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Proteintech mouse monoclonal anti parp
Mouse Monoclonal Anti Parp, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 830 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+monoclonal+anti+parp/PARP1+Antibody/10__3390_slash_v18040409-65-92-95
Average 96 stars, based on 830 article reviews

mouse monoclonal anti parp - by Bioz Stars, 2026-10

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Article Title: HHV-6A Drives Epigenetic Reprogramming via an EZH2–SIRT1 Axis to Sustain Mutant p53 and Reshape Oncogenic Inflammatory Signaling
Article Snippet: The following primary antibodies were used: rabbit polyclonal anti-EZH2 (Proteintech, Rosemont, IL, USA, 21800-1-AP); mouse monoclonal anti-H3K27me3 (Sigma-Aldrich, 05-1951-S); mouse monoclonal anti-p53 (clone DO-1; Santa Cruz Biotechnology, Dallas, TX, USA, sc-126); rabbit polyclonal anti-IL-6 (Proteintech, 21865-1-AP); rabbit polyclonal antiacetyl-p53 (Lys382) (St. John’s Laboratory, London, UK, ST598865-20); mouse monoclonal anti-p300 (Santa Cruz Biotechnology, sc-48343); mouse monoclonal anti-TIP60 (Santa Cruz Biotechnology, sc-166323); mouse monoclonal anti-SIRT1 (Proteintech, 60303-1-Ig); mouse monoclonal anti-p-STAT3 (Santa Cruz Biotecnology, B-7, sc-8059); rabbit polyclonal antiSTAT3 (Santa Cruz Biotecnology, C-20, sc-482); rabbit polyclonal anti-PTPN6 (Proteintech, 24546-1-AP); mouse monoclonal anti-c-Myc (Proteintech, 67447-1-Ig); and mouse monoclonal anti-PARP (Proteintech, 66520-1-Ig).

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PARP-1 regulates cartilage degeneration in OA mice. a Genotypes, along with mRNA and protein expression levels of PARP-1, were evaluated in primary cultured chondrocytes isolated from WT and PARP-1 KO mice. b Immunostaining for PARP-1 was performed on the cartilage and synovium of WT and PARP-1 KO mice. Represented data of ( a )( b ) were collected from biological triplicate. c Cartilage degeneration, erosion, and subchondral bone sclerosis/osteophyte formation were evaluated by Safranin-O staining. Quantification of the OARSI grade (d) , osteophyte maturity ( e ), osteophyte size ( f ), and subchondral bone plate thickness ( g ) are presented. h Synovitis was analyzed using hematoxylin and eosin staining. i Quantification of synovitis is shown. WT ( n = 10) or PARP-1 KO ( n = 17) mice were used. All values, derived from the Mann–Whitney U test, are expressed as the mean ± standard error of the mean. Safranin O-stained images of the joint sections are presented, illustrating the whole joint (50X), subchondral bone sclerosis/osteophyte size (100X), and cartilage and synovium (200X). Scale bar: 50 μm. Abbreviations: WT, wild-type; KO, knockout; PARP-1, poly (ADP-ribose) polymerase-1; OARSI, Osteoarthritis Research Society International

Journal: Arthritis Research & Therapy

Article Title: PARP-1 prevents osteoarthritis pathogenesis by inhibiting apoptosis in chondrocytes: an animal study

doi: 10.1186/s13075-026-03728-7

Figure Lengend Snippet: PARP-1 regulates cartilage degeneration in OA mice. a Genotypes, along with mRNA and protein expression levels of PARP-1, were evaluated in primary cultured chondrocytes isolated from WT and PARP-1 KO mice. b Immunostaining for PARP-1 was performed on the cartilage and synovium of WT and PARP-1 KO mice. Represented data of ( a )( b ) were collected from biological triplicate. c Cartilage degeneration, erosion, and subchondral bone sclerosis/osteophyte formation were evaluated by Safranin-O staining. Quantification of the OARSI grade (d) , osteophyte maturity ( e ), osteophyte size ( f ), and subchondral bone plate thickness ( g ) are presented. h Synovitis was analyzed using hematoxylin and eosin staining. i Quantification of synovitis is shown. WT ( n = 10) or PARP-1 KO ( n = 17) mice were used. All values, derived from the Mann–Whitney U test, are expressed as the mean ± standard error of the mean. Safranin O-stained images of the joint sections are presented, illustrating the whole joint (50X), subchondral bone sclerosis/osteophyte size (100X), and cartilage and synovium (200X). Scale bar: 50 μm. Abbreviations: WT, wild-type; KO, knockout; PARP-1, poly (ADP-ribose) polymerase-1; OARSI, Osteoarthritis Research Society International

Article Snippet: Equal amounts of protein (15 μg) were separated by electrophoresis on a 10% sodium dodecyl sulfate-polyacrylamide gel at 60 V for 1 h and 45 min, followed by 100 V for 1 h and 15 min. Proteins were then transferred to membranes and incubated overnight at 4 °C with the following primary antibodies: β-actin mouse monoclonal antibody (1:8000; K200058M, Solarbio Life Science, Beijing, China), PARP-1 mouse monoclonal antibody (1:500; SC-74470, Santa Cruz Biotechnology, Dallas, TX, USA), PAR/pADPr mouse monoclonal antibody (1:1000; 4335-MC-100, Bio-techne R&D Systems, Minneapolis, MN, USA), cleaved caspase-3 rabbit monoclonal antibody (1:1000; 9664, Cell Signaling Technology, Danvers, MA, USA), NOD-like receptor protein 3 (NLRP3) rabbit monoclonal antibody (1:1000; 15101, Cell Signaling Technology), caspase-1 rabbit monoclonal antibody (1:1000; 24232, Cell Signaling Technology), IL-1β rabbit monoclonal antibody (1:1000; 12703, Cell Signaling Technology), nuclear factor κB (NF-κB) p65 rabbit monoclonal antibody (1:1000; 8242, Cell Signaling Technology), phospho-nuclear factor κB (NF-κB) rabbit monoclonal antibody (1:1000; 3033, Cell Signaling Technology), C-Jun N-terminal protein kinase (JNK) mouse monoclonal antibody (1:500; SC-7345, Santa Cruz Biotechnology), and phospho-c-JNK mouse monoclonal antibody (1:500; SC-135642, Santa Cruz Biotechnology).

