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Biorbyt ebna1 fluorescein isothiocyanate fitc
Ebna1 Fluorescein Isothiocyanate Fitc, supplied by Biorbyt, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Article Title: B Cell-Specific Transcription Activator PAX5 Recruits p300 To Support EBNA1-Driven Transcription
Article Snippet: EBNA1-FITC , Biorbyt , orb4774.

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Antibodies and primers used in this study

Journal: Journal of Virology

Article Title: B Cell-Specific Transcription Activator PAX5 Recruits p300 To Support EBNA1-Driven Transcription

doi: 10.1128/JVI.02028-19

Figure Lengend Snippet: Antibodies and primers used in this study

Article Snippet: EBNA1-FITC , Biorbyt , orb4774.

Techniques: Sequencing

PPI mediated by EBNA1 and PAX5 in vitro and in vivo. (A) The expression plasmids of FPAX5, EBNA1, or EBNA2 were used for transfection-mediated co-IP assays. To avoid nucleic acid-dependent PPI occurring, all of the cells were collected in lysis buffer supplemented with DNase I and RNase A prior to conducting the immunoprecipitation assay for this and all of the following co-IP experiments. M2 agarose-precipitated matrices were blotted for FPAX5, EBNA1, or EBNA2 with the use of 2% input of the lysate as a loading control. (B) The expression plasmids of EBNA1, FPAX5, or FPAX6 were included in the co-IP assay. The immune blots for the indicated proteins are shown. (C) LCL lysate was used to perform co-IP assays using antibodies for EBNA1 (E1), PAX5 (P5), nucleolin (NCL), or IgG control. Western blotting was performed with 2% of the input as loading control. (D) Ni- nitrilotriacetic acid (NTA) Sepharose-bound His-tagged PAX5 (HPAX5) was used as the protein bait to pull down cell lysates derived from LCL or BJAB cells. The HPAX5-bound proteins were identified by immune blot analysis. Five percent input of each protein from the lysates is shown. (E) LCL, BJAB stably expressing Flag-tagged EBNA1 (FEBNA1) (BJAB-FEBNA1), or BJAB cells were used to perform immunofluorescence confocal microscopy. PAX5-stained cells were visualized by a rhodamine-conjugated secondary antibody, whereas the primary EBNA1 antibody was fluorescein isothiocyanate (FITC) conjugated. The nuclei were counterstained with 4′,6-diamidino-2-phenylindole (DAPI).

Journal: Journal of Virology

Article Title: B Cell-Specific Transcription Activator PAX5 Recruits p300 To Support EBNA1-Driven Transcription

doi: 10.1128/JVI.02028-19

Figure Lengend Snippet: PPI mediated by EBNA1 and PAX5 in vitro and in vivo. (A) The expression plasmids of FPAX5, EBNA1, or EBNA2 were used for transfection-mediated co-IP assays. To avoid nucleic acid-dependent PPI occurring, all of the cells were collected in lysis buffer supplemented with DNase I and RNase A prior to conducting the immunoprecipitation assay for this and all of the following co-IP experiments. M2 agarose-precipitated matrices were blotted for FPAX5, EBNA1, or EBNA2 with the use of 2% input of the lysate as a loading control. (B) The expression plasmids of EBNA1, FPAX5, or FPAX6 were included in the co-IP assay. The immune blots for the indicated proteins are shown. (C) LCL lysate was used to perform co-IP assays using antibodies for EBNA1 (E1), PAX5 (P5), nucleolin (NCL), or IgG control. Western blotting was performed with 2% of the input as loading control. (D) Ni- nitrilotriacetic acid (NTA) Sepharose-bound His-tagged PAX5 (HPAX5) was used as the protein bait to pull down cell lysates derived from LCL or BJAB cells. The HPAX5-bound proteins were identified by immune blot analysis. Five percent input of each protein from the lysates is shown. (E) LCL, BJAB stably expressing Flag-tagged EBNA1 (FEBNA1) (BJAB-FEBNA1), or BJAB cells were used to perform immunofluorescence confocal microscopy. PAX5-stained cells were visualized by a rhodamine-conjugated secondary antibody, whereas the primary EBNA1 antibody was fluorescein isothiocyanate (FITC) conjugated. The nuclei were counterstained with 4′,6-diamidino-2-phenylindole (DAPI).

Article Snippet: EBNA1-FITC , Biorbyt , orb4774.

