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HDAC1 was a negative regulator of classical swine fever virus replication in IPEC-J2 and PAM cells. (A–E) Effect of <t>HDAC</t> <t>inhibitors</t> <t>SAHA</t> and MS-275 on CSFV replication in IPEC-J2 cells, shown as Npro protein level by immunoblotting (A) and virus titers (E). Densitometric analysis of HDAC1/β-actin (B), H3k9ac/histone H3 (C), and Npro/β-actin (D) of panel A. (F–J) IPEC-J2 cells transfected with siRNA targeting HDAC1 (siHDAC1) or scramble RNA (siNC) for 12 hours and then infected with CSFV for 36 hours. CSFV Npro, HDAC1, and H3K9ac were detected by immunoblotting (F). Densitometric analysis of HDCA1/β-actin (G), H3k9ac/H3 (H), and Npro/β-actin (I) of panel F, and viral titer (J). (K–O) PAM cells transfected with siHDAC1 or siNC for 12 hours and then infected with CSFV for 36 hours. CSFV Npro, HDAC1, and H3K9ac were detected by immunoblotting (K). Densitometric analysis of HDCA1/β-actin (L), H3k9ac/H3 (M), Npro/β-actin (N) of panel K, and viral titers (O). (P–T) IPEC-J2 cells transfected with pCMV-HDAC1-HA or control vector for 18 hours and then infected with CSFV for 36 hours. (P) Immunoblotting of Npro, HDAC1, and H3K9ac. Densitometric analysis of HDAC1/β-actin (Q), H3k9ac/H3 (R), and Npro/β-actin (S) of panel G and viral titer (T). Data are shown as means ± SD from three independent experiments for panels B–E, G–J, L–O, and Q–T. *, P < 0.05; **, P < 0.01; and ns, not significant.
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HDAC1 was a negative regulator of classical swine fever virus replication in IPEC-J2 and PAM cells. (A–E) Effect of <t>HDAC</t> <t>inhibitors</t> <t>SAHA</t> and MS-275 on CSFV replication in IPEC-J2 cells, shown as Npro protein level by immunoblotting (A) and virus titers (E). Densitometric analysis of HDAC1/β-actin (B), H3k9ac/histone H3 (C), and Npro/β-actin (D) of panel A. (F–J) IPEC-J2 cells transfected with siRNA targeting HDAC1 (siHDAC1) or scramble RNA (siNC) for 12 hours and then infected with CSFV for 36 hours. CSFV Npro, HDAC1, and H3K9ac were detected by immunoblotting (F). Densitometric analysis of HDCA1/β-actin (G), H3k9ac/H3 (H), and Npro/β-actin (I) of panel F, and viral titer (J). (K–O) PAM cells transfected with siHDAC1 or siNC for 12 hours and then infected with CSFV for 36 hours. CSFV Npro, HDAC1, and H3K9ac were detected by immunoblotting (K). Densitometric analysis of HDCA1/β-actin (L), H3k9ac/H3 (M), Npro/β-actin (N) of panel K, and viral titers (O). (P–T) IPEC-J2 cells transfected with pCMV-HDAC1-HA or control vector for 18 hours and then infected with CSFV for 36 hours. (P) Immunoblotting of Npro, HDAC1, and H3K9ac. Densitometric analysis of HDAC1/β-actin (Q), H3k9ac/H3 (R), and Npro/β-actin (S) of panel G and viral titer (T). Data are shown as means ± SD from three independent experiments for panels B–E, G–J, L–O, and Q–T. *, P < 0.05; **, P < 0.01; and ns, not significant.
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HDAC1 was a negative regulator of classical swine fever virus replication in IPEC-J2 and PAM cells. (A–E) Effect of <t>HDAC</t> <t>inhibitors</t> <t>SAHA</t> and MS-275 on CSFV replication in IPEC-J2 cells, shown as Npro protein level by immunoblotting (A) and virus titers (E). Densitometric analysis of HDAC1/β-actin (B), H3k9ac/histone H3 (C), and Npro/β-actin (D) of panel A. (F–J) IPEC-J2 cells transfected with siRNA targeting HDAC1 (siHDAC1) or scramble RNA (siNC) for 12 hours and then infected with CSFV for 36 hours. CSFV Npro, HDAC1, and H3K9ac were detected by immunoblotting (F). Densitometric analysis of HDCA1/β-actin (G), H3k9ac/H3 (H), and Npro/β-actin (I) of panel F, and viral titer (J). (K–O) PAM cells transfected with siHDAC1 or siNC for 12 hours and then infected with CSFV for 36 hours. CSFV Npro, HDAC1, and H3K9ac were detected by immunoblotting (K). Densitometric analysis of HDCA1/β-actin (L), H3k9ac/H3 (M), Npro/β-actin (N) of panel K, and viral titers (O). (P–T) IPEC-J2 cells transfected with pCMV-HDAC1-HA or control vector for 18 hours and then infected with CSFV for 36 hours. (P) Immunoblotting of Npro, HDAC1, and H3K9ac. Densitometric analysis of HDAC1/β-actin (Q), H3k9ac/H3 (R), and Npro/β-actin (S) of panel G and viral titer (T). Data are shown as means ± SD from three independent experiments for panels B–E, G–J, L–O, and Q–T. *, P < 0.05; **, P < 0.01; and ns, not significant.
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HDAC1 was a negative regulator of classical swine fever virus replication in IPEC-J2 and PAM cells. (A–E) Effect of <t>HDAC</t> <t>inhibitors</t> <t>SAHA</t> and MS-275 on CSFV replication in IPEC-J2 cells, shown as Npro protein level by immunoblotting (A) and virus titers (E). Densitometric analysis of HDAC1/β-actin (B), H3k9ac/histone H3 (C), and Npro/β-actin (D) of panel A. (F–J) IPEC-J2 cells transfected with siRNA targeting HDAC1 (siHDAC1) or scramble RNA (siNC) for 12 hours and then infected with CSFV for 36 hours. CSFV Npro, HDAC1, and H3K9ac were detected by immunoblotting (F). Densitometric analysis of HDCA1/β-actin (G), H3k9ac/H3 (H), and Npro/β-actin (I) of panel F, and viral titer (J). (K–O) PAM cells transfected with siHDAC1 or siNC for 12 hours and then infected with CSFV for 36 hours. CSFV Npro, HDAC1, and H3K9ac were detected by immunoblotting (K). Densitometric analysis of HDCA1/β-actin (L), H3k9ac/H3 (M), Npro/β-actin (N) of panel K, and viral titers (O). (P–T) IPEC-J2 cells transfected with pCMV-HDAC1-HA or control vector for 18 hours and then infected with CSFV for 36 hours. (P) Immunoblotting of Npro, HDAC1, and H3K9ac. Densitometric analysis of HDAC1/β-actin (Q), H3k9ac/H3 (R), and Npro/β-actin (S) of panel G and viral titer (T). Data are shown as means ± SD from three independent experiments for panels B–E, G–J, L–O, and Q–T. *, P < 0.05; **, P < 0.01; and ns, not significant.
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HDAC1 was a negative regulator of classical swine fever virus replication in IPEC-J2 and PAM cells. (A–E) Effect of HDAC inhibitors SAHA and MS-275 on CSFV replication in IPEC-J2 cells, shown as Npro protein level by immunoblotting (A) and virus titers (E). Densitometric analysis of HDAC1/β-actin (B), H3k9ac/histone H3 (C), and Npro/β-actin (D) of panel A. (F–J) IPEC-J2 cells transfected with siRNA targeting HDAC1 (siHDAC1) or scramble RNA (siNC) for 12 hours and then infected with CSFV for 36 hours. CSFV Npro, HDAC1, and H3K9ac were detected by immunoblotting (F). Densitometric analysis of HDCA1/β-actin (G), H3k9ac/H3 (H), and Npro/β-actin (I) of panel F, and viral titer (J). (K–O) PAM cells transfected with siHDAC1 or siNC for 12 hours and then infected with CSFV for 36 hours. CSFV Npro, HDAC1, and H3K9ac were detected by immunoblotting (K). Densitometric analysis of HDCA1/β-actin (L), H3k9ac/H3 (M), Npro/β-actin (N) of panel K, and viral titers (O). (P–T) IPEC-J2 cells transfected with pCMV-HDAC1-HA or control vector for 18 hours and then infected with CSFV for 36 hours. (P) Immunoblotting of Npro, HDAC1, and H3K9ac. Densitometric analysis of HDAC1/β-actin (Q), H3k9ac/H3 (R), and Npro/β-actin (S) of panel G and viral titer (T). Data are shown as means ± SD from three independent experiments for panels B–E, G–J, L–O, and Q–T. *, P < 0.05; **, P < 0.01; and ns, not significant.