Techniques: Expressing, Cell Culture, Isolation, Immunostaining, Staining, Derivative Assay, MANN-WHITNEY, Knock-Out

Expression of PARP-1 and its effects on cartilage degeneration in WT and PARP-1 KO. a Expression of PARP-1 was analyzed in cartilage and synovium tissue from WT and PARP-1 KO. Represented images were collected from biological triplicate. TUNEL assay was performed to assess apoptosis in the cartilage ( b ) and synovium ( d ) of WT and PARP-1 KO mice. Quantification of apoptotic cells in cartilage ( c , n = 7) and synovium ( e , n = 4) were presented. All values, derived from the two-tailed Student’s t-test, are expressed as the mean ± standard error of the mean. Scale bar: 50 μm. Abbreviations: WT, wild-type; KO, knockout; PARP-1, poly (ADP-ribose) polymerase-1; TUNEL, terminal deoxynucleotidyl transferase dUTP nick end labeling

Journal: Arthritis Research & Therapy

Article Title: PARP-1 prevents osteoarthritis pathogenesis by inhibiting apoptosis in chondrocytes: an animal study

doi: 10.1186/s13075-026-03728-7

Figure Lengend Snippet: Expression of PARP-1 and its effects on cartilage degeneration in WT and PARP-1 KO. a Expression of PARP-1 was analyzed in cartilage and synovium tissue from WT and PARP-1 KO. Represented images were collected from biological triplicate. TUNEL assay was performed to assess apoptosis in the cartilage ( b ) and synovium ( d ) of WT and PARP-1 KO mice. Quantification of apoptotic cells in cartilage ( c , n = 7) and synovium ( e , n = 4) were presented. All values, derived from the two-tailed Student’s t-test, are expressed as the mean ± standard error of the mean. Scale bar: 50 μm. Abbreviations: WT, wild-type; KO, knockout; PARP-1, poly (ADP-ribose) polymerase-1; TUNEL, terminal deoxynucleotidyl transferase dUTP nick end labeling

Techniques: Expressing, TUNEL Assay, Derivative Assay, Two Tailed Test, Knock-Out

Genetic or pharmaceutical inhibition of PARP-1 increases apoptosis in primary cultured chondrocytes. a MTT assay was performed to evaluate the effect of CHX and 3-AB on chondrocyte viability ( n = 8). Chondrocytes were treated with CHX (25–100 µM), and 3-AB (100 µM) for 24 h. TUNEL assay was performed in primary cultured chondrocytes treated with CHX (50 µM) and 3-AB (100 µM) ( b ), with quantification results presented ( c , n = 6). Western blot analysis was also performed ( d ). Flow cytometry assay with PI/Annexin V was performed in primary cultured chondrocytes treated with CHX (50 µM) and 3-AB (100 µM) ( e ), with quantification results presented ( f , n = 8). Also, PI/Annexin V assay was performed in primary cultured chondrocytes from WT and PARP-1 KO treated with CHX ( g ), and quantification results were shown ( h , n = 8). TUNEL assay was performed in primary cultured chondrocytes from WT and PARP-1 KO treated with CHX ( i ), and quantification results were shown ( j , n = 6). Protein levels of PAPR-1, PAR, and c-caspase-3 were analyzed by Western blotting ( k ). Inflammasome-related factors, including NLRP3, caspase-1, and IL-1β, were also assessed ( l ). Western blotting data were collected from biological triplicate. All values, derived from the two-tailed Student’s t-test, are expressed as the mean ± standard error of the mean. Abbreviations: MTT, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide; CHX, cycloheximide; 3-AB, 3-aminobenzamide; TUNEL, terminal deoxynucleotidyl transferase dUTP nick end labeling; WT, wild-type; KO, knockout; PARP-1, poly (ADP-ribose) polymerase-1; PAR, poly ADP-ribose; c-caspase-3, cleaved caspase-3; NLRP3, nucleotide-binding oligomerization domain, leucine rich repeat and pyrin domain containing 3; IL-1β, interleukin-1 beta

Journal: Arthritis Research & Therapy

Article Title: PARP-1 prevents osteoarthritis pathogenesis by inhibiting apoptosis in chondrocytes: an animal study

doi: 10.1186/s13075-026-03728-7

Figure Lengend Snippet: Genetic or pharmaceutical inhibition of PARP-1 increases apoptosis in primary cultured chondrocytes. a MTT assay was performed to evaluate the effect of CHX and 3-AB on chondrocyte viability ( n = 8). Chondrocytes were treated with CHX (25–100 µM), and 3-AB (100 µM) for 24 h. TUNEL assay was performed in primary cultured chondrocytes treated with CHX (50 µM) and 3-AB (100 µM) ( b ), with quantification results presented ( c , n = 6). Western blot analysis was also performed ( d ). Flow cytometry assay with PI/Annexin V was performed in primary cultured chondrocytes treated with CHX (50 µM) and 3-AB (100 µM) ( e ), with quantification results presented ( f , n = 8). Also, PI/Annexin V assay was performed in primary cultured chondrocytes from WT and PARP-1 KO treated with CHX ( g ), and quantification results were shown ( h , n = 8). TUNEL assay was performed in primary cultured chondrocytes from WT and PARP-1 KO treated with CHX ( i ), and quantification results were shown ( j , n = 6). Protein levels of PAPR-1, PAR, and c-caspase-3 were analyzed by Western blotting ( k ). Inflammasome-related factors, including NLRP3, caspase-1, and IL-1β, were also assessed ( l ). Western blotting data were collected from biological triplicate. All values, derived from the two-tailed Student’s t-test, are expressed as the mean ± standard error of the mean. Abbreviations: MTT, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide; CHX, cycloheximide; 3-AB, 3-aminobenzamide; TUNEL, terminal deoxynucleotidyl transferase dUTP nick end labeling; WT, wild-type; KO, knockout; PARP-1, poly (ADP-ribose) polymerase-1; PAR, poly ADP-ribose; c-caspase-3, cleaved caspase-3; NLRP3, nucleotide-binding oligomerization domain, leucine rich repeat and pyrin domain containing 3; IL-1β, interleukin-1 beta