Techniques: In Vitro, In Vivo, Expressing, Transfection, Co-Immunoprecipitation Assay, Lysis, Immunoprecipitation, Control, Western Blot, Derivative Assay, Stable Transfection, Immunofluorescence, Confocal Microscopy, Staining

PAX5 has a critical role in EBNA1/oriP-dependent functions. (A) FPAX5 expression plasmids (10 or 30 μg) were assessed for their effects on either EBNA1/oriP-Luc- or EBNA2/LMP1-Luc-mediated transcription. A cytomegalovirus (CMV)–β-galactosidase (β-Gal) expression vector was used as an internal control. The degree of EBNA1- or EBNA2-dependent transcription was determined as fold activation, where the resulting luciferase activity is corrected by β-Gal activity. The final results were presented as mean ± standard deviation (SD) for data from three experiments for this and all of the following luciferase activity assays. The statistical analysis for the indicated comparison groups to the control was determined by paired Student’s t test, with P < 0.05 (*) versus P > 0.05 (†). (B) BJAB cells were transduced with lentivirus-expressed shPAX5#1 or shPAX5#2 or with shScr control. The immune blots for endogenous PAX5 and actin control are shown. Cells were cotransfected with EBNA1 or FPAX5 and oriP-Luc, as well as with internal control CMV–β-Gal reporter plasmids. Plasmid-expressed EBNA1, FPAX5, and actin control was determined by Western blotting. The EBNA1/oriP-Luc-induced transcription in each sample is presented and compared. (C) EBV-positive Akata BL cells (Akata+), LCL1, LCL2, or IB4 cells (5 × 106) transduced for 72 h with green fluorescent protein (GFP) expression vector, shPAX5#1, shPAX5#2, or shScr control were collected to perform Western blot assays and for the following indicated experiments. (D) Each selected cell line (5 × 103 cells per 100 μl) was aliquoted into a 96-well microtiter plate in triplicate and subjected to a proliferation assay using the trypan blue exclusion method. The effects of PAX5 depletion on the cell growth of two EBV-negative versus four EBV-positive cells lines were compared. The number of viable cells at the indicated time point was determined by cell counting with a hemocytometer. The results from three independent experiments are represented as mean ± SD for each time point.

Journal: Journal of Virology

Article Title: B Cell-Specific Transcription Activator PAX5 Recruits p300 To Support EBNA1-Driven Transcription

doi: 10.1128/JVI.02028-19

Figure Lengend Snippet: PAX5 has a critical role in EBNA1/oriP-dependent functions. (A) FPAX5 expression plasmids (10 or 30 μg) were assessed for their effects on either EBNA1/oriP-Luc- or EBNA2/LMP1-Luc-mediated transcription. A cytomegalovirus (CMV)–β-galactosidase (β-Gal) expression vector was used as an internal control. The degree of EBNA1- or EBNA2-dependent transcription was determined as fold activation, where the resulting luciferase activity is corrected by β-Gal activity. The final results were presented as mean ± standard deviation (SD) for data from three experiments for this and all of the following luciferase activity assays. The statistical analysis for the indicated comparison groups to the control was determined by paired Student’s t test, with P < 0.05 (*) versus P > 0.05 (†). (B) BJAB cells were transduced with lentivirus-expressed shPAX5#1 or shPAX5#2 or with shScr control. The immune blots for endogenous PAX5 and actin control are shown. Cells were cotransfected with EBNA1 or FPAX5 and oriP-Luc, as well as with internal control CMV–β-Gal reporter plasmids. Plasmid-expressed EBNA1, FPAX5, and actin control was determined by Western blotting. The EBNA1/oriP-Luc-induced transcription in each sample is presented and compared. (C) EBV-positive Akata BL cells (Akata+), LCL1, LCL2, or IB4 cells (5 × 106) transduced for 72 h with green fluorescent protein (GFP) expression vector, shPAX5#1, shPAX5#2, or shScr control were collected to perform Western blot assays and for the following indicated experiments. (D) Each selected cell line (5 × 103 cells per 100 μl) was aliquoted into a 96-well microtiter plate in triplicate and subjected to a proliferation assay using the trypan blue exclusion method. The effects of PAX5 depletion on the cell growth of two EBV-negative versus four EBV-positive cells lines were compared. The number of viable cells at the indicated time point was determined by cell counting with a hemocytometer. The results from three independent experiments are represented as mean ± SD for each time point.

Article Snippet: EBNA1-FITC , Biorbyt , orb4774.

