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蛋白质乙酰化/去乙酰化:一种控制真菌感染的潜在策略。

Protein Acetylation/Deacetylation: A Potential Strategy for Fungal Infection Control.

作者信息

Chen Junzhu, Liu Qiong, Zeng Lingbing, Huang Xiaotian

机构信息

Department of Medical Microbiology, School of Medicine, Nanchang University, Nanchang, China.

The First Affiliated Hospital of Nanchang University, Nanchang, China.

出版信息

Front Microbiol. 2020 Oct 7;11:574736. doi: 10.3389/fmicb.2020.574736. eCollection 2020.

Abstract

Protein acetylation is a universal post-translational modification that fine-tunes the major cellular processes of many life forms. Although the mechanisms regulating protein acetylation have not been fully elucidated, this modification is finely tuned by both enzymatic and non-enzymatic mechanisms. Protein deacetylation is the reverse process of acetylation and is mediated by deacetylases. Together, protein acetylation and deacetylation constitute a reversible regulatory protein acetylation network. The recent application of mass spectrometry-based proteomics has led to accumulating evidence indicating that reversible protein acetylation may be related to fungal virulence because a substantial amount of virulence factors are acetylated. Additionally, the relationship between protein acetylation/deacetylation and fungal drug resistance has also been proven and the potential of deacetylase inhibitors as an anti-infective treatment has attracted attention. This review aimed to summarize the research progress in understanding fungal protein acetylation/deacetylation and discuss the mechanism of its mediation in fungal virulence, providing novel targets for the treatment of fungal infection.

摘要

蛋白质乙酰化是一种普遍存在的翻译后修饰,可对多种生命形式的主要细胞过程进行微调。尽管调节蛋白质乙酰化的机制尚未完全阐明,但这种修饰可通过酶促和非酶促机制进行精细调节。蛋白质去乙酰化是乙酰化的逆过程,由去乙酰化酶介导。蛋白质乙酰化和去乙酰化共同构成一个可逆的蛋白质乙酰化调节网络。基于质谱的蛋白质组学技术的最新应用积累了越来越多的证据,表明可逆蛋白质乙酰化可能与真菌毒力有关,因为大量毒力因子都被乙酰化。此外,蛋白质乙酰化/去乙酰化与真菌耐药性之间的关系也已得到证实,去乙酰化酶抑制剂作为抗感染治疗手段的潜力已引起关注。本综述旨在总结在理解真菌蛋白质乙酰化/去乙酰化方面的研究进展,并探讨其介导真菌毒力的机制,为真菌感染的治疗提供新的靶点。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/308d/7579399/287f53cea625/fmicb-11-574736-g001.jpg

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