Techniques: Inhibition, Cell Culture, MTT Assay, TUNEL Assay, Western Blot, Flow Cytometry, Annexin V Assay, Derivative Assay, Two Tailed Test, Knock-Out, Binding Assay

Effect of PARP-1 KO on inflammatory factor-induced expression of anabolic and catabolic factors in chondrocytes. WT and PARP-1 KO chondrocytes were treated with IL-1β ( a ), TNF-α ( b ), IL-6 ( c ), and LPS ( d ) for 24 h. The mRNA expression levels of Sox9, Col2a1, Aggrecan, Mmp3, Mmp13, and Adamts5 were analyzed using conventional RT-PCR, with GADPH serving as an internal control. Represented images were collected from biological triplicate. Abbreviations: WT, wild-type; KO, knockout; IL-1β, interleukin-1 beta; TNF-α, tumor necrosis factor-alpha; IL-6, interleukin-6; LPS, lipopolysaccharide; Sox9, SRY-box transcription factor 9; Col2a1, collagen type II alpha 1 chain; Aggrecan, aggrecan proteoglycan; Mmp3, matrix metalloproteinase 3; Mmp13, matrix metalloproteinase 13; Adamts5, a disintegrin and metalloproteinase with thrombospondin motifs 5; RT-PCR, reverse transcription polymerase chain reaction; and GAPDH, glyceraldehyde 3-phosphate dehydrogenase

Journal: Arthritis Research & Therapy

Article Title: PARP-1 prevents osteoarthritis pathogenesis by inhibiting apoptosis in chondrocytes: an animal study

doi: 10.1186/s13075-026-03728-7

Figure Lengend Snippet: Effect of PARP-1 KO on inflammatory factor-induced expression of anabolic and catabolic factors in chondrocytes. WT and PARP-1 KO chondrocytes were treated with IL-1β ( a ), TNF-α ( b ), IL-6 ( c ), and LPS ( d ) for 24 h. The mRNA expression levels of Sox9, Col2a1, Aggrecan, Mmp3, Mmp13, and Adamts5 were analyzed using conventional RT-PCR, with GADPH serving as an internal control. Represented images were collected from biological triplicate. Abbreviations: WT, wild-type; KO, knockout; IL-1β, interleukin-1 beta; TNF-α, tumor necrosis factor-alpha; IL-6, interleukin-6; LPS, lipopolysaccharide; Sox9, SRY-box transcription factor 9; Col2a1, collagen type II alpha 1 chain; Aggrecan, aggrecan proteoglycan; Mmp3, matrix metalloproteinase 3; Mmp13, matrix metalloproteinase 13; Adamts5, a disintegrin and metalloproteinase with thrombospondin motifs 5; RT-PCR, reverse transcription polymerase chain reaction; and GAPDH, glyceraldehyde 3-phosphate dehydrogenase

Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Control, Knock-Out, Reverse Transcription, Polymerase Chain Reaction

Journal: Arthritis Research & Therapy

Article Title: PARP-1 prevents osteoarthritis pathogenesis by inhibiting apoptosis in chondrocytes: an animal study

doi: 10.1186/s13075-026-03728-7

Article Snippet: Slides were then blocked with 1% BSA and incubated at 4 °C for 12–16 h with a mouse monoclonal antibody against PARP-1 (1:200; SC-74470; Santa Cruz Biotechnology).

Techniques: Expressing, Cell Culture, Isolation, Immunostaining, Staining, Derivative Assay, MANN-WHITNEY, Knock-Out

Journal: Arthritis Research & Therapy

Article Title: PARP-1 prevents osteoarthritis pathogenesis by inhibiting apoptosis in chondrocytes: an animal study

doi: 10.1186/s13075-026-03728-7

Article Snippet: Slides were then blocked with 1% BSA and incubated at 4 °C for 12–16 h with a mouse monoclonal antibody against PARP-1 (1:200; SC-74470; Santa Cruz Biotechnology).

Techniques: Expressing, TUNEL Assay, Derivative Assay, Two Tailed Test, Knock-Out

Journal: Arthritis Research & Therapy

Article Title: PARP-1 prevents osteoarthritis pathogenesis by inhibiting apoptosis in chondrocytes: an animal study

doi: 10.1186/s13075-026-03728-7

Article Snippet: Slides were then blocked with 1% BSA and incubated at 4 °C for 12–16 h with a mouse monoclonal antibody against PARP-1 (1:200; SC-74470; Santa Cruz Biotechnology).

Techniques: Inhibition, Cell Culture, MTT Assay, TUNEL Assay, Western Blot, Flow Cytometry, Annexin V Assay, Derivative Assay, Two Tailed Test, Knock-Out, Binding Assay

Journal: Arthritis Research & Therapy

Article Title: PARP-1 prevents osteoarthritis pathogenesis by inhibiting apoptosis in chondrocytes: an animal study

doi: 10.1186/s13075-026-03728-7

Article Snippet: Slides were then blocked with 1% BSA and incubated at 4 °C for 12–16 h with a mouse monoclonal antibody against PARP-1 (1:200; SC-74470; Santa Cruz Biotechnology).

Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Control, Knock-Out, Reverse Transcription, Polymerase Chain Reaction

PARP14 promotes IFN production following poly(I:C) treatment in human A549 cells. ( A, B ) WT (red bars) and PARP14 knock-out (KO) (green bars) A549 cells were transfected with 0.5 ug/mL poly(I:C), RNA was isolated from cells at 18 hours post-transfection (hpt), and IFN-β ( A ) and IFN-λ ( B ) mRNA levels were quantified by qPCR using the ΔCt method. ( C, D ) WT and PARP14 KO cells were transfected with 0.5 µg/mL poly(I:C). Supernatant was collected 18 hpt, and IFN-β ( C ) and IFN-λ ( D ) protein levels were quantified by ELISA. Data shown in ( A–D ) are from one experiment and are representative of three independent experiments with N = 3 biological replicates for each experiment. ( E ) WT and PARP14 KO cells were either mock-transfected or transfected with 0.5 µg/mL of poly(I:C). Cell lysates were collected at 18 hpt, and OAS3 and PARP14 protein levels were determined by immunoblotting using β-actin as a loading control. ( F ) Band intensities from ( E ) were quantified by densitometry, normalized to β-actin, and then relative levels compared to mock-transfected WT cells were determined. Data shown in ( E, F ) are from one experiment and are representative of three independent experiments with N = 1 biological replicate per group in each experiment. ( G ) WT cells were either mock-transfected or transfected with 0.5 µg/mL of poly(I:C) and were immediately either treated with DMSO (vehicle) or with increasing concentrations of PARP14i (0.01, 0.1, and 1 µM). At 18 hpt, RNA was isolated from cells, and IFN-β mRNA was quantified by qPCR using the ΔCt method. ( H ) WT and PARP14 KO cells were transfected with 0.5 µg of YFP or YFP-PARP14 plasmids. At 48 hpt, cells were transfected with 0.5 µg/mL of poly(I:C), and 18 hours later, RNA was isolated from cells, and IFNβ mRNA was quantified by qPCR using the ΔCt method. ( I ) WT and PARP14 KO cells were transfected with 0.5 µg of YFP or YFP-PARP14 plasmids. At 48 hpt, cells were transfected with 0.5 µg/mL of poly(I:C) and 18 hours later, cell supernatant was used to quantify IFN-β protein by ELISA. Data shown in ( G–I ) are from one experiment and are representative of 2–3 independent experiments with N = 3 biological replicates per group for each experiment. Data in ( A ), ( B ), ( D ), and ( I ) were tested for statistical significance using a standard t -test and data in ( C ), ( G, H ) were tested for statistical significance using one-way analysis of variance (ANOVA).

Journal: mBio

Article Title: PARP14 is an interferon-induced host factor that promotes IFN production and affects the replication of multiple viruses

doi: 10.1128/mbio.02299-25

Figure Lengend Snippet: PARP14 promotes IFN production following poly(I:C) treatment in human A549 cells. ( A, B ) WT (red bars) and PARP14 knock-out (KO) (green bars) A549 cells were transfected with 0.5 ug/mL poly(I:C), RNA was isolated from cells at 18 hours post-transfection (hpt), and IFN-β ( A ) and IFN-λ ( B ) mRNA levels were quantified by qPCR using the ΔCt method. ( C, D ) WT and PARP14 KO cells were transfected with 0.5 µg/mL poly(I:C). Supernatant was collected 18 hpt, and IFN-β ( C ) and IFN-λ ( D ) protein levels were quantified by ELISA. Data shown in ( A–D ) are from one experiment and are representative of three independent experiments with N = 3 biological replicates for each experiment. ( E ) WT and PARP14 KO cells were either mock-transfected or transfected with 0.5 µg/mL of poly(I:C). Cell lysates were collected at 18 hpt, and OAS3 and PARP14 protein levels were determined by immunoblotting using β-actin as a loading control. ( F ) Band intensities from ( E ) were quantified by densitometry, normalized to β-actin, and then relative levels compared to mock-transfected WT cells were determined. Data shown in ( E, F ) are from one experiment and are representative of three independent experiments with N = 1 biological replicate per group in each experiment. ( G ) WT cells were either mock-transfected or transfected with 0.5 µg/mL of poly(I:C) and were immediately either treated with DMSO (vehicle) or with increasing concentrations of PARP14i (0.01, 0.1, and 1 µM). At 18 hpt, RNA was isolated from cells, and IFN-β mRNA was quantified by qPCR using the ΔCt method. ( H ) WT and PARP14 KO cells were transfected with 0.5 µg of YFP or YFP-PARP14 plasmids. At 48 hpt, cells were transfected with 0.5 µg/mL of poly(I:C), and 18 hours later, RNA was isolated from cells, and IFNβ mRNA was quantified by qPCR using the ΔCt method. ( I ) WT and PARP14 KO cells were transfected with 0.5 µg of YFP or YFP-PARP14 plasmids. At 48 hpt, cells were transfected with 0.5 µg/mL of poly(I:C) and 18 hours later, cell supernatant was used to quantify IFN-β protein by ELISA. Data shown in ( G–I ) are from one experiment and are representative of 2–3 independent experiments with N = 3 biological replicates per group for each experiment. Data in ( A ), ( B ), ( D ), and ( I ) were tested for statistical significance using a standard t -test and data in ( C ), ( G, H ) were tested for statistical significance using one-way analysis of variance (ANOVA).

Article Snippet: WT control and PARP14 knockout expanded clones were validated by western blot analysis using anti-PARP14 mouse monoclonal antibody (sc-377150, Santa Cruz Biotechnology).