Techniques: Expressing, Plasmid Preparation, Control, Activation Assay, Luciferase, Activity Assay, Standard Deviation, Comparison, Transduction, Western Blot, Proliferation Assay, Cell Counting

EBNA1 requires PAX5 to associate with either the oriP or TR-DNA. (A) Schematic diagram of the EBV linear genome. The EBNA1 binding sites within the oriP and the PAX5 binding sites in the TRs are shown. FR, family of repeats; DS, dyad symmetry repeats. The areas targeted by ChIP-quantitative PCR (qPCR) are marked by a pair of arrowheads. (B) Schematic diagrams illustrating two types of the EBV genome derived from Akata +, LCL, and IB4 are shown. (C to H) A series of ChIP assays were performed on the four cell lines with the same treatments as those described in the Fig. 2C legend, using antibodies for PAX5, EBNA1, NCL, or IgG control. The amounts of coimmunoprecipitated TR-DNA, DS-DNA, FR-DNA, CD79a promoter (22), C promoter (Cp), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) promoter from three independent experiments were quantified by qPCR and determined as percentage of input DNA (mean ± SD) for this and all of the following described ChIP assays.

Journal: Journal of Virology

Article Title: B Cell-Specific Transcription Activator PAX5 Recruits p300 To Support EBNA1-Driven Transcription

doi: 10.1128/JVI.02028-19

Figure Lengend Snippet: EBNA1 requires PAX5 to associate with either the oriP or TR-DNA. (A) Schematic diagram of the EBV linear genome. The EBNA1 binding sites within the oriP and the PAX5 binding sites in the TRs are shown. FR, family of repeats; DS, dyad symmetry repeats. The areas targeted by ChIP-quantitative PCR (qPCR) are marked by a pair of arrowheads. (B) Schematic diagrams illustrating two types of the EBV genome derived from Akata +, LCL, and IB4 are shown. (C to H) A series of ChIP assays were performed on the four cell lines with the same treatments as those described in the Fig. 2C legend, using antibodies for PAX5, EBNA1, NCL, or IgG control. The amounts of coimmunoprecipitated TR-DNA, DS-DNA, FR-DNA, CD79a promoter (22), C promoter (Cp), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) promoter from three independent experiments were quantified by qPCR and determined as percentage of input DNA (mean ± SD) for this and all of the following described ChIP assays.

Article Snippet: EBNA1-FITC , Biorbyt , orb4774.

Techniques: Binding Assay, Real-time Polymerase Chain Reaction, Derivative Assay, Control

The PPI induced by EBNA1 and PAX5 is required for EBNA1/oriP-mediated binding and transcription. (A) YN-FPAX5, yellow fluorescent protein (YFP)-C terminus-fused (YC)-FEBNA1 or its deletion mutants, or YC-FNCL control was cotransfected into 293T cells. The resulting protein expression of each BiFC plasmid was identified by Western blotting (left). YN-FPAX5- and YC-FEBNA1-derived plasmids were cotransfected into 293T cells, and the BiFC images were analyzed by immunofluorescence confocal microscopy (middle). Schematic diagrams of FPAX5 and its deletion mutants are shown. The results obtained from the BiFC assays were summarized and presented (right). Y, positive fluorescence signal; N, negative fluorescence signal. (B) The FEBNA1 expression plasmid or each DBD-derived deletion mutant was transfected into BAJB cells. Flag-epitope (M2)-conjugated agarose was used to precipitate either FEBNA1 or its mutant derivatives. The amounts of M2-precipitated FEBNA1 or its mutants or coprecipitated endogenous PAX5 were identified by Western blotting. Input (2%) of each protein from the lysate is shown. (C) The schematic diagrams of FPAX5 and its deletion mutants are shown. BJAB cells cotransfected with the expression plasmids of EBNA1 and FPAX5 or its mutant derivatives were used to perform M2 agarose-mediated co-IP assays. The immune blots for the indicated proteins are shown with 2% of input. (D) BJAB cells cotransfected with the expression plasmids of FPAX5 or two pair domain (PD) mutants, V26G and P80R, and that of EBNA1 were used to perform M2 agarose-mediated co-IP assays. The immune blots for EBNA1, FPAX5, p300, H3K4Me2, and H3K4Me3 are shown with 2% input as the loading control.

