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- W3036693814 abstract "Herpes viruses cause numerous human diseases. Herpes Simplex viruses (HSV1 and HSV2), varicella zoster virus (VSV),cytomegalovirus (CMV), and Epstein-Barr Virus (EBV) cause conditions ranging from peripheral sores (HSV, VSV), generalized viremia (CMV) and recurrent malaise (EBV). The common targets for HSV are neurons in the CNS, peripheral nerve cells or plexuses of sensory ganglia in highly innervated epithelium (e.g. lips, genitals). Interfering with the mechanisms of infection and virus production depends on the ability to target specific stages of viral reproduction. Helicases are enzymes that are essential for the duplication of viral DNA. The origin binding protein (OBP) helicase (encoded by the DNA replication gene UL9 ) binds to sequences in DNA at the three replication origins. These origins are points within the HSV chromosome where DNA replication initiates. The protein is a 83kDa polypeptide which exists as a dimer. Although the role of the UL9 helicase in HSV DNA replication has not been exactly determined, by analogy to other eukaryotic origin binding replication proteins, the binding and enzymatic action of the UL9 helicase to the origin sequences may initiate the assembly of a multiprotein replication complex. Helicase-primase (the product of the DNA replication genes UL5 . UL8 and UL52 ) acts to unwind double-stranded DNA at growing replication forks. The helicaseprimase activity is expressed by a 213kDa heterodimer consisting of the 99kDa UL5 and 114kDA UL52 subunits. ICP8 (SSB—UL29 gene product) is a single-stranded binding protein of 122kDa that complexes with OBP (two SSB/OBP dimer). Each of these gene products has been expressed in insect cells with a recombinant baculovirus and purified to near homogeneity. Assays have been established for the screening of compounds that could inhibit the helicase activity of HSV 1 helicases. Analysis of helicase/DNA substrate complexes under different conditions will be facilitated by a better understanding of the structure of the individual proteins." @default.
- W3036693814 created "2020-06-25" @default.
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- W3036693814 date "1996-08-11" @default.
- W3036693814 modified "2023-09-25" @default.
- W3036693814 title "High resolution rotary shadowing of herpes simplex virus helicase proteins" @default.
- W3036693814 doi "https://doi.org/10.1017/s0424820100162788" @default.
- W3036693814 hasPublicationYear "1996" @default.
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