This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jiang, C.
Right arrow Articles by Hwang, C. B. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jiang, C.
Right arrow Articles by Hwang, C. B. C.

 Previous Article  |  Next Article 

Journal of Virology, November 2007, p. 12077-12079, Vol. 81, No. 21
0022-538X/07/$08.00+0     doi:10.1128/JVI.01133-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Herpes Simplex Virus Mutants with Multiple Substitutions Affecting DNA Binding of UL42 Are Impaired for Viral Replication and DNA Synthesis{triangledown}

Changying Jiang,1 Ying T. Hwang,1 Guangliang Wang,1 John C. W. Randell,2,{dagger} Donald M. Coen,2 and Charles B. C. Hwang1*

Department of Microbiology and Immunology, State University of New York Upstate Medical University, Syracuse, New York 13210,1 Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 021152

Received 24 May 2007/ Accepted 13 August 2007

Herpes simplex virus mutants with single substitutions that decrease DNA binding by the DNA polymerase processivity subunit UL42 are only modestly impaired for viral replication. In this study, recombinant viruses harboring two or four of these mutations were constructed. The more substitutions, the more severe the defects in viral replication and DNA synthesis, suggesting that DNA binding by UL42 is important for these processes.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, State University of New York Upstate Medical University, Syracuse, NY 13210. Phone: (315) 464-8739. Fax: (315) 464-4417. E-mail: hwangc{at}upstate.edu

{triangledown} Published ahead of print on 22 August 2007.

{dagger} Present address: Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.

Journal of Virology, November 2007, p. 12077-12079, Vol. 81, No. 21
0022-538X/07/$08.00+0     doi:10.1128/JVI.01133-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Alvisi, G., Roth, D. M., Camozzi, D., Pari, G. S., Loregian, A., Ripalti, A., Jans, D. A. (2009). The Flexible Loop of the Human Cytomegalovirus DNA Polymerase Processivity Factor ppUL44 Is Required for Efficient DNA Binding and Replication in Cells. J. Virol. 83: 9567-9576 [Abstract] [Full Text]  
  • Jiang, C., Komazin-Meredith, G., Tian, W., Coen, D. M., Hwang, C. B. C. (2009). Mutations That Increase DNA Binding by the Processivity Factor of Herpes Simplex Virus Affect Virus Production and DNA Replication Fidelity. J. Virol. 83: 7573-7580 [Abstract] [Full Text]  
  • Sinigalia, E., Alvisi, G., Mercorelli, B., Coen, D. M., Pari, G. S., Jans, D. A., Ripalti, A., Palu, G., Loregian, A. (2008). Role of Homodimerization of Human Cytomegalovirus DNA Polymerase Accessory Protein UL44 in Origin-Dependent DNA Replication in Cells. J. Virol. 82: 12574-12579 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»