Histone deacetylase inhibition as an alternative strategy against invasive aspergillosis.

Details

Serval ID
serval:BIB_30AE1185FA8C
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Histone deacetylase inhibition as an alternative strategy against invasive aspergillosis.
Journal
Frontiers in microbiology
Author(s)
Lamoth F., Juvvadi P.R., Steinbach W.J.
ISSN
1664-302X (Print)
ISSN-L
1664-302X
Publication state
Published
Issued date
2015
Peer-reviewed
Oui
Volume
6
Pages
96
Language
english
Notes
Publication types: Journal Article
Publication Status: epublish
Abstract
Invasive aspergillosis (IA) is a life-threatening infection due to Aspergillus fumigatus and other Aspergillus spp. Drugs targeting the fungal cell membrane (triazoles, amphotericin B) or cell wall (echinocandins) are currently the sole therapeutic options against IA. Their limited efficacy and the emergence of resistance warrant the identification of new antifungal targets. Histone deacetylases (HDACs) are enzymes responsible of the deacetylation of lysine residues of core histones, thus controlling chromatin remodeling and transcriptional activation. HDACs also control the acetylation and activation status of multiple non-histone proteins, including the heat shock protein 90 (Hsp90), an essential molecular chaperone for fungal virulence and antifungal resistance. This review provides an overview of the different HDACs in Aspergillus spp. as well as their respective contribution to total HDAC activity, fungal growth, stress responses, and virulence. The potential of HDAC inhibitors, currently under development for cancer therapy, as novel alternative antifungal agents against IA is discussed.
Keywords
Aspergillus fumigatus, antifungal resistance, antifungal therapy, heat shock protein 90, lysine deacetylases, trichostatin A
Pubmed
Web of science
Open Access
Yes
Create date
03/10/2019 17:04
Last modification date
04/10/2019 6:26
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