Techniques: Knock-Out, Transfection, Isolation, Enzyme-linked Immunosorbent Assay, Western Blot, Control

PARP14 promotes IFN production following Mac1 mutant CoV infection. ( A ) Schematic diagram showing the generation of PARP14 KO mice. Parp14 floxed mice were crossed with cre heterozygote mice, and the resulting progeny were used to harvest bone marrow. Bone marrow cells were isolated and plated with 10 ng/mL of mCSF or GM-CSF for 6 days to differentiate cells into M0 macrophages or dendritic cells (DCs), respectively. On day 6, these cells were treated with 1 µg/mL of 4-hydroxy tamoxifen (4-OHT) for 24 hours to induce Cre expression, leading to the removal of exon 2 of Parp14 (for details see Materials and Methods). ( B, C ) Parp14 +/+ (Cre-) (red bars) and Parp14 −/− (Cre+) (green bars) M0 cells ( B ) or DCs ( C ) were infected with MHV WT (solid bars) or N1347A (checkered bars) at an MOI of 0.1. RNA was isolated from cells at 12 hpi, and IFN-β mRNA was quantified by qPCR using the ΔCt method. ( D ) Parp14 +/+ cells were infected with WT and N1347A at an MOI of 0.1 and then treated at 1 hpi with DMSO or increasing concentrations of PARP14 inhibitor (PARP14i) (3, 11, 33, 99, and 297 nM). RNA was isolated from cells at 12 hpi, and IFN-β mRNA levels were quantified using qPCR using the ΔCt method. ( E ) Parp14 +/+ and Parp14 −/− M0 macrophages were infected with WT and N1347A MHV at an MOI of 0.1 and then treated with DMSO or 100 nM PARP14i at 1 hpi. The cell supernatant was collected at 12 hpi, and IFN-β protein was quantified by ELISA. ( F ) A549-ACE2 cells were infected with WT and ΔMac1 SARS-CoV-2 at an MOI of 0.1 and treated with DMSO or PARP14i. RNA was isolated from cells at 48 hpi, and IFN-β, IFN-λ, and CXCL-10 mRNA levels were quantified by qPCR using the ΔCt method. Data shown in ( B–F ) are from one experiment and are representative of three independent experiments with N = 3 biological replicates per group for each experiment. Data in ( B–F) were tested for statistical significance using a one-way ANOVA.

Journal: mBio

Article Title: PARP14 is an interferon-induced host factor that promotes IFN production and affects the replication of multiple viruses

doi: 10.1128/mbio.02299-25

Figure Lengend Snippet: PARP14 promotes IFN production following Mac1 mutant CoV infection. ( A ) Schematic diagram showing the generation of PARP14 KO mice. Parp14 floxed mice were crossed with cre heterozygote mice, and the resulting progeny were used to harvest bone marrow. Bone marrow cells were isolated and plated with 10 ng/mL of mCSF or GM-CSF for 6 days to differentiate cells into M0 macrophages or dendritic cells (DCs), respectively. On day 6, these cells were treated with 1 µg/mL of 4-hydroxy tamoxifen (4-OHT) for 24 hours to induce Cre expression, leading to the removal of exon 2 of Parp14 (for details see Materials and Methods). ( B, C ) Parp14 +/+ (Cre-) (red bars) and Parp14 −/− (Cre+) (green bars) M0 cells ( B ) or DCs ( C ) were infected with MHV WT (solid bars) or N1347A (checkered bars) at an MOI of 0.1. RNA was isolated from cells at 12 hpi, and IFN-β mRNA was quantified by qPCR using the ΔCt method. ( D ) Parp14 +/+ cells were infected with WT and N1347A at an MOI of 0.1 and then treated at 1 hpi with DMSO or increasing concentrations of PARP14 inhibitor (PARP14i) (3, 11, 33, 99, and 297 nM). RNA was isolated from cells at 12 hpi, and IFN-β mRNA levels were quantified using qPCR using the ΔCt method. ( E ) Parp14 +/+ and Parp14 −/− M0 macrophages were infected with WT and N1347A MHV at an MOI of 0.1 and then treated with DMSO or 100 nM PARP14i at 1 hpi. The cell supernatant was collected at 12 hpi, and IFN-β protein was quantified by ELISA. ( F ) A549-ACE2 cells were infected with WT and ΔMac1 SARS-CoV-2 at an MOI of 0.1 and treated with DMSO or PARP14i. RNA was isolated from cells at 48 hpi, and IFN-β, IFN-λ, and CXCL-10 mRNA levels were quantified by qPCR using the ΔCt method. Data shown in ( B–F ) are from one experiment and are representative of three independent experiments with N = 3 biological replicates per group for each experiment. Data in ( B–F) were tested for statistical significance using a one-way ANOVA.

Article Snippet: WT control and PARP14 knockout expanded clones were validated by western blot analysis using anti-PARP14 mouse monoclonal antibody (sc-377150, Santa Cruz Biotechnology).

Techniques: Mutagenesis, Infection, Isolation, Expressing, Enzyme-linked Immunosorbent Assay

PARP14 promotes MDA-5-dependent IFN-β production. ( A ) BMDMs were generated from WT, MAVS −/− , MDA-5 −/− , and RIG-I −/− mice and infected with MHV WT or N1347A at an MOI of 0.1. RNA was isolated from cells at 12 hpi, and IFNβ mRNA was quantified by qPCR using the ΔCt method. ( B ) BMDMs were generated from WT, MAVS −/− , MDA-5 −/− , and RIG-I −/− mice and infected with MHV WT or N1347A at an MOI of 0.1. RNA was isolated from cells at 20 hpi, and MHV-JHM genomic RNA (gRNA) was quantified by qPCR using the ΔCt method. The results shown in ( A ) and ( B ) are from one experiment representative of two independent experiments, each with N = 3 biological replicates per group in each experiment. ( C ) A549 cells were transfected with 0.5 μg/mL of the indicated plasmid. Then either DMSO or 100 nM PARP14i was added to the cells 4 hpt. RNA was isolated from cells at 24 hpt, and IFNβ mRNA was quantified by qPCR using the ΔCt method. IFNβ transcript abundances were calculated relative to DMSO-treated control. ( D, E ) BMDMs ( D ) or A549 cells ( E ) were infected with either SeV at an MOI of 1 or EMCV at an MOI of 2. A 100 nM PARP14i or DMSO was then added at 1 hpi. RNA was isolated from cells at 24 hpi (A549 cells) or 36 hpi (BMDMs), and IFNβ mRNA was quantified by qPCR using the ΔCt method. The results in ( C–E ) are from one experiment representative of three independent experiments, each with N = 3 biological replicates per group for each experiment. All data in ( A ), ( B ), ( D ), and ( E ) were tested for statistical significance using a standard t -test between the indicated samples. Data in ( C ) were tested for statistical significance using a one-way ANOVA.

