Histone Deacetylase 1 Plays an Acetylation-Independent Role in Influenza A Virus Replication

Chen, Lin; Wang, Chengmin; Luo, Jing; Su, Wen; Li, Meng; Zhao, Na; Lyu, Wenting; Attaran, H; He, Yapeng; Ding, Hua; He, Hongxuan

doi:10.3389/fimmu.2017.01757

Cited by 12 publications

(10 citation statements)

References 43 publications

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“…However, it seems that downregulation of both HDAC1 and HDAC3 by virus infection was not correlated with the decreased levels of histone H3 acetylation, which emphasized the complexity of the mechanisms for the regulation of histone acetylation following virus infection. It has been reported that HDAC1 regulates influenza A virus (IAV) replication independent of its deacetylation activity [ 41 ]. HDAC1 stimulates host type I interferon antiviral response, therefore IAV infection decreases HDAC1 expression for efficient replication [ 35 ].…”

Section: Discussionmentioning

confidence: 99%

The Involvement of Histone H3 Acetylation in Bovine Herpesvirus 1 Replication in MDBK Cells

Zhu

Jiang

et al. 2018

Viruses

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During bovine herpesvirus 1 (BoHV-1) productive infection in cell cultures, partial of intranuclear viral DNA is present in nucleosomes, and viral protein VP22 associates with histones and decreases histone H4 acetylation, indicating the involvement of histone H4 acetylation in virus replication. In this study, we demonstrated that BoHV-1 infection at the late stage (at 24 h after infection) dramatically decreased histone H3 acetylation [at residues K9 (H3K9ac) and K18 (H3K18ac)], which was supported by the pronounced depletion of histone acetyltransferases (HATs) including CBP/P300 (CREB binding protein and p300), GCN5L2 (general control of amino acid synthesis yeast homolog like 2) and PCAF (P300/CBP-associated factor). The depletion of GCN5L2 promoted by virus infection was partially mediated by ubiquitin-proteasome pathway. Interestingly, the viral replication was enhanced by HAT (histone acetyltransferase) activator CTPB [N-(4-Chloro-3-trifluoromethylphenyl)-2-ethoxy-6-pentadecylbenzamide], and vice versa, inhibited by HAT inhibitor Anacardic acid (AA), suggesting that BoHV-1 may take advantage of histone acetylation for efficient replication. Taken together, we proposed that the HAT-dependent histone H3 acetylation plays an important role in BoHV-1 replication in MDBK (Madin-Darby bovine kidney) cells.

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Section: Discussionmentioning

confidence: 99%

The Involvement of Histone H3 Acetylation in Bovine Herpesvirus 1 Replication in MDBK Cells

Zhu

Jiang

et al. 2018

Viruses

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“…No HDAC1 contains 482 amino acids, identified in 1996 by Taunton et al (17). HDAC1 regulates genes involved in cell differentiation and the cell cycle, and participates in the development of various diseases such as viral infectious diseases, degenerative diseases and cancer (18)(19)(20). HDAC1 can mediate site-specific DNA-binding transcriptional repression and a high level of HDAC1 is observed in tumor invasion and metastasis (21).…”

Section: Expression Of Hdac3 Mrna Clinicopathological ---------------mentioning

confidence: 99%

Clinical significance of HDAC1, -2 and -3 expression levels in esophageal squamous cell carcinoma

Yibulayin

et al. 2020

Exp Ther Med

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The present study analyzed the expression of the histone deacetylase (HDAC) 1, 2 and 3 in primary esophageal squamous cell carcinoma (ESCC) samples and how their levels correlate with clinicopathological parameters. ESCC patients (n=88) in the present study had received no previous treatment before undergoing surgical excision. The mRNA expression of HDAC1,-2 and-3 were detected by semi-quantified PCR in ESCC samples and distal normal samples. The relationship of HDAC1,-2 and-3 expression with clinicopathological parameters was analyzed by χ 2 test. The correlation among these HDACs was analyzed by Pearson's correlation test. Compared with distal normal tissues, ESCC samples had higher expression of HDAC1, but not HDAC2 or HDAC3 (P<0.05). The expression of HDACs was different between Kazak and Han ethnicities. The expression of HDAC2 was correlated with invasion depth (P<0.05), but not with sex, age, metastasis, or the degree of tumor differentiation (P>0.05). There was no association between HDAC1 or HDAC3 and clinicopathological parameters (P>0.05). For the Kazak and Han ethnicities, HDAC1 expression was present in male patients, patients with well/moderate differentiated ESCC and T3 and T4 ESCC (P<0.01). HDAC1 in patients aged <60 was associated with ethnicity (P<0.05). HDAC2 expression was different in positive LN metastasis, well/moderate differentiation and T3 and T4 ESCC (P<0.01). HDAC3 expression in male patients, patients with negative LN metastasis and well/moderate differentiation ESCC was associated with ethnicity (P<0.05). Additionally, the expression levels of HDAC1,-2 and-3 did not correlate with each other. Thus, HDAC1 expression may be used as a risk factor for ESCC and HDAC2 levels may be used to predict invasion depth. The expression of HDAC1,-2 and-3 has ethnic differences.

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“…the nuclear import of NP and suppressing the TBK1-IRF3 signal pathway (Chen et al, 2017) (Table 1 and Figure 2).…”

Section: Ptms Involved In Uncoating and Nuclear Import Of Iav Vrnps Amentioning

confidence: 98%

“…The NP-interacting protein TRIM14 stimulates K48-linked ubiquitination and proteasomal degradation of NP, leading to a reduced efficiency in NP transportation from the cytoplasm to the nucleus and a subsequent inhibition of viral replication ( Wu et al, 2019 ) ( Table 1 and Figure 2 ). Meanwhile, HDAC1 interacts with NP, resulting in a decreased level of NP acetylation, thus facilitating viral replication through promoting the nuclear import of NP and suppressing the TBK1-IRF3 signal pathway ( Chen et al, 2017 ) ( Table 1 and Figure 2 ).…”

Section: Ptms Involved In the Viral Entry Process Of Iavmentioning

confidence: 99%

Role of Post-translational Modifications in Influenza A Virus Life Cycle and Host Innate Immune Response

Zhang

Liu

2020

Front. Microbiol.

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Throughout various stages of its life cycle, influenza A virus relies heavily on host cellular machinery, including the post-translational modifications (PTMs) system. During infection, influenza virus interacts extensively with the cellular PTMs system to aid in its successful infection and dissemination. The complex interplay between viruses and the PTMs system induces global changes in PTMs of the host proteome as well as modifications of specific host or viral proteins. The most common PTMs include phosphorylation, ubiquitination, SUMOylation, acetylation, methylation, NEDDylation, and glycosylation. Many PTMs directly support influenza virus infection, whereas others contribute to modulating antiviral responses. In this review, we describe current knowledge regarding the role of PTMs in different stages of the influenza virus replication cycle. We also discuss the concerted role of PTMs in antagonizing host antiviral responses, with an emphasis on their impact on viral pathogenicity and host range.

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Histone Deacetylase 1 Plays an Acetylation-Independent Role in Influenza A Virus Replication

Cited by 12 publications

References 43 publications

The Involvement of Histone H3 Acetylation in Bovine Herpesvirus 1 Replication in MDBK Cells

The Involvement of Histone H3 Acetylation in Bovine Herpesvirus 1 Replication in MDBK Cells

Clinical significance of HDAC1, -2 and -3 expression levels in esophageal squamous cell carcinoma

Role of Post-translational Modifications in Influenza A Virus Life Cycle and Host Innate Immune Response

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