Skip Navigation



Nucleic Acids Research Advance Access published online on November 26, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn938
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (7978K) Freely available
Right arrow Screen PDF (748K) Freely available
Right arrow Supplementary Data
Right arrowOA All Versions of this Article:
37/1/243    most recent
gkn938v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Valkov, E.
Right arrow Articles by Cherepanov, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Valkov, E.
Right arrow Articles by Cherepanov, P.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

Functional and structural characterization of the integrase from the prototype foamy virus

Eugene Valkov1, Saumya Shree Gupta1, Stephen Hare1, Anna Helander1, Pietro Roversi2, Myra McClure1 and Peter Cherepanov1,*

1Division of Medicine, St. Mary's Campus, Imperial College London, Norfolk Place, London, W2 1PG and 2Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK

*To whom correspondence should be addressed. Tel: +44 20 75943655; Fax: +44 20 75943906; Email: p.cherepanov{at}imperial.ac.uk

Received October 7, 2008. Revised November 4, 2008. Accepted November 5, 2008.

Establishment of the stable provirus is an essential step in retroviral replication, orchestrated by integrase (IN), a virus-derived enzyme. Until now, available structural information was limited to the INs of human immunodeficiency virus type 1 (HIV-1), avian sarcoma virus (ASV) and their close orthologs from the Lentivirus and Alpharetrovirus genera. Here, we characterized the in vitro activity of the prototype foamy virus (PFV) IN from the Spumavirus genus and determined the three-dimensional structure of its catalytic core domain (CCD). Recombinant PFV IN displayed robust and almost exclusively concerted integration activity in vitro utilizing donor DNA substrates as short as 16 bp, underscoring its significance as a model for detailed structural studies. Comparison of the HIV-1, ASV and PFV CCD structures highlighted both conserved as well as unique structural features such as organization of the active site and the putative host factor binding face. Despite possessing very limited sequence identity to its HIV counterpart, PFV IN was sensitive to HIV IN strand transfer inhibitors, suggesting that this class of inhibitors target the most conserved features of retroviral IN-DNA complexes.

Present address Eugene Valkov, School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Australia


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.