Journal: Journal of Virology

Article Title: B Cell-Specific Transcription Activator PAX5 Recruits p300 To Support EBNA1-Driven Transcription

doi: 10.1128/JVI.02028-19

Figure Lengend Snippet: The PPI induced by EBNA1 and PAX5 is required for EBNA1/oriP-mediated binding and transcription. (A) YN-FPAX5, yellow fluorescent protein (YFP)-C terminus-fused (YC)-FEBNA1 or its deletion mutants, or YC-FNCL control was cotransfected into 293T cells. The resulting protein expression of each BiFC plasmid was identified by Western blotting (left). YN-FPAX5- and YC-FEBNA1-derived plasmids were cotransfected into 293T cells, and the BiFC images were analyzed by immunofluorescence confocal microscopy (middle). Schematic diagrams of FPAX5 and its deletion mutants are shown. The results obtained from the BiFC assays were summarized and presented (right). Y, positive fluorescence signal; N, negative fluorescence signal. (B) The FEBNA1 expression plasmid or each DBD-derived deletion mutant was transfected into BAJB cells. Flag-epitope (M2)-conjugated agarose was used to precipitate either FEBNA1 or its mutant derivatives. The amounts of M2-precipitated FEBNA1 or its mutants or coprecipitated endogenous PAX5 were identified by Western blotting. Input (2%) of each protein from the lysate is shown. (C) The schematic diagrams of FPAX5 and its deletion mutants are shown. BJAB cells cotransfected with the expression plasmids of EBNA1 and FPAX5 or its mutant derivatives were used to perform M2 agarose-mediated co-IP assays. The immune blots for the indicated proteins are shown with 2% of input. (D) BJAB cells cotransfected with the expression plasmids of FPAX5 or two pair domain (PD) mutants, V26G and P80R, and that of EBNA1 were used to perform M2 agarose-mediated co-IP assays. The immune blots for EBNA1, FPAX5, p300, H3K4Me2, and H3K4Me3 are shown with 2% input as the loading control.

Article Snippet: EBNA1-FITC , Biorbyt , orb4774.

Techniques: Binding Assay, Control, Expressing, Plasmid Preparation, Western Blot, Derivative Assay, Immunofluorescence, Confocal Microscopy, Fluorescence, Mutagenesis, Transfection, FLAG-tag, Co-Immunoprecipitation Assay

The p300 recruitment to the oriP DNA is PAX5 dependent. (A) BJAB cells cotransfected with EBNA1 or control vector (−), and the oriP plasmid were subjected to a ChIP analysis using antibodies for EBNA1 (E1), PAX5, or IgG control. The abundance of coimmunoprecipitated oriP DNA by each antibody is shown. The statistical analysis for the indicated comparison groups was determined by paired Student’s t test for this and all of the following ChIP assays; P < 0.05 (*) versus P > 0.05 (†). (B) BJAB cells cotransfected with FPAX5 or each of its point mutants along with the oriP plasmid were coimmunoprecipitated for M2 or IgG control. The binding activity of EBNA1 or the association of FPAX5 or its point mutants with the oriP was determined by qPCR as their enrichment at the oriP DNA. The immune blots for plasmid-expressed proteins or the internal GAPDH control are shown. (C) BJAB-shPAX5#1 or BJAB-shScr cells were cotransfected with EBNA1 or control vector and TR plasmid. The abundance of TR-DNA coimmunoprecipitated by each antibody is shown. (D) BJAB cells cotransfected with FPAX5 or its point mutants were coimmunoprecipitated for M2 or IgG control. The binding activity of FPAX5 or its point mutants to the TRs was determined by qPCR as their enrichment at the TR-DNA. (E) The phenotypes of FPAX5 and its mutants in binding to EBNA1, p300, H3K4Me3, and TRs are summarized. (F) Aliquots (5 × 106 cells) of an LCL were used to perform immunoprecipitation assays for EBNA1, PAX5, and IgG control, respectively. The cell lysates were pretreated with DNase/RNase prior to performing the experiment. The precipitated proteins were identified by immunoblotting analysis using antibodies for EBNA1 (E1), PAX5, p300, H3K4Me2, and H3K4Me3, respectively. (G) Aliquots (5 × 106 cells) of an LCL were used to perform a ChIP assay using the indicated antibodies. The amounts of coimmunoprecipitated oriP DNA or TR-DNA were determined as the percentage of input DNA ± SD. The enrichment of each protein at the oriP DNA or TR-DNA in PAX5-deplected cells versus the control was compared by statistical analysis.

