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mouse anti ebna1 antibody (Santa Cruz Biotechnology)

Name: mouse anti ebna1 antibody
Brand: Santa Cruz Biotechnology
Rating: 94 (54 reviews)

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Santa Cruz Biotechnology mouse anti ebna1 antibody
(A-D) HH514-16 BL cells were seeded at 2 × 10 5 /ml. After 24 hours, cells were exposed to varying concentrations of LLL12B (STAT3 inhibitor; A), APTO-253 (MYC inhibitor; B), and VK-1727 <t>(EBNA1</t> inhibitor; C) for 48 hours. Cells were then collected and analyzed by immunoblotting.

(A-D) HH514-16 BL cells were seeded at 2 × 10 5 /ml. After 24 hours, cells were exposed to varying concentrations of LLL12B (STAT3 inhibitor; A), APTO-253 (MYC inhibitor; B), and VK-1727 <t>(EBNA1</t> inhibitor; C) for 48 hours. Cells were then collected and analyzed by immunoblotting.

Mouse Anti Ebna1 Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 54 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse anti ebna1 antibody - by Bioz Stars, 2026-02

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1) Product Images from "STAT3, MYC, and EBNA1 cooperate through a ZC3H18 transcriptional network to regulate survival and proliferation of EBV-positive lymphomas"

Article Title: STAT3, MYC, and EBNA1 cooperate through a ZC3H18 transcriptional network to regulate survival and proliferation of EBV-positive lymphomas

Journal: PLOS Pathogens

doi: 10.1371/journal.ppat.1013166

Figure Legend Snippet: (A-D) HH514-16 BL cells were seeded at 2 × 10 5 /ml. After 24 hours, cells were exposed to varying concentrations of LLL12B (STAT3 inhibitor; A), APTO-253 (MYC inhibitor; B), and VK-1727 (EBNA1 inhibitor; C) for 48 hours. Cells were then collected and analyzed by immunoblotting.

Techniques Used: Western Blot

(A-F) One million HH514-16 BL cells were transfected with two siRNAs targeting each STAT3 (A, D), c-MYC (B, E), or BKRF1 (EBNA1; C, F) versus control siRNA. After 24 hours, cells were collected for immunoblotting with indicated antibodies (A-C) or subjected to RT-qPCR to analyze ZC3H18 , STAT3 , c-MYC , and EBNA1 transcript levels (D-F). (G) One million EBV - BJAB cells were transfected with two siRNAs targeting STAT3 versus control siRNA. After 24 hours, cells were collected for RT-qPCR to analyze STAT3 , c-MYC and ZC3H18 transcript levels. (H) One million cells were seeded at 5 × 10 5 /ml and harvested 24 hours later. The abundance of STAT3 and c-MYC transcripts was analyzed by RT-qPCR in EBV - BJAB, EBV - Akata BL, and EBV + Akata BL cells. (I) STAT3, MYC and EBNA1 plasmids were transfected into EBV - BJAB, EBV - Akata BL, and EBV + Akata BL cells. After 48 hours, cells were collected for RT-qPCR to assess the abundance of ZC3H18 , STAT3 , c-MYC and EBNA1 transcripts. Error bars, SEM of 3 technical replicates; *, p < 0.05; **, p < 0.01; ***, p < 0.001 (versus control); NS, not significant; experiments were performed two to four times.

Figure Legend Snippet: (A-F) One million HH514-16 BL cells were transfected with two siRNAs targeting each STAT3 (A, D), c-MYC (B, E), or BKRF1 (EBNA1; C, F) versus control siRNA. After 24 hours, cells were collected for immunoblotting with indicated antibodies (A-C) or subjected to RT-qPCR to analyze ZC3H18 , STAT3 , c-MYC , and EBNA1 transcript levels (D-F). (G) One million EBV - BJAB cells were transfected with two siRNAs targeting STAT3 versus control siRNA. After 24 hours, cells were collected for RT-qPCR to analyze STAT3 , c-MYC and ZC3H18 transcript levels. (H) One million cells were seeded at 5 × 10 5 /ml and harvested 24 hours later. The abundance of STAT3 and c-MYC transcripts was analyzed by RT-qPCR in EBV - BJAB, EBV - Akata BL, and EBV + Akata BL cells. (I) STAT3, MYC and EBNA1 plasmids were transfected into EBV - BJAB, EBV - Akata BL, and EBV + Akata BL cells. After 48 hours, cells were collected for RT-qPCR to assess the abundance of ZC3H18 , STAT3 , c-MYC and EBNA1 transcripts. Error bars, SEM of 3 technical replicates; *, p < 0.05; **, p < 0.01; ***, p < 0.001 (versus control); NS, not significant; experiments were performed two to four times.

