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Inhibiting HIV-1 and MMLV Reverse Transcriptase: The potential of an Allosteric Broad-Spectrum Inhibitor

Chan, K. F.; Phua, S. X.; Su, C. T. T.; Gan, S. K.

2019-07-13 microbiology
10.1101/699470 bioRxiv
Show abstract

HIV drug resistance continues to demand for alternative drug targets. Since Reverse Transcriptase (RT) is unique and critical for the virus life cycle, it is a rational target that is likely to have less off-target effects in humans. Serendipitously, we found two chemical compound scaffolds from the NCI Diversity Set V that inhibited the HIV1- RT catalytic activity. Computational structural analyses and subsequent experimental testing demonstrated that one of the two chemical scaffolds binds to a novel location in the HIV-1 RT p51 subunit, interacting with residue Y183 that has no known association with previously reported drug resistance. This finding leads to the notion of a novel druggable site on p51 for a new class of non-nucleoside RT Inhibitors that may inhibit HIV-1 RT allosterically. Although inhibitory activity was shown experimentally only to be in the hundreds micromolar range, the scaffolds serve as a proof-of-concept of targeting HIV RT p51, with the possibility for medical chemistry methods to be applied to improve the inhibitory activity, towards a functioning drug.

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