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<p><small><strong> Figure 1. UHRF1 ChIP results</strong><br /> ChIP was performed with HCT116 chromatin extract and 5 μg of either control rabbit IgG or UHRF1 antibody. The precipitated DNA was detected by PCR with primer set targeting to PPARG promoter. </small></p>
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<p><small><strong> Figure 2. IP results</strong><br /> UHRF1 antibody immunoprecipitates UHRF1 protein in IP experiments. IP Sample: HeLa whole cell extract A. 40 μg HeLa whole cell extract B. Control with 2 μg of preimmune rabbit IgG C. Immunoprecipitation of UHRF1 protein by 2 μg of UHRF1 antibody (C15410258) 5% SDS-PAGE The immunoprecipitated UHRF1 protein was detected by western blot with the UHRF1 antibody (C15410258) diluted 1:1,000. </small></p>
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<p><small><strong> Figure 3. Western blot</strong><br /> Sample: 30 μg of HCT116 whole cell lysate 7.5% SDS PAGE UHRF1 diluted 1:1,000 </small></p>
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<p><small><strong> Figure 4. IHC</strong><br /> UHRF1 antibody detects UHRF1 protein on HBL435 xenograft by immunohistochemical analysis. Sample: Paraffin-embedded HBL435 xenograft. UHRF1 antibody (C15410258) dilution: 1:500. </small></p>
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<p><small><strong> Figure 5. IFA</strong><br /> Confocal immunofluorescence analysis of paraformaldehyde-fixed HeLa cells using UHRF1 antibody (Cat. No. C15410258) (Green) at a 1:500 dilution. Red: Alpha-tubulin filaments. </small></p>
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<p><small><strong> Figure 2. IP results</strong><br /> UHRF1 antibody immunoprecipitates UHRF1 protein in IP experiments. IP Sample: HeLa whole cell extract A. 40 μg HeLa whole cell extract B. Control with 2 μg of preimmune rabbit IgG C. Immunoprecipitation of UHRF1 protein by 2 μg of UHRF1 antibody (C15410258) 5% SDS-PAGE The immunoprecipitated UHRF1 protein was detected by western blot with the UHRF1 antibody (C15410258) diluted 1:1,000. </small></p>
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<p><small><strong> Figure 3. Western blot</strong><br /> Sample: 30 μg of HCT116 whole cell lysate 7.5% SDS PAGE UHRF1 diluted 1:1,000 </small></p>
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<p><small><strong> Figure 5. IFA</strong><br /> Confocal immunofluorescence analysis of paraformaldehyde-fixed HeLa cells using UHRF1 antibody (Cat. No. C15410258) (Green) at a 1:500 dilution. Red: Alpha-tubulin filaments. </small></p>
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<p><small><strong> Figure 2. IP results</strong><br /> UHRF1 antibody immunoprecipitates UHRF1 protein in IP experiments. IP Sample: HeLa whole cell extract A. 40 μg HeLa whole cell extract B. Control with 2 μg of preimmune rabbit IgG C. Immunoprecipitation of UHRF1 protein by 2 μg of UHRF1 antibody (C15410258) 5% SDS-PAGE The immunoprecipitated UHRF1 protein was detected by western blot with the UHRF1 antibody (C15410258) diluted 1:1,000. </small></p>
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<p><small><strong> Figure 3. Western blot</strong><br /> Sample: 30 μg of HCT116 whole cell lysate 7.5% SDS PAGE UHRF1 diluted 1:1,000 </small></p>
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<p><small><strong> Figure 4. IHC</strong><br /> UHRF1 antibody detects UHRF1 protein on HBL435 xenograft by immunohistochemical analysis. Sample: Paraffin-embedded HBL435 xenograft. UHRF1 antibody (C15410258) dilution: 1:500. </small></p>
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<p><small><strong> Figure 5. IFA</strong><br /> Confocal immunofluorescence analysis of paraformaldehyde-fixed HeLa cells using UHRF1 antibody (Cat. No. C15410258) (Green) at a 1:500 dilution. Red: Alpha-tubulin filaments. </small></p>
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<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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<p><small><strong> Figure 1. UHRF1 ChIP results</strong><br /> ChIP was performed with HCT116 chromatin extract and 5 μg of either control rabbit IgG or UHRF1 antibody. The precipitated DNA was detected by PCR with primer set targeting to PPARG promoter. </small></p>