Techniques Used: Transfection, Control, Western Blot, Quantitative RT-PCR

(A-I) One million LCL were seeded at 5 × 10 5 /ml. After 24 hours, cells were transfected with control siRNA or two siRNAs targeting each STAT3 (A, B) or BKRF1 (EBNA1; C, D). After another 24 hours, cells were collected for immunoblotting with indicated antibodies (A, C) or RT-qPCR (B, D) to measure c-MYC transcript levels. (E, H) Four million LCL were subjected to ChIP with indicated antibodies or control IgG followed by qPCR with primers targeting the c-MYC (E), STAT3 (H), and EBNA1 (H) promoters. Data were normalized to IgG; error bars represent SEM of technical replicates. The experiment was performed twice. (F, G) One million LCL were transduced with lenti-shControl (shCtrl) or lenti-shZC3H18 (shZC3H18#1, #2) for 7 days and then analyzed by RT-qPCR to quantify STAT3 , c-MYC , EBNA1 , and BZLF1 transcripts (F) or immunoblotting to confirm depletion of ZC3H18 (G). (I) Four million LCL were subjected to ChIP using indicated antibodies or control IgG. Precipitated DNA was subjected to qPCR analysis with primers targeting promoter regions of EBNA1 promoters Cp, Wp, or Qp. Data were normalized to input. Error bars, SEM of 3 technical replicates; *, p < 0.05; **, p < 0.01; ***, p < 0.001 (versus control); NS, not significant; experiments were performed twice.

Figure Legend Snippet: (A-I) One million LCL were seeded at 5 × 10 5 /ml. After 24 hours, cells were transfected with control siRNA or two siRNAs targeting each STAT3 (A, B) or BKRF1 (EBNA1; C, D). After another 24 hours, cells were collected for immunoblotting with indicated antibodies (A, C) or RT-qPCR (B, D) to measure c-MYC transcript levels. (E, H) Four million LCL were subjected to ChIP with indicated antibodies or control IgG followed by qPCR with primers targeting the c-MYC (E), STAT3 (H), and EBNA1 (H) promoters. Data were normalized to IgG; error bars represent SEM of technical replicates. The experiment was performed twice. (F, G) One million LCL were transduced with lenti-shControl (shCtrl) or lenti-shZC3H18 (shZC3H18#1, #2) for 7 days and then analyzed by RT-qPCR to quantify STAT3 , c-MYC , EBNA1 , and BZLF1 transcripts (F) or immunoblotting to confirm depletion of ZC3H18 (G). (I) Four million LCL were subjected to ChIP using indicated antibodies or control IgG. Precipitated DNA was subjected to qPCR analysis with primers targeting promoter regions of EBNA1 promoters Cp, Wp, or Qp. Data were normalized to input. Error bars, SEM of 3 technical replicates; *, p < 0.05; **, p < 0.01; ***, p < 0.001 (versus control); NS, not significant; experiments were performed twice.

Techniques Used: Transfection, Control, Western Blot, Quantitative RT-PCR, Transduction

(A-C) HH514-16 BL cells were seeded at 5 × 10 5 /ml. After 24 hours, 4 million cells were subjected to ChIP using indicated antibodies or control IgG. Precipitated DNA was subjected to qPCR analysis with primers targeting indicated promoters (A), EBNA1 promoters Cp, Wp, or Qp (B), or gene body regions of c-MYC or ZC3H18 (C). Data were normalized to input. Error bars, SEM of 3 technical replicates; *, p < 0.05; **, p < 0.01; ***, p < 0.001 (versus control); NS, not significant; experiments were performed twice.

Figure Legend Snippet: (A-C) HH514-16 BL cells were seeded at 5 × 10 5 /ml. After 24 hours, 4 million cells were subjected to ChIP using indicated antibodies or control IgG. Precipitated DNA was subjected to qPCR analysis with primers targeting indicated promoters (A), EBNA1 promoters Cp, Wp, or Qp (B), or gene body regions of c-MYC or ZC3H18 (C). Data were normalized to input. Error bars, SEM of 3 technical replicates; *, p < 0.05; **, p < 0.01; ***, p < 0.001 (versus control); NS, not significant; experiments were performed twice.

Techniques Used: Control

STAT3, in EBV-infected B cells, localizes to the nucleus to regulate the expression of multiple genes, including MYC and BKRF1 (EBNA1), which in turn promote the expression of the transcription factor ZC3H18. ZC3H18 transcriptionally regulates STAT3, c-MYC, and EBNA1 while also contributing to NF-κB components even in the absence of LMP1, thereby contributing to cell survival and proliferation.

Figure Legend Snippet: STAT3, in EBV-infected B cells, localizes to the nucleus to regulate the expression of multiple genes, including MYC and BKRF1 (EBNA1), which in turn promote the expression of the transcription factor ZC3H18. ZC3H18 transcriptionally regulates STAT3, c-MYC, and EBNA1 while also contributing to NF-κB components even in the absence of LMP1, thereby contributing to cell survival and proliferation.

Techniques Used: Infection, Expressing

Image Search Results

Journal: PLOS Pathogens

Article Title: STAT3, MYC, and EBNA1 cooperate through a ZC3H18 transcriptional network to regulate survival and proliferation of EBV-positive lymphomas

doi: 10.1371/journal.ppat.1013166

Figure Lengend Snippet: (A-D) HH514-16 BL cells were seeded at 2 × 10 5 /ml. After 24 hours, cells were exposed to varying concentrations of LLL12B (STAT3 inhibitor; A), APTO-253 (MYC inhibitor; B), and VK-1727 (EBNA1 inhibitor; C) for 48 hours. Cells were then collected and analyzed by immunoblotting.

