PMC:3320587 / 26918-31871 JSONTXT

{"target":"http://pubannotation.org/docs/sourcedb/PMC/sourceid/3320587","sourcedb":"PMC","sourceid":"3320587","source_url":"http://www.ncbi.nlm.nih.gov/pmc/3320587","text":"NF-κB and NFAT5 binding to the HIV-1 LTR can be specifically disrupted\nTo demonstrate that the impact of NFAT5 silencing on MTb-induced viral replication was a direct effect due to modulation of recruitment of NFAT5 to the HIV-1 LTR and not due to secondary, NFAT5-regulated effects, we set out to disrupt NFAT5 binding to the viral LTR in the context of HIV-1/MTb co-infection. This series of experiments also allowed us to dissect the relative importance of NFAT5 and NF-κB binding to the HIV-1 LTR in MTb regulation of HIV-1 replication.\nTo perform these experiments, we constructed a panel of infectious HIV-1Lai/Bal-env molecular clones where either the NFAT5 site was specifically disrupted or the two NF-κB binding sites were either individually or dually disrupted (Figure 3A). Specifically, we constructed a clone in which the NFAT5 binding site was mutated (named HIV-1Lai/Bal-env-N5-Mut) by changing the CC dinucleotide to TT in the core NFAT5 binding site and introduced substitution mutations into the NF-κB/NFAT5 shared binding element that we predicted would disrupt NF-κB binding but preserve NFAT5 binding. Specifically, we mutated two guanines (GG) in the κB I site and changed them to thymine and adenine (TA) (HIV-1Lai/Bal-env-κB I-mut) and also introduced the same GG to TA change in the second, more distal NF-κB site (κB II) in HIV-1Lai/Bal-env (HIV-1Lai/Bal-env-κB II-Mut). We also created a double NF-κB site mutant virus (HIV-1Lai/Bal-env-κB I+II-Mut) in order to test the impact of complete disruption of NF-κB binding to the HIV-1 LTR on MTb regulation.\n10.1371/journal.ppat.1002620.g003 Figure 3 Specific disruption of NFAT5 or NF-κB binding sites in the LTR of HIV-1 subtype B.\n(A) Mutations introduced into a HIV-1Lai/Bal-env infectious molecular clone. NF-κB and NFAT5 binding site mutations were introduced into the LTR of the HIV-1Lai/Bal-env-wild type (WT) infectious molecular clone. The NF-κB binding site mutants (HIV-1Lai/Bal-env-κB I-Mut, HIV-1Lai/Bal-env-κB II-Mut, HIV-1Lai/Bal-env-κB I+II-Mut), and NFAT5 binding site mutant (HIV-1Lai/Bal-env-N5-Mut) are shown along with the HIV-1Lai/Bal-env-WT sequence. Mutations were introduced into the 3′ LTR of the HIV-1Lai/Bal-env–WT proviral sequence. (B) Specific mutation of the NFAT5 binding site abolishes NFAT5 binding to the viral LTR but does not affect NF-κB p50/p65 binding to the overlapping NF-κB binding site. Quantitative DNaseI footprinting analysis is shown using HIV-1 LTR fragments (-262 to +4 nt relative to the transcription start site) from HIV-1Lai/Bal-env-WT and HIV-1Lai/Bal-env-N5-Mut and increasing concentrations of recombinant NF-κB (p50/p65) (25 ng, 100 ng, and 500 ng), or NFAT5 (10 ng, 50 ng, and 250 ng). The regions that are protected from DNase I cleavage by the binding of NF-κB and NFAT5 are indicated with a bars. (C) Specific disruption of the HIV-1 subtype B NF-κB binding sites effectively abrogates recombinant p50/p65 binding. Quantitative DNaseI footprinting analysis is shown of nucleotides −262 to +4 from HIV-1Lai/Bal-env-WT, HIV-1Lai/Bal-env-κB I-Mut, HIV-1Lai/Bal-env-κB II-Mut, and HIV-1Lai/Bal-env-κB I+II-Mut and increasing concentrations of recombinant NF-κB (p50/p65) (25 ng, 100 ng, and 500 ng). The regions that are protected from DNase I cleavage by the binding of recombinant NF-κB are indicated with a bars. (D) Specific disruption of the HIV-1 subtype B NF-κB binding site does not inhibit but enhances NFAT5 binding to this region. Quantitative DNaseI footprinting analysis is shown of nucleotides −262 to +4 from HIV-1Lai/Bal-env-WT, HIV-1Lai/Bal-env-κB I-Mut, HIV-1Lai/Bal-env-κB II-Mut, and HIV-1Lai/Bal-env-κB I+II-Mut and increasing concentrations of recombinant NFAT5 (10 ng, 50 ng, and 250 ng). The regions that are protected from DNase I cleavage by the binding of recombinant NFAT5 are indicated with a bars. To determine the specificity of these substitutions upon NFAT5 and NF-κB p50/p65 binding to the LTR, we performed a quantitative DNase I footprinting analysis using the wild-type LTR or mutant LTRs in combination with increasing concentrations of recombinant NFAT5 or NF-κB p50/p65 proteins. As shown in Figure 3B, the N5-Mut LTR could not bind NFAT5 (compare lanes 12–15 and lanes 17–20), but p50/p65 binding was not impaired (compare lanes 2–5 with lanes 7–10). By contrast, changing the GG dinucleotide to TA in either NF-κB binding motif, as predicted, inhibited p50/p65 binding at each site (compare lanes 2–5 with lanes 7–10 and lanes 12–15 of Figure 3C). As expected, mutation of both NF-κB sites (κB I+II-Mut) resulted in abrogation of p50/p65 binding to the LTR. However, recombinant NFAT5 binding to the single and the double NF-κB mutant LTRs was not impaired and indeed appeared enhanced (compare lanes 2–5 to lanes 7–20 of Figure 3D). Thus, binding of NFAT5 or NF-κB p50/p65 to their respective motifs can be specifically disrupted within an overlapping or shared binding site.","divisions":[{"label":"title","span":{"begin":0,"end":70}},{"label":"p","span":{"begin":71,"end":540}},{"label":"p","span":{"begin":541,"end":1581}},{"label":"figure 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