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<p><small><strong> Figure 2. IP results</strong><br /> UHRF1 antibody immunoprecipitates UHRF1 protein in IP experiments. IP Sample: HeLa whole cell extract A. 40 μg HeLa whole cell extract B. Control with 2 μg of preimmune rabbit IgG C. Immunoprecipitation of UHRF1 protein by 2 μg of UHRF1 antibody (C15410258) 5% SDS-PAGE The immunoprecipitated UHRF1 protein was detected by western blot with the UHRF1 antibody (C15410258) diluted 1:1,000. </small></p>
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<p><small><strong> Figure 5. IFA</strong><br /> Confocal immunofluorescence analysis of paraformaldehyde-fixed HeLa cells using UHRF1 antibody (Cat. No. C15410258) (Green) at a 1:500 dilution. Red: Alpha-tubulin filaments. </small></p>
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<p><small><strong> Figure 2. IP results</strong><br /> UHRF1 antibody immunoprecipitates UHRF1 protein in IP experiments. IP Sample: HeLa whole cell extract A. 40 μg HeLa whole cell extract B. Control with 2 μg of preimmune rabbit IgG C. Immunoprecipitation of UHRF1 protein by 2 μg of UHRF1 antibody (C15410258) 5% SDS-PAGE The immunoprecipitated UHRF1 protein was detected by western blot with the UHRF1 antibody (C15410258) diluted 1:1,000. </small></p>
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<p><small><strong> Figure 5. IFA</strong><br /> Confocal immunofluorescence analysis of paraformaldehyde-fixed HeLa cells using UHRF1 antibody (Cat. No. C15410258) (Green) at a 1:500 dilution. Red: Alpha-tubulin filaments. </small></p>
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<p><small><strong> Figure 4. IHC</strong><br /> UHRF1 antibody detects UHRF1 protein on HBL435 xenograft by immunohistochemical analysis. Sample: Paraffin-embedded HBL435 xenograft. UHRF1 antibody (C15410258) dilution: 1:500. </small></p>
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<p><small><strong> Figure 5. IFA</strong><br /> Confocal immunofluorescence analysis of paraformaldehyde-fixed HeLa cells using UHRF1 antibody (Cat. No. C15410258) (Green) at a 1:500 dilution. Red: Alpha-tubulin filaments. </small></p>
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<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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'description' => '<p>To accomplish the remarkable task of lifelong infection, the Epstein-Barr virus (EBV) switches between four viral genome latency and lytic programmes to navigate the B-cell compartment and evade immune responses. The transforming programme, consisting of highly immunogenic EBV nuclear antigen (EBNA) and latent membrane proteins (LMPs), is expressed in newly infected B lymphocytes and in post-transplant lymphomas. On memory cell differentiation and in most EBV-associated Burkitt's lymphomas, all but one viral antigen are repressed for immunoevasion. To gain insights into the epigenetic mechanisms that restrict immunogenic oncoprotein expression, a genome-scale CRISPR-Cas9 screen was performed in EBV and Burkitt's lymphoma cells. Here, we show that the ubiquitin ligase ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1) and its DNA methyltransferase partner DNA methyltransferase I (DNMT1) are critical for the restriction of EBNA and LMP expression. All UHRF1 reader and writer domains were necessary for silencing and DNMT3B was identified as an upstream viral genome CpG methylation initiator. Polycomb repressive complex I exerted a further layer of control over LMP expression, suggesting a second mechanism for latency programme switching. UHRF1, DNMT1 and DNMT3B are upregulated in germinal centre B cells, the Burkitt's lymphoma cell of origin, providing a molecular link between B-cell state and the EBV latency programme. These results suggest rational therapeutic targets to manipulate EBV oncoprotein expression.</p>',
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<p><small><strong> Figure 1. UHRF1 ChIP results</strong><br /> ChIP was performed with HCT116 chromatin extract and 5 μg of either control rabbit IgG or UHRF1 antibody. The precipitated DNA was detected by PCR with primer set targeting to PPARG promoter. </small></p>
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<p><small><strong> Figure 2. IP results</strong><br /> UHRF1 antibody immunoprecipitates UHRF1 protein in IP experiments. IP Sample: HeLa whole cell extract A. 40 μg HeLa whole cell extract B. Control with 2 μg of preimmune rabbit IgG C. Immunoprecipitation of UHRF1 protein by 2 μg of UHRF1 antibody (C15410258) 5% SDS-PAGE The immunoprecipitated UHRF1 protein was detected by western blot with the UHRF1 antibody (C15410258) diluted 1:1,000. </small></p>