Journal: Journal of Virology

Article Title: B Cell-Specific Transcription Activator PAX5 Recruits p300 To Support EBNA1-Driven Transcription

doi: 10.1128/JVI.02028-19

Figure Lengend Snippet: The p300 recruitment to the oriP DNA is PAX5 dependent. (A) BJAB cells cotransfected with EBNA1 or control vector (−), and the oriP plasmid were subjected to a ChIP analysis using antibodies for EBNA1 (E1), PAX5, or IgG control. The abundance of coimmunoprecipitated oriP DNA by each antibody is shown. The statistical analysis for the indicated comparison groups was determined by paired Student’s t test for this and all of the following ChIP assays; P < 0.05 (*) versus P > 0.05 (†). (B) BJAB cells cotransfected with FPAX5 or each of its point mutants along with the oriP plasmid were coimmunoprecipitated for M2 or IgG control. The binding activity of EBNA1 or the association of FPAX5 or its point mutants with the oriP was determined by qPCR as their enrichment at the oriP DNA. The immune blots for plasmid-expressed proteins or the internal GAPDH control are shown. (C) BJAB-shPAX5#1 or BJAB-shScr cells were cotransfected with EBNA1 or control vector and TR plasmid. The abundance of TR-DNA coimmunoprecipitated by each antibody is shown. (D) BJAB cells cotransfected with FPAX5 or its point mutants were coimmunoprecipitated for M2 or IgG control. The binding activity of FPAX5 or its point mutants to the TRs was determined by qPCR as their enrichment at the TR-DNA. (E) The phenotypes of FPAX5 and its mutants in binding to EBNA1, p300, H3K4Me3, and TRs are summarized. (F) Aliquots (5 × 106 cells) of an LCL were used to perform immunoprecipitation assays for EBNA1, PAX5, and IgG control, respectively. The cell lysates were pretreated with DNase/RNase prior to performing the experiment. The precipitated proteins were identified by immunoblotting analysis using antibodies for EBNA1 (E1), PAX5, p300, H3K4Me2, and H3K4Me3, respectively. (G) Aliquots (5 × 106 cells) of an LCL were used to perform a ChIP assay using the indicated antibodies. The amounts of coimmunoprecipitated oriP DNA or TR-DNA were determined as the percentage of input DNA ± SD. The enrichment of each protein at the oriP DNA or TR-DNA in PAX5-deplected cells versus the control was compared by statistical analysis.

Article Snippet: EBNA1-FITC , Biorbyt , orb4774.

Techniques: Control, Plasmid Preparation, Comparison, Binding Assay, Activity Assay, Immunoprecipitation, Western Blot

PAX5 recruits p300 to support EBNA1/oriP-mediated transcription. (A) The schematic diagrams of two mini-EBV episome reporter plasmids, oriP-nLuc and oriP-TRs-nLuc. Each reporter plasmid was cotransfected with the expression plasmids of EBNA1 and FPAX5 or control into BJAB cells. EBNA1-dependent transcription was verified by the detected nonlytic luciferase activity produced by the reporter plasmid. (B) BJAB cells depleted for PAX5 or shScr control were cotransfected with the expression vectors of EBNA1, FPAX5, or FPAX5 point mutants with the indicated reporter plasmid. The resulting nonlytic nLuc activity was assayed at 24 h posttransfection. (C) BJAB-shPAX5#1 transfected with EBNA1, FPAX5 or its point mutants, and the oriP-nLuc plasmid were subjected to ChIP assays using the indicated antibody. The amounts of coimmunoprecipitated oriP DNA or TR-DNA were quantified by qPCR. The abundance of coimmunoprecipitated-DNA was determined as the percentage of input ± SD. (D) The same experimental procedure described above was carried out, except the oriP-nLuc was replaced by oriP-TRs-nLuc. (E) BJAB cells depleted for PAX5 or shScr control were used to perform a transfection-mediated ChIP assay. The enrichment of EBNA1, endogenous PAX5, transfected FPAX5 and/or its mutants, p300, H3K4Me2, and H3K4Me3 at the oriP DNA or TR-DNA of the oriP-TRs-nLuc reporter plasmid was quantified by qPCR following the same protocols described elsewhere.

