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A more recent version of this article appeared on February 17, 2006
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M507660200v1
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Papers In Press, published online ahead of print December 19, 2005
J. Biol. Chem, 10.1074/jbc.M507660200
Submitted on July 14, 2005
Revised on December 12, 2005
Accepted on December 19, 2005

Synthesis, processing and composition of the Virion-associated HTLV-1 reverse transcriptase

Michael S. Mitchell, Jozsef Tozser, Gerald Princler, Patricia A. Lloyd, Auth Ashleigh, and Derse David

HIV Drug Resistance Program, National Cancer Institute, NCI-Frederick, Frederick, MD 21702-1201

Corresponding Author: derse{at}ncifcrf.gov

It is not known whether the low infectivity and low virion-associated polymerase activity of HTLV-1 are due to the quantity or quality of the reverse transcriptase, because the protein has not yet been fully characterized. We have developed anti-RT antibodies and constructed HTLV-1 expression plasmids that express truncated or HA-tagged Pol polyproteins to examine the maturation and composition of HTLV-1 RT. We detected virion-associated proteins corresponding to RT-IN (pr98) and RT (p62), as well as smaller proteins containing the polymerase (p49) or RNase H domains. We have identified the amino acid sequences in the Pol polyprotein that are cleaved by HTLV-1 protease to yield RT and IN. We have also identified the cleavage sites within RT that give rise to the p49 polymerase fragment. Immunoprecip-itation of an epitope-tagged p62 subunit coprecipitated p49, indicating that the HTLV-1 RT complex can exist as a p62/p49 heterodimer analogous to the RT of HIV-1 (p66/p51).


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M. S. Mitchell, E. T. Bodine, S. Hill, G. Princler, P. Lloyd, H. Mitsuya, M. Matsuoka, and D. Derse
Phenotypic and Genotypic Comparisons of Human T-Cell Leukemia Virus Type 1 Reverse Transcriptases from Infected T-Cell Lines and Patient Samples
J. Virol., May 1, 2007; 81(9): 4422 - 4428.
[Abstract] [Full Text] [PDF]


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