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<p><small><strong> Figure 4. IHC</strong><br /> UHRF1 antibody detects UHRF1 protein on HBL435 xenograft by immunohistochemical analysis. Sample: Paraffin-embedded HBL435 xenograft. UHRF1 antibody (C15410258) dilution: 1:500. </small></p>
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<p><small><strong> Figure 5. IFA</strong><br /> Confocal immunofluorescence analysis of paraformaldehyde-fixed HeLa cells using UHRF1 antibody (Cat. No. C15410258) (Green) at a 1:500 dilution. Red: Alpha-tubulin filaments. </small></p>
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<p><small><strong> Figure 5. IFA</strong><br /> Confocal immunofluorescence analysis of paraformaldehyde-fixed HeLa cells using UHRF1 antibody (Cat. No. C15410258) (Green) at a 1:500 dilution. Red: Alpha-tubulin filaments. </small></p>
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<p><small><strong> Figure 4. IHC</strong><br /> UHRF1 antibody detects UHRF1 protein on HBL435 xenograft by immunohistochemical analysis. Sample: Paraffin-embedded HBL435 xenograft. UHRF1 antibody (C15410258) dilution: 1:500. </small></p>
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<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
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<p><br />Chromatin immunoprecipitation (<b>ChIP</b>) is a technique to study the associations of proteins with the specific genomic regions in intact cells. One of the most important steps of this protocol is the immunoprecipitation of targeted protein using the antibody specifically recognizing it. The quality of antibodies used in ChIP is essential for the success of the experiment. Diagenode offers extensively validated ChIP-grade antibodies, confirmed for their specificity, and high level of performance in ChIP. Each batch is validated, and batch-specific data are available on the website.</p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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'description' => '<p>BACKGROUND: The multiplicity, heterogeneity, and dynamic nature of human immunodeficiency virus type-1 (HIV-1) latency mechanisms are reflected in the current lack of functional cure for HIV-1. Accordingly, all classes of latency-reversing agents (LRAs) have been reported to present variable ex vivo potencies. Here, we investigated the molecular mechanisms underlying the potency variability of one LRA: the DNA methylation inhibitor 5-aza-2'-deoxycytidine (5-AzadC). METHODS: We employed epigenetic interrogation methods (electrophoretic mobility shift assays, chromatin immunoprecipitation, Infinium array) in complementary HIV-1 infection models (latently-infected T-cell line models, primary CD4 T-cell models and ex vivo cultures of PBMCs from HIV individuals). Extracellular staining of cell surface receptors and intracellular metabolic activity were measured in drug-treated cells. HIV-1 expression in reactivation studies was explored by combining the measures of capsid p24 protein, green fluorescence protein signal, intracellular and extracellular viral RNA and viral DNA. FINDINGS: We uncovered specific demethylation CpG signatures induced by 5-AzadC in the HIV-1 promoter. By analyzing the binding modalities to these CpG, we revealed the recruitment of the epigenetic integrator Ubiquitin-like with PHD and RING finger domain 1 (UHRF1) to the HIV-1 promoter. We showed that UHRF1 redundantly binds to the HIV-1 promoter with different binding modalities where DNA methylation was either non-essential, essential or enhancing UHRF1 binding. We further demonstrated the role of UHRF1 in the epigenetic repression of the latent viral promoter by a concerted control of DNA and histone methylations. INTERPRETATION: A better understanding of the molecular mechanisms of HIV-1 latency allows for the development of innovative antiviral strategies. As a proof-of-concept, we showed that pharmacological inhibition of UHRF1 in ex vivo HIV patient cell cultures resulted in potent viral reactivation from latency. Together, we identify UHRF1 as a novel actor in HIV-1 epigenetic silencing and highlight that it constitutes a new molecular target for HIV-1 cure strategies. FUNDING: Funding was provided by the Belgian National Fund for Scientific Research (F.R.S.