Article Snippet: The following antibodies were used for immunostaining: rabbit anti-STAT3 antibody (4904S, Cell Signaling Technology), mouse anti-EBNA1 antibody (sc-81581, Santa Cruz Biotechnology), rabbit anti-MYC antibody (A190-105A, Bethyl Laboratories), mouse anti-β-actin antibody (clone AC-15) (A1978, Sigma-Aldrich), rabbit anti-phospho-IκBα (Ser32) antibody (2859S, Cell Signaling Technology), rabbit anti-IκBα antibody (9242S, Cell Signaling Technology), rabbit anti-p65 antibody (8242S, Cell Signaling Technology), rabbit anti-p50 antibody (13586, Cell Signaling Technology), rabbit anti-ZC3H18 antibody (A304-682A, Bethyl Laboratories), rabbit anti-Caspase 3 antibody (GTX110543, GeneTex), mouse anti-Cyclin A antibody (sc-53228, Santa Cruz Biotechnology), rabbit anti-Cyclin B antibody (4138S, Cell Signaling Technology), rabbit anti-Cyclin E antibody (A301-566, Bethyl Laboratories), mouse anti-ZEBRA antibody (sc-53904, Santa Cruz Biotechnology), rabbit anti-PCNA antibody (A300-276, Bethyl Laboratories), HRP-conjugated goat anti-mouse IgG (626520, Thermo Fisher Scientific), and HRP-conjugated goat anti-rabbit IgG (31460, Thermo Fisher Scientific).

Techniques: Western Blot

Journal: PLOS Pathogens

Article Title: STAT3, MYC, and EBNA1 cooperate through a ZC3H18 transcriptional network to regulate survival and proliferation of EBV-positive lymphomas

doi: 10.1371/journal.ppat.1013166

Figure Lengend Snippet: (A-F) One million HH514-16 BL cells were transfected with two siRNAs targeting each STAT3 (A, D), c-MYC (B, E), or BKRF1 (EBNA1; C, F) versus control siRNA. After 24 hours, cells were collected for immunoblotting with indicated antibodies (A-C) or subjected to RT-qPCR to analyze ZC3H18 , STAT3 , c-MYC , and EBNA1 transcript levels (D-F). (G) One million EBV - BJAB cells were transfected with two siRNAs targeting STAT3 versus control siRNA. After 24 hours, cells were collected for RT-qPCR to analyze STAT3 , c-MYC and ZC3H18 transcript levels. (H) One million cells were seeded at 5 × 10 5 /ml and harvested 24 hours later. The abundance of STAT3 and c-MYC transcripts was analyzed by RT-qPCR in EBV - BJAB, EBV - Akata BL, and EBV + Akata BL cells. (I) STAT3, MYC and EBNA1 plasmids were transfected into EBV - BJAB, EBV - Akata BL, and EBV + Akata BL cells. After 48 hours, cells were collected for RT-qPCR to assess the abundance of ZC3H18 , STAT3 , c-MYC and EBNA1 transcripts. Error bars, SEM of 3 technical replicates; *, p < 0.05; **, p < 0.01; ***, p < 0.001 (versus control); NS, not significant; experiments were performed two to four times.

Techniques: Transfection, Control, Western Blot, Quantitative RT-PCR

Journal: PLOS Pathogens

Article Title: STAT3, MYC, and EBNA1 cooperate through a ZC3H18 transcriptional network to regulate survival and proliferation of EBV-positive lymphomas

doi: 10.1371/journal.ppat.1013166

Figure Lengend Snippet: (A-I) One million LCL were seeded at 5 × 10 5 /ml. After 24 hours, cells were transfected with control siRNA or two siRNAs targeting each STAT3 (A, B) or BKRF1 (EBNA1; C, D). After another 24 hours, cells were collected for immunoblotting with indicated antibodies (A, C) or RT-qPCR (B, D) to measure c-MYC transcript levels. (E, H) Four million LCL were subjected to ChIP with indicated antibodies or control IgG followed by qPCR with primers targeting the c-MYC (E), STAT3 (H), and EBNA1 (H) promoters. Data were normalized to IgG; error bars represent SEM of technical replicates. The experiment was performed twice. (F, G) One million LCL were transduced with lenti-shControl (shCtrl) or lenti-shZC3H18 (shZC3H18#1, #2) for 7 days and then analyzed by RT-qPCR to quantify STAT3 , c-MYC , EBNA1 , and BZLF1 transcripts (F) or immunoblotting to confirm depletion of ZC3H18 (G). (I) Four million LCL were subjected to ChIP using indicated antibodies or control IgG. Precipitated DNA was subjected to qPCR analysis with primers targeting promoter regions of EBNA1 promoters Cp, Wp, or Qp. Data were normalized to input. Error bars, SEM of 3 technical replicates; *, p < 0.05; **, p < 0.01; ***, p < 0.001 (versus control); NS, not significant; experiments were performed twice.