Journal: Journal of Virology

Article Title: N-terminal domain of classical swine fever virus N pro induces proteasomal degradation of specificity protein 1 with reduced HDAC1 expression to evade from innate immune responses

doi: 10.1128/jvi.01115-23

Figure Lengend Snippet: HDAC1 was a negative regulator of classical swine fever virus replication in IPEC-J2 and PAM cells. (A–E) Effect of HDAC inhibitors SAHA and MS-275 on CSFV replication in IPEC-J2 cells, shown as Npro protein level by immunoblotting (A) and virus titers (E). Densitometric analysis of HDAC1/β-actin (B), H3k9ac/histone H3 (C), and Npro/β-actin (D) of panel A. (F–J) IPEC-J2 cells transfected with siRNA targeting HDAC1 (siHDAC1) or scramble RNA (siNC) for 12 hours and then infected with CSFV for 36 hours. CSFV Npro, HDAC1, and H3K9ac were detected by immunoblotting (F). Densitometric analysis of HDCA1/β-actin (G), H3k9ac/H3 (H), and Npro/β-actin (I) of panel F, and viral titer (J). (K–O) PAM cells transfected with siHDAC1 or siNC for 12 hours and then infected with CSFV for 36 hours. CSFV Npro, HDAC1, and H3K9ac were detected by immunoblotting (K). Densitometric analysis of HDCA1/β-actin (L), H3k9ac/H3 (M), Npro/β-actin (N) of panel K, and viral titers (O). (P–T) IPEC-J2 cells transfected with pCMV-HDAC1-HA or control vector for 18 hours and then infected with CSFV for 36 hours. (P) Immunoblotting of Npro, HDAC1, and H3K9ac. Densitometric analysis of HDAC1/β-actin (Q), H3k9ac/H3 (R), and Npro/β-actin (S) of panel G and viral titer (T). Data are shown as means ± SD from three independent experiments for panels B–E, G–J, L–O, and Q–T. *, P < 0.05; **, P < 0.01; and ns, not significant.

Article Snippet: The chemical inhibitors MS-275 (a selective HDAC inhibitor for HDACs 1 and 3), SAHA (a pan-HDAC inhibitor for HDACs 1, 2, 3, 6, 7, and 11), ammonium chloride (NH 4 Cl), and chloroquine (CQ) were from Selleck (Houston, USA); and MG132, from Beyotime Biotech (Shanghai, China); poly(I:C) and recombinant IFN-λ3 (rIFN-λ3), from Abclonal (Wuhan, China).

Techniques: Virus, Western Blot, Transfection, Infection, Control, Plasmid Preparation