J Gen Virol. 2000 Dec;81(Pt 12):2941-7.
Primate foamy virus Pol proteins are imported into the nucleus.
Imrich H, Heinkelein M, Herchenröder O, Rethwilm A.
Mouse monoclonal antibodies (MAbs) that specifically detect the 127 kDa Pol precursor and the 85 kDa reverse transcriptase/RNase H (RT/RN) or pr127 and the 40 kDa integrase (IN) in immunoblot and immunofluorescence assays (IFA) were used to investigate the subcellular localization of primate foamy virus (PFV) proteins. IFA of cells infected with PFV using the anti-Pol MAbs and rabbit anti-capsid (Gag) serum revealed that both the Gag and Pol proteins are transported into the nucleus. Transfection of cells with eukaryotic expression constructs for pr127(Pol), p85(RT/RN) and p40(IN) served to show Gag-independent subcellular localization of Pol proteins. Interestingly, not only the Pol precursor and IN molecules were found to be localized to the nucleus, but also the RT/RN subdomain. It is therefore suggested that PFV cores bear at least three separate nuclear localization signals, one in Gag and two in Pol. The latter appear to be localized to the two Pol subdomains.
A multi-protein complex consisting of the cellular coactivator p300, AP-1/ATF as well as NF-kB is responsible for the activation of the mouse major histocompatibility class I (H-2Kb) enhancer A.
Efficient intracellular retrotransposition of an exogenous primate retrovirus genome.