Techniques: Transfection, Control, Western Blot, Quantitative RT-PCR, Transduction

Journal: PLOS Pathogens

Article Title: STAT3, MYC, and EBNA1 cooperate through a ZC3H18 transcriptional network to regulate survival and proliferation of EBV-positive lymphomas

doi: 10.1371/journal.ppat.1013166

Figure Lengend Snippet: (A-C) HH514-16 BL cells were seeded at 5 × 10 5 /ml. After 24 hours, 4 million cells were subjected to ChIP using indicated antibodies or control IgG. Precipitated DNA was subjected to qPCR analysis with primers targeting indicated promoters (A), EBNA1 promoters Cp, Wp, or Qp (B), or gene body regions of c-MYC or ZC3H18 (C). Data were normalized to input. Error bars, SEM of 3 technical replicates; *, p < 0.05; **, p < 0.01; ***, p < 0.001 (versus control); NS, not significant; experiments were performed twice.

Techniques: Control

Journal: PLOS Pathogens

Article Title: STAT3, MYC, and EBNA1 cooperate through a ZC3H18 transcriptional network to regulate survival and proliferation of EBV-positive lymphomas

doi: 10.1371/journal.ppat.1013166

Figure Lengend Snippet: STAT3, in EBV-infected B cells, localizes to the nucleus to regulate the expression of multiple genes, including MYC and BKRF1 (EBNA1), which in turn promote the expression of the transcription factor ZC3H18. ZC3H18 transcriptionally regulates STAT3, c-MYC, and EBNA1 while also contributing to NF-κB components even in the absence of LMP1, thereby contributing to cell survival and proliferation.

Techniques: Infection, Expressing

CetB selectively induces G1-arrest and early apoptosis of EBV-infected B lymphoma cells without activation of lytic replication (A) Cytotoxicity of CetB on EBV-infected (BL41-B95.8, DG75-EBV, Akata-EBV, and LCL) and -uninfected (BL41, DG75, Akata, and BJAB) B lymphoma cell lines. Cells (5 × 10 3 ) were seeded in a 96-well plate (100 μL per well) and treated with different concentrations of CetB, as indicated, for 48 h. The percentage of cell viability was measured by CCK-8 staining, and compared with that of the untreated group. (B) CetB selectively induces G1 arrest of EBV-infected B lymphoma cells. Cells treated with 0.5, 1, or 2 μM CetB for 24 h, as indicated, were analyzed by flow cytometry after propidium iodide staining. Untreated (mock) and DMSO were used as parallel controls. The percentages of G1, S, and G2/M populations were quantified from triplicate experiments. (C) CetB dramatically enhanced early apoptosis of EBV-infected but not -uninfected B lymphoma cells. Cells treated with or without 1 or 2 μM CetB for 24 h, as indicated, were analyzed by flow cytometry after FITC-Annexin V and propidium iodide staining. The percentages of early apoptotic cells (positive for only Annexin V) or late apoptotic cells (positive for only PI) are highlighted. The relative fold change of early and late apoptosis of each cell line after CetB treatment is shown in the bottom panel. (D) CetB induces cytotoxicity and blocks production of EBV viral particles. LCL or BL41-B95.8 cells (5 × 10 3 ) were seeded in a 96-well plate (100 μL per well) and treated with different concentrations of CetB, as indicated, for 48 h, with three replicate wells per experimental group. The CetB-induced cell cytotoxicity was measured by a live cell counter and presented as the relative percentage compared to the untreated group. The viral particles in culture supernatant were detected by quantitative PCR, and are presented as the relative percentage compared to the untreated group. (E) CetB reduced the expression of EBNA1 without activating ZTA expression. Immunoblotting results of LCL cells treated with CetB from (C). The LCL cells treated with TPA and sodium butyrate (T and B), and BJAB cells were used as controls.

Journal: iScience

Article Title: A small molecule that selectively inhibits the growth of Epstein-Barr virus-latently infected cancer cells

doi: 10.1016/j.isci.2024.110581

Figure Lengend Snippet: CetB selectively induces G1-arrest and early apoptosis of EBV-infected B lymphoma cells without activation of lytic replication (A) Cytotoxicity of CetB on EBV-infected (BL41-B95.8, DG75-EBV, Akata-EBV, and LCL) and -uninfected (BL41, DG75, Akata, and BJAB) B lymphoma cell lines. Cells (5 × 10 3 ) were seeded in a 96-well plate (100 μL per well) and treated with different concentrations of CetB, as indicated, for 48 h. The percentage of cell viability was measured by CCK-8 staining, and compared with that of the untreated group. (B) CetB selectively induces G1 arrest of EBV-infected B lymphoma cells. Cells treated with 0.5, 1, or 2 μM CetB for 24 h, as indicated, were analyzed by flow cytometry after propidium iodide staining. Untreated (mock) and DMSO were used as parallel controls. The percentages of G1, S, and G2/M populations were quantified from triplicate experiments. (C) CetB dramatically enhanced early apoptosis of EBV-infected but not -uninfected B lymphoma cells. Cells treated with or without 1 or 2 μM CetB for 24 h, as indicated, were analyzed by flow cytometry after FITC-Annexin V and propidium iodide staining. The percentages of early apoptotic cells (positive for only Annexin V) or late apoptotic cells (positive for only PI) are highlighted. The relative fold change of early and late apoptosis of each cell line after CetB treatment is shown in the bottom panel. (D) CetB induces cytotoxicity and blocks production of EBV viral particles. LCL or BL41-B95.8 cells (5 × 10 3 ) were seeded in a 96-well plate (100 μL per well) and treated with different concentrations of CetB, as indicated, for 48 h, with three replicate wells per experimental group. The CetB-induced cell cytotoxicity was measured by a live cell counter and presented as the relative percentage compared to the untreated group. The viral particles in culture supernatant were detected by quantitative PCR, and are presented as the relative percentage compared to the untreated group. (E) CetB reduced the expression of EBNA1 without activating ZTA expression. Immunoblotting results of LCL cells treated with CetB from (C). The LCL cells treated with TPA and sodium butyrate (T and B), and BJAB cells were used as controls.

