Active foamy virus proteinase is essential for virus infectivity but not for formation of a Pol polyprotein.

@article{Konvalinka1995ActiveFV,
  title={Active foamy virus proteinase is essential for virus infectivity but not for formation of a Pol polyprotein.},
  author={Jan Konvalinka and Martin L{\"o}chelt and H. Zentgraf and Rolf M. Fl{\"u}gel and Hans Georg Kraeusslich},
  journal={Journal of virology},
  year={1995},
  volume={69 11},
  pages={7264-8}
}
To analyze proteolytic processing of foamy (spuma) retroviruses, two mutations were generated in the presumed active-site triplet Asp-Ser-Gly in the predicted proteinase (PR) region of the human foamy virus (HSRV). The mutations changed either the presumed catalytic aspartic acid residue to a catalytically incompetent alanine or the adjacent serine to a threonine found in most cellular and retroviral proteases at this position. Both mutations were cloned into the full-length infectious HSRV DNA… CONTINUE READING
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Retroviral proteases

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The molecular biology of human and primate spuma retroviruses

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