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.
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Short hairpin-loop-structured oligodeoxynucleotides reduce HSV-1 replication
Virology Journal Open Access 27 April 2009
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References
Elion, G.B. et al. Selectivity of action of an antiherpectic agent 9-(hydroxyethoxymethyl) guanine. Proc. Natl. Acad. Sci. USA 74, 5716–5720 (1977).
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).
Kleymann, G. et al. New helicase–primase inhibitors as drug candidates for the treatment of herpes simplex disease. Nature Med. 8, 392–398 (2002).
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).
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).
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).
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)
Crute, J.J. & Lehman, I.R. Herpes simplex virus helicase primase. Physical and catalytic properties. J. Biol. Chem. 266, 4484–4488 (1991).
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).
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).
Boehmer, P.E. & Lehman, I.R. Herpes simplex virus DNA replication. Annu. Rev. Biochem. 66, 347–384 (1997).
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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
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DOI: https://doi.org/10.1038/nm0402-327
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