Article Snippet: Mouse monoclonal anti-EBNA1 , Santa Cruz , sc-57719, Clone 0211.

Techniques: Infection, Activation Assay, CCK-8 Assay, Staining, Flow Cytometry, Real-time Polymerase Chain Reaction, Expressing, Western Blot

CetB impairs the protein stability of EBNA1 not its transcripts in EBV-infected LCL cells (A) CetB induces caspase -mediated EBNA1 degradation. LCL cells were treated with different concentrations of CetB for 48 h in the presence or absence of caspase 3/7 inhibitor (Z-DEVD-FMK, 200 μg/mL) as indicated in the figure, followed by immunoblotting with EBNA1 antibody. GAPDH was used as an internal control. (B) CetB reduces protein stability of EBNA1. LCL cells treated with or without CetB (0.19μM) for 6 h, were subjected to cycloheximide (CHX, 200 μg/mL) treatment for the indicated time before harvesting and lysing for immunoblotting (IB). The relative density of EBNA1 was quantified and shown at the bottom panel. (C) CetB does not impair the transcripts of EBNA1. LCL cells treated with different concentrations of CetB for 48 h were subjected to quantitative PCR analysis for EBNA1 transcripts. GAPDH was used as an internal control. n.s., non-significant.

Journal: iScience

Article Title: A small molecule that selectively inhibits the growth of Epstein-Barr virus-latently infected cancer cells

doi: 10.1016/j.isci.2024.110581

Figure Lengend Snippet: CetB impairs the protein stability of EBNA1 not its transcripts in EBV-infected LCL cells (A) CetB induces caspase -mediated EBNA1 degradation. LCL cells were treated with different concentrations of CetB for 48 h in the presence or absence of caspase 3/7 inhibitor (Z-DEVD-FMK, 200 μg/mL) as indicated in the figure, followed by immunoblotting with EBNA1 antibody. GAPDH was used as an internal control. (B) CetB reduces protein stability of EBNA1. LCL cells treated with or without CetB (0.19μM) for 6 h, were subjected to cycloheximide (CHX, 200 μg/mL) treatment for the indicated time before harvesting and lysing for immunoblotting (IB). The relative density of EBNA1 was quantified and shown at the bottom panel. (C) CetB does not impair the transcripts of EBNA1. LCL cells treated with different concentrations of CetB for 48 h were subjected to quantitative PCR analysis for EBNA1 transcripts. GAPDH was used as an internal control. n.s., non-significant.

Article Snippet: Mouse monoclonal anti-EBNA1 , Santa Cruz , sc-57719, Clone 0211.

Techniques: Infection, Western Blot, Control, Real-time Polymerase Chain Reaction

CetB selectively inhibits the in vitro proliferation of EBV-infected cells derived from patients with B cell lymphoma (A) Inhibitory effects of CetB on the proliferation of B lymphoma cells infected with wild-type EBV strain. Top panels , the immunoblotting analysis of BJAB cells infected with wild-type EBV from the plasma of patients with hemophagocytic syndrome. The whole cell lysates extracted at 7 days post infection were subjected to immunoblotting, as indicated. Middle panels , the BJAB cells infected with wild-type EBV strains from the top panel were individually treated with CetB at different dosages (0, 0.1, 0.5, 1, and 2 μM) for 0, 1, 2, 3, 4, 5, and 6 days. The cell number was quantified using a live cell counter. The EBV viral copy number per mL in the plasma of each patient (P1, P2, P3, P4, and P5) is shown in the top panels. The percentage of BJAB cells with EBV infection were quantified by EBNA1-positive staining and shown at the bottom panel. The representative immunofluorescent staining of EBNA1 was shown in the <xref ref-type=

Figure S3 . The LCL cells treated with TPA and sodium butyrate (T and B), and BJAB cells were used as controls. (B) CetB dramatically reduced the viability of PBMCs from patients with EBV-positive B cell lymphoma. PBMCs (1 million per mL) from patients with EBV-positive (P#1 to P#4) and negative (P#5 to P#8) diffuse large B cell lymphoma (DLBCL) were individually cultured in a 6-well plate and treated with different final concentrations of CetB (0, 0.5, 1, and 2 μM) for 48 h, before counting with a live cell counter to determine the viability. The presented data are from duplicated experiments. (C) CetB selectively inhibits the B cell but not T cell population in PBMCs from patients with EBV-positive B cell lymphoma. PBMCs from patients with EBV-positive and -negative diffuse large B cell lymphoma were subjected to CetB treatment for 24 h, followed by flow cytometry analysis with FITC-CD3 and BV510-CD20 staining for T cells and B cells, respectively. The relative fold change of the B cell population in each patient after CetB treatment is shown in the bottom panel. " width="100%" height="100%">

