Sirtuin-1 and HIV-1: An Overview

Author(s): Marilia Rita Pinzone, Bruno Cacopardo, Fabrizio Condorelli, Michele Di Rosa, Giuseppe Nunnari

Journal Name: Current Drug Targets

Volume 14 , Issue 6 , 2013

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Sirtuins are a family of NAD+-dependent protein deacetylases, which regulate cell survival and energy metabolism, inflammation and cancer. Recent studies have shown that sirtuin-1 (SIRT1) modulates Human Immunodeficiency Virus (HIV)-1 transcription. The HIV-1 Tat protein is a substrate for the deacetylase activity of SIRT1; SIRT1 recycles Tat to its unacetylated form, catalyzing a fundamental step to start new cycles of viral transcription. Moreover, Tat has been reported to promote T-cell hyperactivation by suppressing SIRT1 activity. In fact, Tat blocks the ability of SIRT1 to deacetylate lysine 310 in the p65 subunit of nuclear factor-κB (NF-κB) by interacting with the deacetylase domain of SIRT1. This mechanism leads therefore to the hyperactivation of NF-κB proinflammatory pathway and may likely contribute to the chronic immune activation state of HIV-infected individuals.

In the present review we first briefly describe the biological functions of sirtuins, then we delineate the interplay between SIRT1 and HIV-1 and discuss the potential role of SIRT1 as a pharmacological target of HIV-1 replication.

Keywords: Deacetylase activity, HIV-1, HDAC, resveratrol, sirtuin, SIRT1.

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Article Details

Year: 2013
Published on: 30 April, 2013
Page: [648 - 652]
Pages: 5
DOI: 10.2174/1389450111314060005
Price: $65

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