HIV-1 RTHuman Immunodeficiency Virus Type 1 Reverse Transcriptase
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HIV-1 RT gene subcloned into the p6HRT_prot plasmid was kindly provided by Stuart Le Grice (NCI, Frederick, Maryland, USA).
Since Sennosides A and B were identified as novel dual functions RTIs, we wanted to compare them to known NNRTIs or RNase H inhibitors by using a series of previously described HIV-1 RT mutants.
Such analysis can reveal whether simultaneous binding (or inhibition) of the HIV-1 RT enzyme by the two compounds is occurring or not.
Given their ability to inhibit both the HIV-1 RT and IN functions in biochemical assays, we wanted to evaluate the effect of Sennoside A and B on the early phases of the HIV-1 replication.
Overall, Sennoside A represents a novel attractive scaffold of dual function RTI that deserves further investigations by means of chemical modification, in search of new dual enzyme derivatives active on both HIV-1 RT and IN.
Following absorption, TDF is rapidly converted to tenofovir which is metabolized intracellularly to the active metabolite, TDF diphosphate, a competitive inhibitor of HIV-1 RT that terminates the growing DNA chain.
The Lys103Asn mutation of HIV-1 RT: a novel mechanism of drug resistance.
For this, we provided a multidrug-resistant variant of HIV-1 RT (RT1.14) [16], complemented for safety sake, with mutations inhibiting polymerase and RNase H activity, with a leader signal peptide (Ld) of the nonstructural protein 1 of tick-borne encephalitis virus (NS1 of TBEV).
Wild-type p66/p51 heterodimeric HIV-1 RT was expressed in M-15 [pREP4] E.coli strain transformed with the plasmid p6HRT [31] and purified as previously described [32].
RNase H activity assay of HIV-1 RT was tested by using 6,7 mmol of 18-ribo-Fl/18-deoxy duplex (18-mer oligoribonucleotide (18-ribo-Fl: 5-r(GAUCUGAGCCUGGGAGCU)-fluorescein-3,f and 18-mer oligodeoxyribonucleotide (18-deoxy d5-d(AGCTCCCAGGCTC AGAUC)-3;)).
Both lysates contained also a protein with the molecular mass of 51 kDa corresponding the polymerase subunit of HIV-1 RT [44].