  CAS  Google Scholar 

  5. Schnipper, L.E. & Crumpacker, C.S. Resistance of herpes simplex virus to acycloguanosine: The role of viral thymidine kinase and DNA polymerase loci. Proc. Natl. Acad. Sci. USA 77, 2270–2273 (1980).

    Article  CAS  Google Scholar 

  6. Furman, P.A. et al. Inhibition of herpes simplex virus induced DNA polymerase activity and viral DNA replication by 9-(2-hydroxyehoxymethyl) guanine and its triphosphate. J. Virol. 32, 72–77 (1979).

    CAS  PubMed  PubMed Central  Google Scholar 

  7. Safrin, S. et al. Treatment of acyclovir-resistant mucocutaneous herpes simplex infection in patients with the acquired immunodeficiency syndrome. A randomized multicenter study of foscarnet vs. vidarabrine. New Engl. J. Med. 325, 551–555 (1991)

    Article  CAS  Google Scholar 

  8. Crute, J.J. & Lehman, I.R. Herpes simplex virus helicase primase. Physical and catalytic properties. J. Biol. Chem. 266, 4484–4488 (1991).

    CAS  PubMed  Google Scholar 

  9. Zhu, L.A. & Weller, S.K. The UL5 gene of herpes simplex virus type 1: Isolation of a lac Z insertion mutant and association of the UL5 gene product with other members of the helicase-primase complex. J. Virol. 66, 1458–1468 (1992).

    Google Scholar 

  10. Spector, F.C., Liang, L., Giordano, H., Sivaraja, M. & Peterson, M.G. Inhibition of herpes simplex virus replication by a 2-amino-thiazole via interactions with the helicase component of the UL5-UL8-UL52 complex. J. Virol. 72, 6979–6987 (1998).

    CAS  PubMed  PubMed Central  Google Scholar 

  11. Boehmer, P.E. & Lehman, I.R. Herpes simplex virus DNA replication. Annu. Rev. Biochem. 66, 347–384 (1997).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Crumpacker, C., Schaffer, P. New anti-HSV therapeutics target the helicase–primase complex. Nat Med 8, 327–328 (2002). https://doi.org/10.1038/nm0402-327

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/nm0402-327

This article is cited by

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing