Skip to main content Accessibility help
×
Hostname: page-component-77c89778f8-swr86 Total loading time: 0 Render date: 2024-07-18T23:38:06.206Z Has data issue: false hasContentIssue false

10 - Alphaherpesvirus DNA replication

from Part II - Basic virology and viral gene effects on host cell functions: alphaherpesviruses

Published online by Cambridge University Press:  24 December 2009

John Hay
Affiliation:
Witebsky Center for Microbial Pathogenesis and Immunology, SUNY at Buffalo School of Medicine, NY, USA
William T. Ruyechan
Affiliation:
Witebsky Center for Microbial Pathogenesis and Immunology, SUNY at Buffalo School of Medicine, NY, USA
Ann Arvin
Affiliation:
Stanford University, California
Gabriella Campadelli-Fiume
Affiliation:
Università degli Studi, Bologna, Italy
Edward Mocarski
Affiliation:
Emory University, Atlanta
Patrick S. Moore
Affiliation:
University of Pittsburgh
Bernard Roizman
Affiliation:
University of Chicago
Richard Whitley
Affiliation:
University of Alabama, Birmingham
Koichi Yamanishi
Affiliation:
University of Osaka, Japan
Get access

Summary

DNA replication in alphaherpesviruses has been the subject of study in bursts over the years. Interest in the subject depends not just on simple curiosity about this central feature of the viral growth cycle, but also because DNA replication is a potentially useful target for antiviral therapy, as has already been shown with agents such as acyclovir. The viral contributions to the mechanism of genome replication are quite well understood but we still are unable to duplicate the in vivo situation in an in vitro assay. Much of the recent interesting work involves the host cell's contribution to the process, and this seems likely to remain a focus for the future.

Structure of the genome

There are over 30 alphaherpesviruses that infect a wide range of host species. Their genomes fall into two general categories, either herpes simplex (HSV) – like or varicella zoster (VZV) – like, with four or two, respectively, isomeric forms (Fig. 10.1). There is a wide range of G + C content (32%–75%), with a bias towards higher (>50%) numbers. There is also size heterogeneity (125–180 kbp) which, although quantitatively less than the nucleotide composition variation, may be much more significant for the lifestyle of the virus. All alphaherpesvirus genomes contain four general structural components: unique long and short (UL, US) sequences that encode single-copy genes and inverted repeat regions that bound the unique regions; these may contain diploid genes and sequences required for cleavage and packaging of viral DNA (Fig. 10.1).

Type
Chapter
Information
Human Herpesviruses
Biology, Therapy, and Immunoprophylaxis
, pp. 138 - 143
Publisher: Cambridge University Press
Print publication year: 2007

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Baker, R. O., Murata, L. B., Dodson, M. S., and Hall, J. D. (2000). Purification and characterization of OF-1, a host factor implicated in herpes simplex replication. J. Biol. Chem., 275, 30050–30057.CrossRefGoogle ScholarPubMed
Balliet, J. W., Min, J. C., Cabatingan, M. S., and Schaffer, P. A. (2005). Site-directed mutagenesis of large DNA palindromes: construction and in vitro characterization of herpes simplex virus type 1 mutants containing point mutations that eliminate the oriL or oriS function. J. Virol., 79, 12783–12797.CrossRefGoogle ScholarPubMed
Barrera, I., Bloom, D., and Challberg, M. (1998). An intertypic herpes simplex virus helicase–primase complex associated with a defect in neurovirulence has reduced primase activity. J. Virol., 72, 1203–1209.Google ScholarPubMed
Bell, P., Lieberman, P. M., and Maul, G. G. (2000). Lytic but not latent replication of Epstein–Barr virus is associated with PML and induces sequential release of nuclear domain 10 proteins. J. Virol., 74, 11800–11810.CrossRefGoogle Scholar
Biswas, N. and Weller, S. K. (2001). The UL5 and UL52 subunits of the herpes simplex virus type 1 helicase–primase subcomplex exhibit a complex interdependence for DNA binding. J. Biol. Chem., 276, 17610–17619.CrossRefGoogle ScholarPubMed
Boehmer, P. E. and Lehman, I. R. (1997). Herpes simplex virus DNA replication. Ann. Rev. Biochem., 66, 147–184.CrossRefGoogle ScholarPubMed
Bridges, K. G., Hua, Q., Brigham-Burke, M. R.et al. (2000). Secondary structure and structure–activity relationships of peptides corresponding to the subunit interface of herpes simplex virus DNA polymerase. J. Biol. Chem., 275, 472–478.CrossRefGoogle ScholarPubMed
Carrington-Lawrence, S. D., and Weller, S. K. (2003). Recruitment of polymerase to herpes simplex virus type 1 replication foci in cells expressing mutant primase (UL52) proteins. J. Virol., 77, 4237–4247.CrossRefGoogle Scholar
Chaudhuri, M., Song, L., and Parris, D. S. (2003) The herpes simplex virus type 1 DNA polymerase processivity factor increases fidelity without altering pre-steady-state rate constants for polymerization or excision. J. Biol. Chem., 278, 8996–9004.CrossRefGoogle ScholarPubMed
Chen, X. P., Mata, M., Kelley, M., Glorioso, J. C., and Fink, D. J. (2002) The relationship of herpes simplex virus latency associated transcript expression to genome copy number: a quantitative study using laser capture microdissection. J. Neurovirol., 8, 204–210.CrossRefGoogle ScholarPubMed
Crute, J. J., Grygon, C. A., Hargarce, K. D.et al. (2002). Herpes simplex virus helicase-primase inhibitors are active in animal models of human disease. Nature Med., 8, 386–391.CrossRefGoogle ScholarPubMed
Falkenberg, M., Lehman, I. R., and Elias, P. (2000). Leading and lagging strand DNA synthesis in vitro by a reconstituted herpes simplex virus type 1 replisome. Proc. Natl Acad. Sci. USA, 97, 3896–3900.CrossRefGoogle ScholarPubMed
Griffiths, A., Chen, S. H., Horsburgh, B. C., and Coen, D. M. (2003). Translational compensation of a frameshift mutation affecting herpes simplex virus thymidine kinase is sufficient to permit reactivation from latency. J. Virol., 77, 4703–4709.CrossRefGoogle ScholarPubMed
Hayashi, K., Hayashi, T., Sun, H. D., and Takeda, Y. (2002). Contribution of a combination of ponicidin and acyclovir/ganciclovir to the antitumor afficacy of the herpes simplex virus thymidine kinase gene therapy system. Hum. Gene Therapy, 13, 415–423.CrossRefGoogle Scholar
Hodge, P. D. and Stow, N. D. (2001). Effects of mutations within the herpes simplex virus type 1 DNA encapsidation signal on packaging efficiency. J. Virol., 65, 8977–8986.CrossRefGoogle Scholar
Hsiang, C. Y. (2002). Pseudorabies virus DNA-binding protein stimulates the exonuclease activity and regulates the processivity of pseudorabies virus DNase. Biochem. Biophys. Res. Commun., 293, 1301–1308.CrossRefGoogle ScholarPubMed
Huang, K. J., Zemelman, B. V., and Lehman, I. R. (2002). Endonuclease G, a candidate human enzyme for the initiation of genomic inversion in herpes simplex type 1 virus. J. Biol. Chem., 277, 21071–21079.CrossRefGoogle ScholarPubMed
Ishov, A. M. and Maul, G. G. (1996). The periphery of nuclear domain 10 (ND10) as a site of DNA virus deposition. J. Cell Biol., 134, 815–826.CrossRefGoogle ScholarPubMed
Komatsu, T., Ballestas, M. E., Barbera, A. J., Kelly-Clarke, B., and Kaye, K. M. (2004). KSHV LANA-1 binds DNA as an oligomer and residues N-terminal to the oligomerization domain are essential for DNA binding, replication and episome persistence. Virology, 319, 225–236.CrossRefGoogle Scholar
Kristie, T. M., Vogel, J. L., and Sears, A. (1999). Nuclear localization of the C1 factor (host cell factor) in sensory neurons correlates with reactivation of herpes simplex virus from latency. Proc. Natl Acad. Sci, USA, 96, 1229–1233.CrossRefGoogle ScholarPubMed
Kuperschmidt, S., DeMarchi, J. M., Lu, Z., and Ben-Porat, T. (1991). Analysis of an origin of DNA replication located at the L terminus of the genome of pseudorabies virus. J. Virol., 65, 6283–6291.Google Scholar
Langelier, Y., Champoux, L., Hamel, M.et al. (1998). The R1 subunit of herpes simplex virus ribonucleotide reductase is a good substrate for host cell protein kinases but is not itself a protein kinase. J. Biol. Chem., 273, 1435–1443.CrossRefGoogle Scholar
Lehman, I. R. and Boehmer, P. E. (1999). Replication of herpes simplex virus DNA. J. Biol. Chem., 274, 28059–28062.CrossRefGoogle ScholarPubMed
Lomonte, P. and Everett, R. (1999). Herpes simplex virus type 1 immediate early protein Vmw 110 inhibits progression of cells through mitosis and from G(1) into S phase of the cell cycle. J. Virol., 73, 9456–9467.Google Scholar
Murata, L. B., Dodson, M. S., and Hall, J. D. (2004). A human cellular protein activity (OF-1), which binds herpes simplex type 1 origins, contains the Ku70/Ku80 heterodimer. J. Virol., 78, 7839–7842.CrossRefGoogle Scholar
Nimonkar, A. V. and Boehman, P. E. (2003). The herpess implex virus type 1 single-strand DNA-binding protein (ICP8) promotes strand invasion. J. Biol. Chem., 278, 9678–9682.CrossRefGoogle Scholar
Quinlan, M. P., Chen, L. B., and Knipe, D. M. (1984). The intranuclear location of a herpes simplex virus DNA-binding protein is determined by the status of viral DNA replication. Cell, 36, 857–868.CrossRefGoogle ScholarPubMed
Randell, J. C. and Coen, D. M. (2001). Linear diffusion on DNA despite high-affinity binding by a DNA polymerase processivity factor. Mol. Cell, 8, 911–920.CrossRefGoogle ScholarPubMed
Reuven, N. B., Staire, A. E., Myers, R. S., and Weller, S. K. (2003). The herpes simplex virus type 1 alkaline nuclease and single stranded DNA binding protein mediate strand exchange in vitro. J. Virol., 77, 7425–7433.CrossRefGoogle ScholarPubMed
Roizman, B. and Knipe D. (2001). Herpes simplex viruses and their replication. In Fields Virology, ed. Knipe, D. M. and Howley, P. M., pp. 2399–2459. Philadelphia, PA: Lippincott, Williams and Wilkins.Google Scholar
Schang, L. M., Rosenberg, A., and Schaffer, P. A. (2000). Roscovitine, a specific inhibitor of cellular cyclin-dependent kinases inhibits herpes simplex virus DNA synthesis in the presence of viral early proteins. J. Virol., 74, 2107–2120.CrossRefGoogle ScholarPubMed
Song, B., Yeh, K. C., Liu, J., and Knipe, D. M. (2001). Herpes simplex virus gene products required for viral inhibition of expression of G1-phase functions. Virology, 290, 320–328.CrossRefGoogle ScholarPubMed
Sourvinos, G. and Everett, R. D. (2002). Visualization of parental HSV-1 genomes and replication compartments in association with ND10 in live infected cells. EMBO J., 21, 4989–4997.CrossRefGoogle ScholarPubMed
, Stow N. D. and , Davison A. J. (1986). Identification of a varicella-zoster virus origin of DNA replication and its activation by herpes simplex virus type 1 gene products. J. Gen. Virol., 67, 1613–1623.CrossRefGoogle Scholar
Sulpizi, M., Schelling, P., Folkers, G.Carloni, P., and Scapozza, L. (2001). The rationale of catalytic activity of herpes simplex virus thymidine kinase: a combined biochemical and quantum chemical study. J. Biol. Chem., 276, 21692–21697.CrossRefGoogle Scholar
Taylor, T. J. and Knipe, D. M. (2003). C-terminal region of herpes simplex virus ICP8 protein needed for intranuclear localization. Virology, 309, 219–231.CrossRefGoogle ScholarPubMed
Telford, E. A. R., Watson, M. S., McBride, K., and Davison, A. (1992). The DNA sequence of equine herpesvirus-1. Virology, 189, 304–316.CrossRefGoogle ScholarPubMed
Thornton, K. E., Chaudhuri, M., Monahan, S. J., Grinstead, L. A., and Parris, D. S. (2000). Analysis of in vitro activities of herpes simplex virus type 1 UL42 mutant proteins: correlation with in vivo function. Virology, 275, 373–390.CrossRefGoogle ScholarPubMed
White, C. A., Stow, N. D., Patel, A. H., Hughes, M., and Preston, V. G. (2003). Herpes simplex virus type 1 portal protein UL6 interacts with the putative terminase subunits UL15 and UL28. J. Virol., 77, 6351–6358.CrossRefGoogle ScholarPubMed
Zuccola, H. J., Filman, D. J., Coen, D. M., and Hogle, J. M. (2000). The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase. Mol. Cell, 5, 267–278.CrossRefGoogle Scholar

Save book to Kindle

To save this book to your Kindle, first ensure coreplatform@cambridge.org is added to your Approved Personal Document E-mail List under your Personal Document Settings on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part of your Kindle email address below. Find out more about saving to your Kindle.

Note you can select to save to either the @free.kindle.com or @kindle.com variations. ‘@free.kindle.com’ emails are free but can only be saved to your device when it is connected to wi-fi. ‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.

Find out more about the Kindle Personal Document Service.

Available formats
×

Save book to Dropbox

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Dropbox.

Available formats
×

Save book to Google Drive

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Google Drive.

Available formats
×