Journal: mBio

Article Title: PARP14 is an interferon-induced host factor that promotes IFN production and affects the replication of multiple viruses

doi: 10.1128/mbio.02299-25

Figure Lengend Snippet: PARP14 promotes MDA-5-dependent IFN-β production. ( A ) BMDMs were generated from WT, MAVS −/− , MDA-5 −/− , and RIG-I −/− mice and infected with MHV WT or N1347A at an MOI of 0.1. RNA was isolated from cells at 12 hpi, and IFNβ mRNA was quantified by qPCR using the ΔCt method. ( B ) BMDMs were generated from WT, MAVS −/− , MDA-5 −/− , and RIG-I −/− mice and infected with MHV WT or N1347A at an MOI of 0.1. RNA was isolated from cells at 20 hpi, and MHV-JHM genomic RNA (gRNA) was quantified by qPCR using the ΔCt method. The results shown in ( A ) and ( B ) are from one experiment representative of two independent experiments, each with N = 3 biological replicates per group in each experiment. ( C ) A549 cells were transfected with 0.5 μg/mL of the indicated plasmid. Then either DMSO or 100 nM PARP14i was added to the cells 4 hpt. RNA was isolated from cells at 24 hpt, and IFNβ mRNA was quantified by qPCR using the ΔCt method. IFNβ transcript abundances were calculated relative to DMSO-treated control. ( D, E ) BMDMs ( D ) or A549 cells ( E ) were infected with either SeV at an MOI of 1 or EMCV at an MOI of 2. A 100 nM PARP14i or DMSO was then added at 1 hpi. RNA was isolated from cells at 24 hpi (A549 cells) or 36 hpi (BMDMs), and IFNβ mRNA was quantified by qPCR using the ΔCt method. The results in ( C–E ) are from one experiment representative of three independent experiments, each with N = 3 biological replicates per group for each experiment. All data in ( A ), ( B ), ( D ), and ( E ) were tested for statistical significance using a standard t -test between the indicated samples. Data in ( C ) were tested for statistical significance using a one-way ANOVA.

Article Snippet: WT control and PARP14 knockout expanded clones were validated by western blot analysis using anti-PARP14 mouse monoclonal antibody (sc-377150, Santa Cruz Biotechnology).

Techniques: Generated, Infection, Isolation, Transfection, Plasmid Preparation, Control

PARP14 regulates the transcription of dozens of genes with multiple biological functions following MHV-N1347A infection of BMDMs. ( A ) WT BMDMs were infected with N1347A MHV at an MOI of 0.1 and then treated with DMSO or 100 nM PARP14i at 1 hpi. RNA was collected from these cells at 12 hpi, and RNAseq was performed to quantify the transcriptome with and without PARP14i. The ratio of gene expression in the presence or absence of PARP14i treatment was plotted against the minus log 10 value of the P -adjusted value as a volcano plot. ( B ) Gene ontology analysis/pathway enrichment analysis of genes that were identified to be promoted by PARP14 catalytic activity was carried out using the DAVID gene ontology tool. Pathways enriched with a P -value of less than 0.05 were plotted. ( C ) WT BMDMs were infected with MHV N1347A at an MOI of 0.1 and treated with DMSO or 100 nM PARP14i at 1 hpi. RNA was isolated from cells at 12 hpi, and CASP1, FOXO3, and RNF111 mRNAs were quantified by qPCR using the ΔCt method. RNAseq data shown in ( A, B ) are from one experiment with N = 3. Data shown in ( C ) are from one experiment and are representative of two independent experiments with N = 3 biological replicates per group for each experiment. Data in ( C ) were tested for statistical significance using a standard t -test between the indicated samples.

Journal: mBio

Article Title: PARP14 is an interferon-induced host factor that promotes IFN production and affects the replication of multiple viruses

doi: 10.1128/mbio.02299-25

Figure Lengend Snippet: PARP14 regulates the transcription of dozens of genes with multiple biological functions following MHV-N1347A infection of BMDMs. ( A ) WT BMDMs were infected with N1347A MHV at an MOI of 0.1 and then treated with DMSO or 100 nM PARP14i at 1 hpi. RNA was collected from these cells at 12 hpi, and RNAseq was performed to quantify the transcriptome with and without PARP14i. The ratio of gene expression in the presence or absence of PARP14i treatment was plotted against the minus log 10 value of the P -adjusted value as a volcano plot. ( B ) Gene ontology analysis/pathway enrichment analysis of genes that were identified to be promoted by PARP14 catalytic activity was carried out using the DAVID gene ontology tool. Pathways enriched with a P -value of less than 0.05 were plotted. ( C ) WT BMDMs were infected with MHV N1347A at an MOI of 0.1 and treated with DMSO or 100 nM PARP14i at 1 hpi. RNA was isolated from cells at 12 hpi, and CASP1, FOXO3, and RNF111 mRNAs were quantified by qPCR using the ΔCt method. RNAseq data shown in ( A, B ) are from one experiment with N = 3. Data shown in ( C ) are from one experiment and are representative of two independent experiments with N = 3 biological replicates per group for each experiment. Data in ( C ) were tested for statistical significance using a standard t -test between the indicated samples.

Article Snippet: WT control and PARP14 knockout expanded clones were validated by western blot analysis using anti-PARP14 mouse monoclonal antibody (sc-377150, Santa Cruz Biotechnology).

