NDLI: Histone deacetylase inhibitor Scriptaid reactivates latent HIV-1 promoter by inducing histone modification in in vitro latency cell lines.

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Histone deacetylase inhibitor Scriptaid reactivates latent HIV-1 promoter by inducing histone modification in in vitro latency cell lines.

Content Provider	Semantic Scholar
Author	Ying, Hao Zhang, Yuhao Lin, Shiguan Han, Yefei Zhu, Huan-Zhang
Copyright Year	2010
Abstract	Human immunodeficiency virus type 1 (HIV-1) latency remains a major problem for the eradication of viruses in infected individuals undergoing highly active anti-retroviral therapy. By inhibiting HIV-1 gene expression and virus production, histone deacetylase (HDAC) may contribute to the quiescence of HIV-1 within resting CD4+ T cells. A novel HDAC inhibitor, Scriptaid, has been found to have robust activity and lower toxicity compared to trichostatin A (TSA). We therefore investigated Scriptaid for its capability to reverse HIV-1 latency by inducing HIV-1 activation in the Jurkat T cell line containing latent HIV proviruses. We found that Scriptaid can activate HIV-1 gene expression in these latent infected cells by 2-15-fold over background levels, as analyzed by flow cytometry. Chromatin immunoprecipitation (ChIP) assays further revealed that the Scriptaid increased the acetylation level of histones H3 and H4 at the nucleosome 1 site of the HIV-1 long terminal repeat compared to mock treatment. In addition, Scriptaid can synergize with prostratin or tumor necrosis factor-alpha to activate the HIV-1 promoter, with relatively lower toxicity compared to TSA. These studies suggest the potential of Scriptaid in anti-latency therapies.
File Format	PDF HTM / HTML
DOI	10.3892/ijmm_00000461
PubMed reference number	20596607
Journal	Medline
Volume Number	26
Issue Number	2
Alternate Webpage(s)	https://www.spandidos-publications.com/ijmm/26/2/265/download
Alternate Webpage(s)	https://doi.org/10.3892/ijmm_00000461
Journal	International journal of molecular medicine
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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