Journal: iScience

Article Title: A small molecule that selectively inhibits the growth of Epstein-Barr virus-latently infected cancer cells

doi: 10.1016/j.isci.2024.110581

Figure Lengend Snippet: CetB selectively inhibits the in vitro proliferation of EBV-infected cells derived from patients with B cell lymphoma (A) Inhibitory effects of CetB on the proliferation of B lymphoma cells infected with wild-type EBV strain. Top panels , the immunoblotting analysis of BJAB cells infected with wild-type EBV from the plasma of patients with hemophagocytic syndrome. The whole cell lysates extracted at 7 days post infection were subjected to immunoblotting, as indicated. Middle panels , the BJAB cells infected with wild-type EBV strains from the top panel were individually treated with CetB at different dosages (0, 0.1, 0.5, 1, and 2 μM) for 0, 1, 2, 3, 4, 5, and 6 days. The cell number was quantified using a live cell counter. The EBV viral copy number per mL in the plasma of each patient (P1, P2, P3, P4, and P5) is shown in the top panels. The percentage of BJAB cells with EBV infection were quantified by EBNA1-positive staining and shown at the bottom panel. The representative immunofluorescent staining of EBNA1 was shown in the Figure S3 . The LCL cells treated with TPA and sodium butyrate (T and B), and BJAB cells were used as controls. (B) CetB dramatically reduced the viability of PBMCs from patients with EBV-positive B cell lymphoma. PBMCs (1 million per mL) from patients with EBV-positive (P#1 to P#4) and negative (P#5 to P#8) diffuse large B cell lymphoma (DLBCL) were individually cultured in a 6-well plate and treated with different final concentrations of CetB (0, 0.5, 1, and 2 μM) for 48 h, before counting with a live cell counter to determine the viability. The presented data are from duplicated experiments. (C) CetB selectively inhibits the B cell but not T cell population in PBMCs from patients with EBV-positive B cell lymphoma. PBMCs from patients with EBV-positive and -negative diffuse large B cell lymphoma were subjected to CetB treatment for 24 h, followed by flow cytometry analysis with FITC-CD3 and BV510-CD20 staining for T cells and B cells, respectively. The relative fold change of the B cell population in each patient after CetB treatment is shown in the bottom panel.

Article Snippet: Mouse monoclonal anti-EBNA1 , Santa Cruz , sc-57719, Clone 0211.

Techniques: In Vitro, Infection, Derivative Assay, Western Blot, Staining, Cell Culture, Flow Cytometry

Journal: iScience

Article Title: A small molecule that selectively inhibits the growth of Epstein-Barr virus-latently infected cancer cells

doi: 10.1016/j.isci.2024.110581

Figure Lengend Snippet:

Article Snippet: Mouse monoclonal anti-EBNA1 , Santa Cruz , sc-57719, Clone 0211.

Techniques: Recombinant, Software, Imaging

Comparative visualization of Kaposi Sarcoma (KS) from the Ocular Surface and Control Samples: (A) Macroscopic view of the ocular surface affected by KS. (B) Histological examination at low magnification (X4) of the KS lesion, stained with hematoxylin and eosin. (C) Detailed histological view at higher magnification (X20) derived from Image panel (B) . (D) Immunohistochemical (IHC) analysis. LANA positivity in the ocular KS lesion, utilizing Abcam’s Rat anti-LANA primary antibody. (E) IHC control for LANA with a KS-negative skin biopsy. (F) Magnified view emphasizing endothelial cell markers CD31 with positive IHC staining in the ocular KS lesion. (G) IHC depiction revealing EBNA1 positivity in the KS lesion, employing Abcam’s mouse anti-EBNA1 primary antibody. The image exhibits both diffuse and punctate nuclear staining patterns. (H) IHC analysis using Abcam’s mouse anti-EBNA1 primary antibody, indicating EBNA1 absence in a skin biopsy without KS. (I) Mouse isotype control for IHC. (J) IHC representation highlighting EBNA1 positivity in the ocular KS lesion, using Invitrogen’s mouse anti-EBNA1 primary antibody. The staining presents a punctate nuclear pattern. (K) IHC examination employing Invitrogen’s mouse anti-EBNA1 primary antibody, demonstrating the absence of EBNA1 in a skin biopsy without KS. (L) IHC analysis with the CD20 antibody, confirming the lack of B cells in the KS lesion. All digital microscopic images of the stained slides were captured using the MoticEasyScan Pro 6 scanner (Motic, USA) and analyzed using the Motic DSAssistant VM 3.0 software. For the journal presentation, images were cropped to a 500x500 pixel resolution using Microsoft’s Paint 3D software.

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Co-infection and co-localization of Kaposi sarcoma-associated herpesvirus and Epstein-Barr virus in HIV-associated Kaposi sarcoma: a case report

doi: 10.3389/fcimb.2023.1270935

Figure Lengend Snippet: Comparative visualization of Kaposi Sarcoma (KS) from the Ocular Surface and Control Samples: (A) Macroscopic view of the ocular surface affected by KS. (B) Histological examination at low magnification (X4) of the KS lesion, stained with hematoxylin and eosin. (C) Detailed histological view at higher magnification (X20) derived from Image panel (B) . (D) Immunohistochemical (IHC) analysis. LANA positivity in the ocular KS lesion, utilizing Abcam’s Rat anti-LANA primary antibody. (E) IHC control for LANA with a KS-negative skin biopsy. (F) Magnified view emphasizing endothelial cell markers CD31 with positive IHC staining in the ocular KS lesion. (G) IHC depiction revealing EBNA1 positivity in the KS lesion, employing Abcam’s mouse anti-EBNA1 primary antibody. The image exhibits both diffuse and punctate nuclear staining patterns. (H) IHC analysis using Abcam’s mouse anti-EBNA1 primary antibody, indicating EBNA1 absence in a skin biopsy without KS. (I) Mouse isotype control for IHC. (J) IHC representation highlighting EBNA1 positivity in the ocular KS lesion, using Invitrogen’s mouse anti-EBNA1 primary antibody. The staining presents a punctate nuclear pattern. (K) IHC examination employing Invitrogen’s mouse anti-EBNA1 primary antibody, demonstrating the absence of EBNA1 in a skin biopsy without KS. (L) IHC analysis with the CD20 antibody, confirming the lack of B cells in the KS lesion. All digital microscopic images of the stained slides were captured using the MoticEasyScan Pro 6 scanner (Motic, USA) and analyzed using the Motic DSAssistant VM 3.0 software. For the journal presentation, images were cropped to a 500x500 pixel resolution using Microsoft’s Paint 3D software.

Article Snippet: Anti-EBV nuclear antigen/EBNA1 mouse monoclonal antibody E1-2.5 (ab8329, Abcam, USA) was used at 1/1000 dilution, and anti-EBV nuclear antigen/EBNA1 mouse monoclonal antibody EBS-I-024 (MA5-33321, Invitrogen, USA) was used at 1/200 dilution.

Techniques: Staining, Derivative Assay, Immunohistochemistry, Software

DNA Polymerase Chain Reaction (PCR) analysis of Kaposi Sarcoma (KS) tumor from the ocular surface: DNA was extracted from frozen tissue samples of the KS tumor for PCR analysis. (A) PCR detecting Kaposi sarcoma-associated herpesvirus (KSHV) using Latency-Associated Nuclear Antigen (LANA) primers. Case: Patient sample demonstrating KSHV positivity. Positive Control: BC3 cell line, known to be infected solely by KSHV. Negative Control: Water. (B) PCR detecting Epstein Barr virus (EBV) using Epstein Barr virus Nuclear Antigen-1 (EBNA1) primers. Case: Patient sample showing EBV positivity. Positive Control: Akata cell line, known to be infected solely by EBV. Negative Controls: Akata31 cell line, normal skin, and water.

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Co-infection and co-localization of Kaposi sarcoma-associated herpesvirus and Epstein-Barr virus in HIV-associated Kaposi sarcoma: a case report

doi: 10.3389/fcimb.2023.1270935

Figure Lengend Snippet: DNA Polymerase Chain Reaction (PCR) analysis of Kaposi Sarcoma (KS) tumor from the ocular surface: DNA was extracted from frozen tissue samples of the KS tumor for PCR analysis. (A) PCR detecting Kaposi sarcoma-associated herpesvirus (KSHV) using Latency-Associated Nuclear Antigen (LANA) primers. Case: Patient sample demonstrating KSHV positivity. Positive Control: BC3 cell line, known to be infected solely by KSHV. Negative Control: Water. (B) PCR detecting Epstein Barr virus (EBV) using Epstein Barr virus Nuclear Antigen-1 (EBNA1) primers. Case: Patient sample showing EBV positivity. Positive Control: Akata cell line, known to be infected solely by EBV. Negative Controls: Akata31 cell line, normal skin, and water.

Techniques: Polymerase Chain Reaction, Positive Control, Infection, Negative Control, Virus

Immunofluorescence Assay (IFA) showing the colocalization of the Kaposi sarcoma-associated herpesvirus-encoded latency-associated nuclear antigen (LANA) protein and Epstein Barr virus’s nuclear antigen 1 (EBNA1) with endothelial cell markers, specifically CD31. (A–F) (Using EBNA1 from Abcam): (A) Nuclear staining with DAPI. (B) Overlay image of DAPI and LANA, denoting the presence of KSHV within the cell nucleus. (C) Overlay image of DAPI and EBNA1 (Abcam antibody), indicating the presence of EBV within the cell nucleus. (D) Overlay image of DAPI and CD31, emphasizing that the tumor cells exhibit endothelial cell markers. (E) Tri-overlay of A, B, and C, illustrating the colocalization of EBNA1 and LANA within tumor cells. (F) Quad-overlay of A, B, C, and D, highlighting the colocalization of EBNA1 and LANA in CD31-positive tumor cells. (G–L) (Using EBNA1 from Invitrogen): (G) Nuclear staining with DAPI. (H) Overlay image of DAPI and LANA, denoting the presence of KSHV within the cell nucleus. (I) Overlay image of DAPI and EBNA1 (Invitrogen antibody), indicating the presence of EBV within the cell nucleus. (J) Overlay image of DAPI and CD31, emphasizing that the tumor cells exhibit endothelial cell markers. (K) Tri-overlay of G, H, and I, illustrating the colocalization of EBNA1 and LANA within tumor cells. (L) Quad-overlay of G, H, I, and J, highlighting the colocalization of EBNA1 and LANA in CD31-positive tumor cells. All images were captured at 40X magnification with a KEYENCE microscope and analyzed using the KEYENCE BZ-X800 Analyzer. For journal presentation, images were cropped to a 300x300 pixel resolution using Microsoft’s Paint 3D software.

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Co-infection and co-localization of Kaposi sarcoma-associated herpesvirus and Epstein-Barr virus in HIV-associated Kaposi sarcoma: a case report

doi: 10.3389/fcimb.2023.1270935

Figure Lengend Snippet: Immunofluorescence Assay (IFA) showing the colocalization of the Kaposi sarcoma-associated herpesvirus-encoded latency-associated nuclear antigen (LANA) protein and Epstein Barr virus’s nuclear antigen 1 (EBNA1) with endothelial cell markers, specifically CD31. (A–F) (Using EBNA1 from Abcam): (A) Nuclear staining with DAPI. (B) Overlay image of DAPI and LANA, denoting the presence of KSHV within the cell nucleus. (C) Overlay image of DAPI and EBNA1 (Abcam antibody), indicating the presence of EBV within the cell nucleus. (D) Overlay image of DAPI and CD31, emphasizing that the tumor cells exhibit endothelial cell markers. (E) Tri-overlay of A, B, and C, illustrating the colocalization of EBNA1 and LANA within tumor cells. (F) Quad-overlay of A, B, C, and D, highlighting the colocalization of EBNA1 and LANA in CD31-positive tumor cells. (G–L) (Using EBNA1 from Invitrogen): (G) Nuclear staining with DAPI. (H) Overlay image of DAPI and LANA, denoting the presence of KSHV within the cell nucleus. (I) Overlay image of DAPI and EBNA1 (Invitrogen antibody), indicating the presence of EBV within the cell nucleus. (J) Overlay image of DAPI and CD31, emphasizing that the tumor cells exhibit endothelial cell markers. (K) Tri-overlay of G, H, and I, illustrating the colocalization of EBNA1 and LANA within tumor cells. (L) Quad-overlay of G, H, I, and J, highlighting the colocalization of EBNA1 and LANA in CD31-positive tumor cells. All images were captured at 40X magnification with a KEYENCE microscope and analyzed using the KEYENCE BZ-X800 Analyzer. For journal presentation, images were cropped to a 300x300 pixel resolution using Microsoft’s Paint 3D software.

Techniques: Immunofluorescence, Staining, Microscopy, Software

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Co-infection and co-localization of Kaposi sarcoma-associated herpesvirus and Epstein-Barr virus in HIV-associated Kaposi sarcoma: a case report

doi: 10.3389/fcimb.2023.1270935

Article Snippet: IFA for EBV was carried out using anti-EBNA1 mouse monoclonal antibodies from Abcam and Invitrogen as primary antibodies, and anti-LANA Rat monoclonal antibody LN53 was used as a primary antibody against KSHV.

Techniques: Staining, Derivative Assay, Immunohistochemistry, Software

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Co-infection and co-localization of Kaposi sarcoma-associated herpesvirus and Epstein-Barr virus in HIV-associated Kaposi sarcoma: a case report

doi: 10.3389/fcimb.2023.1270935

Techniques: Polymerase Chain Reaction, Positive Control, Infection, Negative Control, Virus

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Co-infection and co-localization of Kaposi sarcoma-associated herpesvirus and Epstein-Barr virus in HIV-associated Kaposi sarcoma: a case report

doi: 10.3389/fcimb.2023.1270935

Techniques: Immunofluorescence, Staining, Microscopy, Software

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Co-infection and co-localization of Kaposi sarcoma-associated herpesvirus and Epstein-Barr virus in HIV-associated Kaposi sarcoma: a case report

doi: 10.3389/fcimb.2023.1270935

Techniques: Staining, Derivative Assay, Immunohistochemistry, Software

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Co-infection and co-localization of Kaposi sarcoma-associated herpesvirus and Epstein-Barr virus in HIV-associated Kaposi sarcoma: a case report

doi: 10.3389/fcimb.2023.1270935

Techniques: Polymerase Chain Reaction, Positive Control, Infection, Negative Control, Virus

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Co-infection and co-localization of Kaposi sarcoma-associated herpesvirus and Epstein-Barr virus in HIV-associated Kaposi sarcoma: a case report

doi: 10.3389/fcimb.2023.1270935

Techniques: Immunofluorescence, Staining, Microscopy, Software

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