Techniques: Infection, Gene Expression, Activity Assay, Isolation

PARP14 inhibits the replication of Mac1-mutant MHV and SARS-CoV-2. ( A ) Parp14 floxed cre +/− BMDMs were treated with and without 4-OHT. Twenty-four hours later, these cells were infected with WT and N1347A MHV at an MOI of 0.1. At 20 hpi, cells and supernatants were collected, and progeny virus was quantified by plaque assay. Data shown in ( A ) are from one experiment and are representative of two independent experiments with N = 3 biological replicates per group for each experiment. ( B, C ) PARP14 floxed cre + BMDMs ( B ) and DCs ( C ) were treated with or without 4-OHT. Twenty-four hours later, these cells were infected with WT and N1347A MHV at an MOI of 0.1. At 20 hpi, cells and supernatants were collected, and progeny virus was quantified by plaque assay. ( D ) PARP14 +/+ BMDMs and DCs were infected with WT and N1347A MHV at an MOI of 0.1 and then treated with DMSO or PARP14i (1 μM). At 20 hpi, cells and supernatants were collected, and progeny virus was quantified by plaque assay. ( E ) WT A549-ACE2 cells were treated with IFN-γ (50 units) O/N and then infected with WT (red bars) and ΔMac1 (green bars) SARS-CoV-2 at an MOI of 0.1 and treated with DMSO or PARP14i (1 μM) at 1 hpi. At 48 hpi, cells and supernatants were collected and progeny virus was quantified by plaque assay. Data shown in ( B–E ) are from one experiment and are representative of three independent experiments with N = 3 or 4 biological replicates per group for each experiment. Data in ( A–E ) were tested for statistical significance using a one-way ANOVA.

Journal: mBio

Article Title: PARP14 is an interferon-induced host factor that promotes IFN production and affects the replication of multiple viruses

doi: 10.1128/mbio.02299-25

Figure Lengend Snippet: PARP14 inhibits the replication of Mac1-mutant MHV and SARS-CoV-2. ( A ) Parp14 floxed cre +/− BMDMs were treated with and without 4-OHT. Twenty-four hours later, these cells were infected with WT and N1347A MHV at an MOI of 0.1. At 20 hpi, cells and supernatants were collected, and progeny virus was quantified by plaque assay. Data shown in ( A ) are from one experiment and are representative of two independent experiments with N = 3 biological replicates per group for each experiment. ( B, C ) PARP14 floxed cre + BMDMs ( B ) and DCs ( C ) were treated with or without 4-OHT. Twenty-four hours later, these cells were infected with WT and N1347A MHV at an MOI of 0.1. At 20 hpi, cells and supernatants were collected, and progeny virus was quantified by plaque assay. ( D ) PARP14 +/+ BMDMs and DCs were infected with WT and N1347A MHV at an MOI of 0.1 and then treated with DMSO or PARP14i (1 μM). At 20 hpi, cells and supernatants were collected, and progeny virus was quantified by plaque assay. ( E ) WT A549-ACE2 cells were treated with IFN-γ (50 units) O/N and then infected with WT (red bars) and ΔMac1 (green bars) SARS-CoV-2 at an MOI of 0.1 and treated with DMSO or PARP14i (1 μM) at 1 hpi. At 48 hpi, cells and supernatants were collected and progeny virus was quantified by plaque assay. Data shown in ( B–E ) are from one experiment and are representative of three independent experiments with N = 3 or 4 biological replicates per group for each experiment. Data in ( A–E ) were tested for statistical significance using a one-way ANOVA.

Article Snippet: WT control and PARP14 knockout expanded clones were validated by western blot analysis using anti-PARP14 mouse monoclonal antibody (sc-377150, Santa Cruz Biotechnology).

Techniques: Mutagenesis, Infection, Virus, Plaque Assay

PARP14 restricts the replication of HSV-1 in A549 cells. ( A ) WT and PARP14 KO A549 cells were infected with HSV-1 at an MOI of 0.1. Cells and supernatants were collected 24 hpi, and progeny virus was quantified by plaque assay on Vero cells. The results in ( A ) are the combined results of three independent experiments, N = 9 biological replicates per group. ( B ) WT and PARP14 KO A549 cells were infected with HSV-1 at an MOI of 0.1. At 24 hpi, RNA was harvested from infected cells, and HSV-1 immediate early gene ICP4, ICP0, and ICP27 mRNAs were quantified by qPCR using the ΔCt method, having 18S rRNA abundance as the endogenous control. The data in B is from one experiment representative of two independent experiments, N = 3 biological replicates per group for each experiment. ( C ) WT and PARP14 KO A549 cells were infected with serial dilutions of HSV-1 starting at a concentration of 1.85 × 10 9 PFU/mL and overlaid with methylcellulose. At 24 hpi, the plaquing efficiency was determined by counting the number of plaques at each dilution. The data in C is the combined results of three separate experiments, N = 9 biological replicates per group. ( D ) WT A549 cells were treated with 1 µM PARP14 degron control (CTL) or PARP14 degron (DEG) overnight. The cells were then infected with HSV-1 at an MOI of 0.1 PFU/cell. At 24 hpi, cells and supernatants were collected at indicated time points, and progeny virus was quantified by plaque assay. The data in ( D ) is from one experiment representative of two independent experiments, N = 3 biological replicates per group for each experiment. ( E ) WT A549 cells were treated and infected as described in ( D ), at 24 hpi, RNA was harvested from infected cells, and HSV-1 immediate early gene ICP4, ICP0, and ICP27 mRNAs were quantified by qPCR using the ΔCt method, having 18S rRNA abundance as the endogenous control. The data in ( E ) is from one experiment representative of two independent experiments, N = 3 biological replicates per group for each experiment. ( F ) WT A549 cells were infected with HSV-1 at an MOI of 0.1 PFU/cell and then treated with DMSO or PARP14i (1 μM) at 1 hpi. Cells and supernatants were collected at 24 hpi, and progeny virus was quantified by plaque assay. The data in ( F ) are the combined results of two independent experiments, N = 6 biological replicates per group. Data in ( A–D ) were tested for statistical significance using a one-way ANOVA, and data in ( E, F ) were tested for statistical significance using a standard t -test.

