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Structural and Functional Insights into Foamy Viral Integrase

Department of Biotechnology, Chung-Ang University, Ansung 456-756, South Korea
Author to whom correspondence should be addressed.
Viruses 2013, 5(7), 1850-1866;
Received: 24 June 2013 / Revised: 12 July 2013 / Accepted: 12 July 2013 / Published: 18 July 2013
(This article belongs to the Special Issue Recent Progress in Foamy Virus (FV) Research)
Successful integration of retroviral DNA into the host chromosome is an essential step for viral replication. The process is mediated by virally encoded integrase (IN) and orchestrated by 3'-end processing and the strand transfer reaction. In vitro reaction conditions, such as substrate specificity, cofactor usage, and cellular binding partners for such reactions by the three distinct domains of prototype foamy viral integrase (PFV-IN) have been described well in several reports. Recent studies on the three‑dimensional structure of the interacting complexes between PFV-IN and DNA, cofactors, binding partners, or inhibitors have explored the mechanistic details of such interactions and shown its utilization as an important target to develop anti-retroviral drugs. The presence of a potent, non-transferable nuclear localization signal in the PFV C-terminal domain extends its use as a model for investigating cellular trafficking of large molecular complexes through the nuclear pore complex and also to identify novel cellular targets for such trafficking. This review focuses on recent advancements in the structural analysis and in vitro functional aspects of PFV-IN. View Full-Text
Keywords: foamy virus; integrase; anti-retroviral drugs; cellular trafficking foamy virus; integrase; anti-retroviral drugs; cellular trafficking
MDPI and ACS Style

Hossain, M.A.; Ali, M.K.; Shin, C.-G. Structural and Functional Insights into Foamy Viral Integrase. Viruses 2013, 5, 1850-1866.

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