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Characterization of the polymerase and RNase H activities of human foamy virus reverse transcriptase

  1. Author:
    Boyer, P. L.
    Stenbak, C. R.
    Clark, P. K.
    Linial, M. L.
    Hughes, S. H.
  2. Author Address

    NCI, Frederick Canc Res & Dev Ctr, HIV Drug Resistance Program, Canc Res Ctr, Frederick, MD 21702 USA. SAIC, Basic Res Program, Frederick, MD 21702 USA. Fred Hutchinson Canc Res Ctr, Div Basic Sci, Seattle, WA 98109 USA. Univ Washington, Dept Microbiol, Seattle, WA 98195 USA. Hughes, SH, NCI, Frederick Canc Res & Dev Ctr, HIV Drug Resistance Program, Canc Res Ctr, POB B,Bldg 539,Room 130A, Frederick, MD 21702 USA
    1. Year: 2004
  1. Journal: Journal of Virology
    1. 78
    2. 12
    3. Pages: 6112-6121
  2. Type of Article: Article
  1. Abstract:

    Foamy virus (FV) replication, while related to that of orthoretroviruses, differs at a number of steps. Several of these differences involve the reverse transcriptase (RT). There appear to be fewer RTs present in FV than in orthoretroviruses; we previously proposed that the polymerase of FV RT was more active than orthoretroviral RTs to compensate for the numerical difference. Here we present further characterization of the RT of FV. The polymerase activity of FV RT was greater than that of human immunodeficiency virus type I RT in a variety of assays. We also examined the RNase H activity of FV RT, and we propose that FV RT has a basic loop in the RNase H domain. Although the sequence of the basic loop of FV RT is different from the basic loop of either Moloney leukemia virus RNase H or Escherichia coli RNase H, the FV RT basic loop appears to have a similar function

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