One of the biggest challenges for AIDS treatment is the frequent mutation of the virus genome, which makes many existing anti-HIV drugs less effective over time. This calls for the continuous search for new anti-HIV drugs. In this work, we engineered a novel molecular probe to visualize the inhibition of HIV-1 protease within living cells through F�rster resonance energy transfer (FRET) microscopy imaging. The probe was developed by sandwiching a HIV-1 protease cleavage site p2/p7 peptide between two fluorescent proteins, i.e., AcGFP (a mutant green fluorescent protein) and mCherry (a red fluorescent protein). The addition of protease inhibitor prevents the peptide cleavage, allowing the resonance energy transfer from the donor to the acceptor. Thus, the HIV-1 protease inhibition can be quantitatively determined by measuring the change of FRET ratio of mCherry to AcGFP. Our studies demonstrated that the probe would allow high-content screening during the development of new anti-HIV drugs.

Visualization of HIV protease inhibition using a FRET molecular probe

239th National Meeting (2010)

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