-FNRS, Belgium), the « Fondation Roi Baudouin », the NEAT (European AIDS Treatment Network) program, the Internationale Brachet Stiftung, ViiV Healthcare, the Télévie, the Walloon Region (« Fonds de Maturation »), « Les Amis des Instituts Pasteur à Bruxelles, asbl », the University of Brussels (Action de Recherche Concertée ULB grant), the Marie Skodowska Curie COFUND action, the European Union's Horizon 2020 research and innovation program under grant agreement No 691119-EU4HIVCURE-H2020-MSCA-RISE-2015, the French Agency for Research on AIDS and Viral Hepatitis (ANRS), the Sidaction and the "Alsace contre le Cancer" Foundation. This work is supported by 1UM1AI164562-01, co-funded by National Heart, Lung and Blood Institute, National Institute of Diabetes and Digestive and Kidney Diseases, National Institute of Neurological Disorders and Stroke, National Institute on Drug Abuse and the National Institute of Allergy and Infectious Diseases.</p>',
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'description' => '<p>To accomplish the remarkable task of lifelong infection, the Epstein-Barr virus (EBV) switches between four viral genome latency and lytic programmes to navigate the B-cell compartment and evade immune responses. The transforming programme, consisting of highly immunogenic EBV nuclear antigen (EBNA) and latent membrane proteins (LMPs), is expressed in newly infected B lymphocytes and in post-transplant lymphomas. On memory cell differentiation and in most EBV-associated Burkitt's lymphomas, all but one viral antigen are repressed for immunoevasion. To gain insights into the epigenetic mechanisms that restrict immunogenic oncoprotein expression, a genome-scale CRISPR-Cas9 screen was performed in EBV and Burkitt's lymphoma cells. Here, we show that the ubiquitin ligase ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1) and its DNA methyltransferase partner DNA methyltransferase I (DNMT1) are critical for the restriction of EBNA and LMP expression. All UHRF1 reader and writer domains were necessary for silencing and DNMT3B was identified as an upstream viral genome CpG methylation initiator. Polycomb repressive complex I exerted a further layer of control over LMP expression, suggesting a second mechanism for latency programme switching. UHRF1, DNMT1 and DNMT3B are upregulated in germinal centre B cells, the Burkitt's lymphoma cell of origin, providing a molecular link between B-cell state and the EBV latency programme. These results suggest rational therapeutic targets to manipulate EBV oncoprotein expression.</p>',
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<p><small><strong> Figure 1. UHRF1 ChIP results</strong><br /> ChIP was performed with HCT116 chromatin extract and 5 μg of either control rabbit IgG or UHRF1 antibody. The precipitated DNA was detected by PCR with primer set targeting to PPARG promoter. </small></p>
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<p><small><strong> Figure 2. IP results</strong><br /> UHRF1 antibody immunoprecipitates UHRF1 protein in IP experiments. IP Sample: HeLa whole cell extract A. 40 μg HeLa whole cell extract B. Control with 2 μg of preimmune rabbit IgG C. Immunoprecipitation of UHRF1 protein by 2 μg of UHRF1 antibody (C15410258) 5% SDS-PAGE The immunoprecipitated UHRF1 protein was detected by western blot with the UHRF1 antibody (C15410258) diluted 1:1,000. </small></p>
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<p><small><strong> Figure 3. Western blot</strong><br /> Sample: 30 μg of HCT116 whole cell lysate 7.5% SDS PAGE UHRF1 diluted 1:1,000 </small></p>
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<p><small><strong> Figure 4. IHC</strong><br /> UHRF1 antibody detects UHRF1 protein on HBL435 xenograft by immunohistochemical analysis. Sample: Paraffin-embedded HBL435 xenograft. UHRF1 antibody (C15410258) dilution: 1:500. </small></p>
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<p><small><strong> Figure 5. IFA</strong><br /> Confocal immunofluorescence analysis of paraformaldehyde-fixed HeLa cells using UHRF1 antibody (Cat. No. C15410258) (Green) at a 1:500 dilution. Red: Alpha-tubulin filaments. </small></p>