Journal: mBio

Article Title: PARP14 is an interferon-induced host factor that promotes IFN production and affects the replication of multiple viruses

doi: 10.1128/mbio.02299-25

Figure Lengend Snippet: PARP14 restricts the replication of HSV-1 in A549 cells. ( A ) WT and PARP14 KO A549 cells were infected with HSV-1 at an MOI of 0.1. Cells and supernatants were collected 24 hpi, and progeny virus was quantified by plaque assay on Vero cells. The results in ( A ) are the combined results of three independent experiments, N = 9 biological replicates per group. ( B ) WT and PARP14 KO A549 cells were infected with HSV-1 at an MOI of 0.1. At 24 hpi, RNA was harvested from infected cells, and HSV-1 immediate early gene ICP4, ICP0, and ICP27 mRNAs were quantified by qPCR using the ΔCt method, having 18S rRNA abundance as the endogenous control. The data in B is from one experiment representative of two independent experiments, N = 3 biological replicates per group for each experiment. ( C ) WT and PARP14 KO A549 cells were infected with serial dilutions of HSV-1 starting at a concentration of 1.85 × 10 9 PFU/mL and overlaid with methylcellulose. At 24 hpi, the plaquing efficiency was determined by counting the number of plaques at each dilution. The data in C is the combined results of three separate experiments, N = 9 biological replicates per group. ( D ) WT A549 cells were treated with 1 µM PARP14 degron control (CTL) or PARP14 degron (DEG) overnight. The cells were then infected with HSV-1 at an MOI of 0.1 PFU/cell. At 24 hpi, cells and supernatants were collected at indicated time points, and progeny virus was quantified by plaque assay. The data in ( D ) is from one experiment representative of two independent experiments, N = 3 biological replicates per group for each experiment. ( E ) WT A549 cells were treated and infected as described in ( D ), at 24 hpi, RNA was harvested from infected cells, and HSV-1 immediate early gene ICP4, ICP0, and ICP27 mRNAs were quantified by qPCR using the ΔCt method, having 18S rRNA abundance as the endogenous control. The data in ( E ) is from one experiment representative of two independent experiments, N = 3 biological replicates per group for each experiment. ( F ) WT A549 cells were infected with HSV-1 at an MOI of 0.1 PFU/cell and then treated with DMSO or PARP14i (1 μM) at 1 hpi. Cells and supernatants were collected at 24 hpi, and progeny virus was quantified by plaque assay. The data in ( F ) are the combined results of two independent experiments, N = 6 biological replicates per group. Data in ( A–D ) were tested for statistical significance using a one-way ANOVA, and data in ( E, F ) were tested for statistical significance using a standard t -test.

Article Snippet: WT control and PARP14 knockout expanded clones were validated by western blot analysis using anti-PARP14 mouse monoclonal antibody (sc-377150, Santa Cruz Biotechnology).

Techniques: Infection, Virus, Plaque Assay, Control, Concentration Assay

PARP14 is required for efficient replication of VSV-GFP in cell culture. ( A ) A549 WT and PARP14 KO cells were infected with VSV-GFP at an MOI of 1. At 10 hpi, cells and supernatants were collected, and progeny virus was quantified by 50% tissue culture infectious dose (TCID 50 ). The results in A are the combined results of four independent experiments, N = 12 biological replicates per group. ( B ) A549-ACE2 WT and PARP14 KO cells were infected with VSV-GFP at 1 MOI and then treated with 1 µM PARP14 degron control (CTL) or PARP14 degron (DEG) at 1 hpi. At 10 hpi, cells and supernatants were collected, and progeny virus was quantified by TCID 50 . The results in ( B ) are from one experiment representative of two independent experiments, N = 3 biological replicates per group for each experiment. ( C ) A549 WT cells were infected with VSV at an MOI of 1 and then treated with DMSO or 100 nM PARP14i (P14i) at 1 hpi. At 10 hpi, cells and supernatants were collected, and progeny virus was quantified by TCID 50 . The results in ( C ) are the combined results of four independent experiments, N = 12 biological replicates per group. Data in ( A ) and ( C ) were tested for statistical significance using a non-parametric t -test, while data in ( B ) were tested for statistical significance using a one-way ANOVA.

Journal: mBio

Article Title: PARP14 is an interferon-induced host factor that promotes IFN production and affects the replication of multiple viruses

doi: 10.1128/mbio.02299-25

Figure Lengend Snippet: PARP14 is required for efficient replication of VSV-GFP in cell culture. ( A ) A549 WT and PARP14 KO cells were infected with VSV-GFP at an MOI of 1. At 10 hpi, cells and supernatants were collected, and progeny virus was quantified by 50% tissue culture infectious dose (TCID 50 ). The results in A are the combined results of four independent experiments, N = 12 biological replicates per group. ( B ) A549-ACE2 WT and PARP14 KO cells were infected with VSV-GFP at 1 MOI and then treated with 1 µM PARP14 degron control (CTL) or PARP14 degron (DEG) at 1 hpi. At 10 hpi, cells and supernatants were collected, and progeny virus was quantified by TCID 50 . The results in ( B ) are from one experiment representative of two independent experiments, N = 3 biological replicates per group for each experiment. ( C ) A549 WT cells were infected with VSV at an MOI of 1 and then treated with DMSO or 100 nM PARP14i (P14i) at 1 hpi. At 10 hpi, cells and supernatants were collected, and progeny virus was quantified by TCID 50 . The results in ( C ) are the combined results of four independent experiments, N = 12 biological replicates per group. Data in ( A ) and ( C ) were tested for statistical significance using a non-parametric t -test, while data in ( B ) were tested for statistical significance using a one-way ANOVA.

Article Snippet: WT control and PARP14 knockout expanded clones were validated by western blot analysis using anti-PARP14 mouse monoclonal antibody (sc-377150, Santa Cruz Biotechnology).

Techniques: Cell Culture, Infection, Virus, Control

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