Journal: Journal of Virology

Article Title: B Cell-Specific Transcription Activator PAX5 Recruits p300 To Support EBNA1-Driven Transcription

doi: 10.1128/JVI.02028-19

Figure Lengend Snippet: PAX5 recruits p300 to support EBNA1/oriP-mediated transcription. (A) The schematic diagrams of two mini-EBV episome reporter plasmids, oriP-nLuc and oriP-TRs-nLuc. Each reporter plasmid was cotransfected with the expression plasmids of EBNA1 and FPAX5 or control into BJAB cells. EBNA1-dependent transcription was verified by the detected nonlytic luciferase activity produced by the reporter plasmid. (B) BJAB cells depleted for PAX5 or shScr control were cotransfected with the expression vectors of EBNA1, FPAX5, or FPAX5 point mutants with the indicated reporter plasmid. The resulting nonlytic nLuc activity was assayed at 24 h posttransfection. (C) BJAB-shPAX5#1 transfected with EBNA1, FPAX5 or its point mutants, and the oriP-nLuc plasmid were subjected to ChIP assays using the indicated antibody. The amounts of coimmunoprecipitated oriP DNA or TR-DNA were quantified by qPCR. The abundance of coimmunoprecipitated-DNA was determined as the percentage of input ± SD. (D) The same experimental procedure described above was carried out, except the oriP-nLuc was replaced by oriP-TRs-nLuc. (E) BJAB cells depleted for PAX5 or shScr control were used to perform a transfection-mediated ChIP assay. The enrichment of EBNA1, endogenous PAX5, transfected FPAX5 and/or its mutants, p300, H3K4Me2, and H3K4Me3 at the oriP DNA or TR-DNA of the oriP-TRs-nLuc reporter plasmid was quantified by qPCR following the same protocols described elsewhere.

Article Snippet: EBNA1-FITC , Biorbyt , orb4774.

Techniques: Plasmid Preparation, Expressing, Control, Luciferase, Activity Assay, Produced, Transfection

PAX5 is implicated in the maintenance of the genome copy number of the mini-EBV episome and EBV genome in specified BJAB derivative cell lines. (A) BJAB-FE1/oriP-TRs-nLuc or (B) BJAB-B95.8 cells were transduced with lentivirus-expressed shPAX5#1. The growth curve for each cell line with shPAX5#1 or control shScr transduction from 0 to 120 h is shown. The stable copy number of the oriP-TRs-nLuc plasmid and the EBV genome at 0 to120 h posttransduction were quantified by qPCR. The immune blots for EBNA1, PAX5, and GAPDH control are shown. (C) The BJAB-FE1/oriP-TRs-nLuc stable clone was transduced with shPAX5#1 for 72 h. Cells were then collected and transfected with FPAX5 or its mutants and incubated for another 24 h. The genome copy number of oriP-TRs-nLuc was determined by qPCR as the relative amount versus the genomic GAPDH DNA. The obtained genome copy number for oriP-TRs-nLuc in shScr transduced cells was set to 1 for the subsequent comparative analyses. (D) The proposed model depicting EBNA1/PAX5-mediated transcription from the EBV epigenome is shown.

Journal: Journal of Virology

Article Title: B Cell-Specific Transcription Activator PAX5 Recruits p300 To Support EBNA1-Driven Transcription

doi: 10.1128/JVI.02028-19

Figure Lengend Snippet: PAX5 is implicated in the maintenance of the genome copy number of the mini-EBV episome and EBV genome in specified BJAB derivative cell lines. (A) BJAB-FE1/oriP-TRs-nLuc or (B) BJAB-B95.8 cells were transduced with lentivirus-expressed shPAX5#1. The growth curve for each cell line with shPAX5#1 or control shScr transduction from 0 to 120 h is shown. The stable copy number of the oriP-TRs-nLuc plasmid and the EBV genome at 0 to120 h posttransduction were quantified by qPCR. The immune blots for EBNA1, PAX5, and GAPDH control are shown. (C) The BJAB-FE1/oriP-TRs-nLuc stable clone was transduced with shPAX5#1 for 72 h. Cells were then collected and transfected with FPAX5 or its mutants and incubated for another 24 h. The genome copy number of oriP-TRs-nLuc was determined by qPCR as the relative amount versus the genomic GAPDH DNA. The obtained genome copy number for oriP-TRs-nLuc in shScr transduced cells was set to 1 for the subsequent comparative analyses. (D) The proposed model depicting EBNA1/PAX5-mediated transcription from the EBV epigenome is shown.

Article Snippet: EBNA1-FITC , Biorbyt , orb4774.

Techniques: Transduction, Control, Plasmid Preparation, Stable Transfection, Transfection, Incubation

Journal: Journal of Virology

Article Title: B Cell-Specific Transcription Activator PAX5 Recruits p300 To Support EBNA1-Driven Transcription

doi: 10.1128/JVI.02028-19

Figure Lengend Snippet: Antibodies and primers used in this study

Article Snippet: EBNA1-FITC , Biorbyt , orb4774.

Techniques: Sequencing

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