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'description' => '<p>To accomplish the remarkable task of lifelong infection, the Epstein-Barr virus (EBV) switches between four viral genome latency and lytic programmes to navigate the B-cell compartment and evade immune responses. The transforming programme, consisting of highly immunogenic EBV nuclear antigen (EBNA) and latent membrane proteins (LMPs), is expressed in newly infected B lymphocytes and in post-transplant lymphomas. On memory cell differentiation and in most EBV-associated Burkitt's lymphomas, all but one viral antigen are repressed for immunoevasion. To gain insights into the epigenetic mechanisms that restrict immunogenic oncoprotein expression, a genome-scale CRISPR-Cas9 screen was performed in EBV and Burkitt's lymphoma cells. Here, we show that the ubiquitin ligase ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1) and its DNA methyltransferase partner DNA methyltransferase I (DNMT1) are critical for the restriction of EBNA and LMP expression. All UHRF1 reader and writer domains were necessary for silencing and DNMT3B was identified as an upstream viral genome CpG methylation initiator. Polycomb repressive complex I exerted a further layer of control over LMP expression, suggesting a second mechanism for latency programme switching. UHRF1, DNMT1 and DNMT3B are upregulated in germinal centre B cells, the Burkitt's lymphoma cell of origin, providing a molecular link between B-cell state and the EBV latency programme. These results suggest rational therapeutic targets to manipulate EBV oncoprotein expression.</p>',
'date' => '2020-05-18',
'pmid' => 'http://www.pubmed.gov/32424339',
'doi' => '10.1038/s41564-020-0724-y',
'modified' => '2020-08-17 10:24:57',
'created' => '2020-08-10 12:12:25',
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View::render() - CORE/Cake/View/View.php, line 473
Controller::render() - CORE/Cake/Controller/Controller.php, line 963
ProductsController::slug() - APP/Controller/ProductsController.php, line 1052
ReflectionMethod::invokeArgs() - [internal], line ??
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<p><small><strong> Figure 5. IFA</strong><br /> Confocal immunofluorescence analysis of paraformaldehyde-fixed HeLa cells using UHRF1 antibody (Cat. No. C15410258) (Green) at a 1:500 dilution. Red: Alpha-tubulin filaments. </small></p>
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<p><small><strong> Figure 4. IHC</strong><br /> UHRF1 antibody detects UHRF1 protein on HBL435 xenograft by immunohistochemical analysis. Sample: Paraffin-embedded HBL435 xenograft. UHRF1 antibody (C15410258) dilution: 1:500. </small></p>
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<p><small><strong> Figure 5. IFA</strong><br /> Confocal immunofluorescence analysis of paraformaldehyde-fixed HeLa cells using UHRF1 antibody (Cat. No. C15410258) (Green) at a 1:500 dilution. Red: Alpha-tubulin filaments. </small></p>
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<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
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<p><br />Chromatin immunoprecipitation (<b>ChIP</b>) is a technique to study the associations of proteins with the specific genomic regions in intact cells. One of the most important steps of this protocol is the immunoprecipitation of targeted protein using the antibody specifically recognizing it. The quality of antibodies used in ChIP is essential for the success of the experiment. Diagenode offers extensively validated ChIP-grade antibodies, confirmed for their specificity, and high level of performance in ChIP. Each batch is validated, and batch-specific data are available on the website.</p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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'description' => '<p>BACKGROUND: The multiplicity, heterogeneity, and dynamic nature of human immunodeficiency virus type-1 (HIV-1) latency mechanisms are reflected in the current lack of functional cure for HIV-1. Accordingly, all classes of latency-reversing agents (LRAs) have been reported to present variable ex vivo potencies. Here, we investigated the molecular mechanisms underlying the potency variability of one LRA: the DNA methylation inhibitor 5-aza-2'-deoxycytidine (5-AzadC). METHODS: We employed epigenetic interrogation methods (electrophoretic mobility shift assays, chromatin immunoprecipitation, Infinium array) in complementary HIV-1 infection models (latently-infected T-cell line models, primary CD4 T-cell models and ex vivo cultures of PBMCs