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Journal of Virology, August 2008, p. 8235-8238, Vol. 82, No. 16
0022-538X/08/$08.00+0     doi:10.1128/JVI.00088-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Deoxynucleoside Triphosphate Incorporation Mechanism of Foamy Virus (FV) Reverse Transcriptase: Implications for Cell Tropism of FV{triangledown}

Jose Santos-Velazquez1 and Baek Kim1,2*

Department of Microbiology and Immunology,1 Department of Oncology, School of Medicine, University of Rochester, 601 Elmwood Avenue, Box 672, Rochester, New York 146422

Received 14 January 2008/ Accepted 19 May 2008

Here, we investigated the pre-steady-state deoxynucleoside triphosphate (dNTP) incorporation kinetics of primate foamy virus (PFV) reverse transcriptase (RT) in comparison with those of HIV-1 and MuLV RTs. PFV RT displayed a drastic reduction in primer extension at low dNTP concentrations where HIV-1 RT remains highly active, indicating a low dNTP binding affinity in the case of PFV RT. Indeed, kinetic analysis showed that, as observed with MuLV RT, PFV RT exhibits ~10 to 80 times lower dNTP binding affinity than HIV-1 RT. These three RTs, however, show similar catalytic activities. In conclusion, PFV RT displays mechanistic distinctions in comparison to HIV-1 RT and shares close similarity to MuLV RT.

* Corresponding author. Mailing address: 601 Elmwood Avenue, Box 672, Department of Microbiology and Immunology, University of Rochester Medical Center, Rochester, NY 14642. Phone: (602) 275-6916. Fax: (602) 473-9573. E mail: baek_kim{at}urmc.rochester.edu

{triangledown} Published ahead of print on 28 May 2008.

Journal of Virology, August 2008, p. 8235-8238, Vol. 82, No. 16
0022-538X/08/$08.00+0     doi:10.1128/JVI.00088-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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