Abstract
Background In foamy viruses (FVs) only the integrase domain is cleaved off from the Pol precursor protein, resulting in a multifunctional mature reverse transcriptase (RT) harbouring the protease (PR) domain at its N-terminus. In contrast to the heterodimeric RT of human immunodeficiency virus type 1 (HIV-1), which consists of a 66 kDa and a 51 kDa subunit, the PR-RT of FVs is a monomeric protein. Thus, we wanted to analyse the inhibitory effect of HIV-1 nonnucleoside and RNase H inhibitors on the enzyme functions of FV PR-RT.
Highlights
In foamy viruses (FVs) only the integrase domain is cleaved off from the Pol precursor protein, resulting in a multifunctional mature reverse transcriptase (RT) harbouring the protease (PR) domain at its N-terminus
We tested the effect of five human immunodeficiency virus type 1 (HIV-1) RNase H inhibitors, known to interact with different HIV-1 RT pockets [1,2], on the PR-RT of prototype FV (PFV)
The non-nucleoside RT inhibitor Efavirenz was inactive on PFV PR-RT, implying the absence of a binding pocket similar to the one in HIV-1 RT
Summary
In foamy viruses (FVs) only the integrase domain is cleaved off from the Pol precursor protein, resulting in a multifunctional mature reverse transcriptase (RT) harbouring the protease (PR) domain at its N-terminus. Results We tested the effect of five HIV-1 RNase H inhibitors, known to interact with different HIV-1 RT pockets [1,2], on the PR-RT of prototype FV (PFV).
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