from HIV individuals). Extracellular staining of cell surface receptors and intracellular metabolic activity were measured in drug-treated cells. HIV-1 expression in reactivation studies was explored by combining the measures of capsid p24 protein, green fluorescence protein signal, intracellular and extracellular viral RNA and viral DNA. FINDINGS: We uncovered specific demethylation CpG signatures induced by 5-AzadC in the HIV-1 promoter. By analyzing the binding modalities to these CpG, we revealed the recruitment of the epigenetic integrator Ubiquitin-like with PHD and RING finger domain 1 (UHRF1) to the HIV-1 promoter. We showed that UHRF1 redundantly binds to the HIV-1 promoter with different binding modalities where DNA methylation was either non-essential, essential or enhancing UHRF1 binding. We further demonstrated the role of UHRF1 in the epigenetic repression of the latent viral promoter by a concerted control of DNA and histone methylations. INTERPRETATION: A better understanding of the molecular mechanisms of HIV-1 latency allows for the development of innovative antiviral strategies. As a proof-of-concept, we showed that pharmacological inhibition of UHRF1 in ex vivo HIV patient cell cultures resulted in potent viral reactivation from latency. Together, we identify UHRF1 as a novel actor in HIV-1 epigenetic silencing and highlight that it constitutes a new molecular target for HIV-1 cure strategies. FUNDING: Funding was provided by the Belgian National Fund for Scientific Research (F.R.S.-FNRS, Belgium), the « Fondation Roi Baudouin », the NEAT (European AIDS Treatment Network) program, the Internationale Brachet Stiftung, ViiV Healthcare, the Télévie, the Walloon Region (« Fonds de Maturation »), « Les Amis des Instituts Pasteur à Bruxelles, asbl », the University of Brussels (Action de Recherche Concertée ULB grant), the Marie Skodowska Curie COFUND action, the European Union's Horizon 2020 research and innovation program under grant agreement No 691119-EU4HIVCURE-H2020-MSCA-RISE-2015, the French Agency for Research on AIDS and Viral Hepatitis (ANRS), the Sidaction and the "Alsace contre le Cancer" Foundation. This work is supported by 1UM1AI164562-01, co-funded by National Heart, Lung and Blood Institute, National Institute of Diabetes and Digestive and Kidney Diseases, National Institute of Neurological Disorders and Stroke, National Institute on Drug Abuse and the National Institute of Allergy and Infectious Diseases.</p>',
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'description' => '<p>To accomplish the remarkable task of lifelong infection, the Epstein-Barr virus (EBV) switches between four viral genome latency and lytic programmes to navigate the B-cell compartment and evade immune responses. The transforming programme, consisting of highly immunogenic EBV nuclear antigen (EBNA) and latent membrane proteins (LMPs), is expressed in newly infected B lymphocytes and in post-transplant lymphomas. On memory cell differentiation and in most EBV-associated Burkitt's lymphomas, all but one viral antigen are repressed for immunoevasion. To gain insights into the epigenetic mechanisms that restrict immunogenic oncoprotein expression, a genome-scale CRISPR-Cas9 screen was performed in EBV and Burkitt's lymphoma cells. Here, we show that the ubiquitin ligase ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1) and its DNA methyltransferase partner DNA methyltransferase I (DNMT1) are critical for the restriction of EBNA and LMP expression. All UHRF1 reader and writer domains were necessary for silencing and DNMT3B was identified as an upstream viral genome CpG methylation initiator. Polycomb repressive complex I exerted a further layer of control over LMP expression, suggesting a second mechanism for latency programme switching. UHRF1, DNMT1 and DNMT3B are upregulated in germinal centre B cells, the Burkitt's lymphoma cell of origin, providing a molecular link between B-cell state and the EBV latency programme. These results suggest rational therapeutic targets to manipulate EBV oncoprotein expression.</p>',
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<p><small><strong> Figure 1. UHRF1 ChIP results</strong><br /> ChIP was performed with HCT116 chromatin extract and 5 μg of either control rabbit IgG or UHRF1 antibody. The precipitated DNA was detected by PCR with primer set targeting to PPARG promoter. </small></p>
