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Fig. 1 | Cell & Bioscience

Fig. 1

From: A fission yeast cell-based system for multidrug resistant HIV-1 proteases

Fig. 1

HIV-1 mdrPRs specifically cleave the GFP-MA-Vpr and the GFP-p6-Vpr fusion protein constructs that contain indigenous cleavage sites of HIV-1 p6 or MA viral proteins. A A schematic drawing to show how the proteolytic test was designed to measure the HIV-1 mdrPR-mediated cleavages of the GFP-MA-Vpr or the GFP-p6-Vpr fusion protein constructs in fission yeast. GFP, green fluorescent protein, which typically distributes uniformly throughout fission yeast cell, here we referred it as the “GFP pattern” [35, 52]. Vpr, HIV-1 viral protein R normally localizes predominantly on the nuclear membrane and appears as a “ring-like” structure. Thus we called it the “Vpr pattern” [35, 52]. The polypeptide shown was derived either from the HIV-1 MA↓CA (DSQNY↓PIVQ) or the p6 protein (DSFNF↓PQIT). The arrow indicates the PR cleavage site. B The GFP fluorescent images show the status of the HIV-1 mdrPRs-mediated cleavages against the GFP-MA-Vpr fusion protein construct (a) or the GFP-p6-Vpr construct (b) without (left column) or with the IDV treatment (right column). The cells were examined 20 h after the PR gene induction. Arrows indicate where the PR cleavage sites are. Scale bar 10 µm

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