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<p><small><strong> Figure 2. IP results</strong><br /> UHRF1 antibody immunoprecipitates UHRF1 protein in IP experiments. IP Sample: HeLa whole cell extract A. 40 μg HeLa whole cell extract B. Control with 2 μg of preimmune rabbit IgG C. Immunoprecipitation of UHRF1 protein by 2 μg of UHRF1 antibody (C15410258) 5% SDS-PAGE The immunoprecipitated UHRF1 protein was detected by western blot with the UHRF1 antibody (C15410258) diluted 1:1,000. </small></p>
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<p><small><strong> Figure 3. Western blot</strong><br /> Sample: 30 μg of HCT116 whole cell lysate 7.5% SDS PAGE UHRF1 diluted 1:1,000 </small></p>
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<p><small><strong> Figure 4. IHC</strong><br /> UHRF1 antibody detects UHRF1 protein on HBL435 xenograft by immunohistochemical analysis. Sample: Paraffin-embedded HBL435 xenograft. UHRF1 antibody (C15410258) dilution: 1:500. </small></p>
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<p><small><strong> Figure 5. IFA</strong><br /> Confocal immunofluorescence analysis of paraformaldehyde-fixed HeLa cells using UHRF1 antibody (Cat. No. C15410258) (Green) at a 1:500 dilution. Red: Alpha-tubulin filaments. </small></p>
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'url' => 'files/brochures/Epigenetic_Antibodies_Brochure.pdf',
'slug' => 'epigenetic-antibodies-brochure',
'meta_keywords' => '',
'meta_description' => '',
'modified' => '2016-06-15 11:24:06',
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$publication = array(
'id' => '3942',
'name' => 'DNA methylation enzymes and PRC1 restrict B-cell Epstein-Barr virus oncoprotein expression.',
'authors' => 'Guo R, Zhang Y, Teng M, Jiang C, Schineller M, Zhao B, Doench JG, O'Reilly RJ, Cesarman E, Giulino-Roth L, Gewurz BE',
'description' => '<p>To accomplish the remarkable task of lifelong infection, the Epstein-Barr virus (EBV) switches between four viral genome latency and lytic programmes to navigate the B-cell compartment and evade immune responses. The transforming programme, consisting of highly immunogenic EBV nuclear antigen (EBNA) and latent membrane proteins (LMPs), is expressed in newly infected B lymphocytes and in post-transplant lymphomas. On memory cell differentiation and in most EBV-associated Burkitt's lymphomas, all but one viral antigen are repressed for immunoevasion. To gain insights into the epigenetic mechanisms that restrict immunogenic oncoprotein expression, a genome-scale CRISPR-Cas9 screen was performed in EBV and Burkitt's lymphoma cells. Here, we show that the ubiquitin ligase ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1) and its DNA methyltransferase partner DNA methyltransferase I (DNMT1) are critical for the restriction of EBNA and LMP expression. All UHRF1 reader and writer domains were necessary for silencing and DNMT3B was identified as an upstream viral genome CpG methylation initiator. Polycomb repressive complex I exerted a further layer of control over LMP expression, suggesting a second mechanism for latency programme switching. UHRF1, DNMT1 and DNMT3B are upregulated in germinal centre B cells, the Burkitt's lymphoma cell of origin, providing a molecular link between B-cell state and the EBV latency programme. These results suggest rational therapeutic targets to manipulate EBV oncoprotein expression.</p>',
'date' => '2020-05-18',
'pmid' => 'http://www.pubmed.gov/32424339',
'doi' => '10.1038/s41564-020-0724-y',
'modified' => '2020-08-17 10:24:57',
'created' => '2020-08-10 12:12:25',
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'id' => '4616',
'product_id' => '2368',
'publication_id' => '3942'
)
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View::_evaluate() - CORE/Cake/View/View.php, line 971
View::_render() - CORE/Cake/View/View.php, line 933
View::render() - CORE/Cake/View/View.php, line 473
Controller::render() - CORE/Cake/Controller/Controller.php, line 963
ProductsController::slug() - APP/Controller/ProductsController.php, line 1052
ReflectionMethod::invokeArgs() - [internal], line ??
Controller::invokeAction() - CORE/Cake/Controller/Controller.php, line 491
Dispatcher::_invoke() - CORE/Cake/Routing/Dispatcher.php, line 193
Dispatcher::dispatch() - CORE/Cake/Routing/Dispatcher.php, line 167
[main] - APP/webroot/index.php, line 118
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