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口腔细菌中的翻译后修饰及其功能影响

Post-translational Modifications in Oral Bacteria and Their Functional Impact.

作者信息

Ma Qizhao, Zhang Qiong, Chen Yang, Yu Shuxing, Huang Jun, Liu Yaqi, Gong Tao, Li Yuqing, Zou Jing

机构信息

State Key Laboratory of Oral Diseases, National Clinical Research Center for Oral Diseases, West China Hospital of Stomatology, Sichuan University, Chengdu, China.

Department of Pediatric Dentistry, West China Hospital of Stomatology, Sichuan University, Chengdu, China.

出版信息

Front Microbiol. 2021 Dec 2;12:784923. doi: 10.3389/fmicb.2021.784923. eCollection 2021.

DOI:10.3389/fmicb.2021.784923
PMID:34925293
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8674579/
Abstract

Oral bacteria colonize the oral cavity, surrounding complex and variable environments. Post-translational modifications (PTMs) are an efficient biochemical mechanism across all domains of life. Oral bacteria could depend on PTMs to quickly regulate their metabolic processes in the face of external stimuli. In recent years, thanks to advances in enrichment strategies, the number and variety of PTMs that have been identified and characterized in oral bacteria have increased. PTMs, covalently modified by diverse enzymes, occur in amino acid residues of the target substrate, altering the functions of proteins involved in different biological processes. For example, Ptk1 reciprocally phosphorylates Php1 on tyrosine residues 159 and 161, required for EPS production and community development with the antecedent oral biofilm constituent , and in turn Php1 dephosphorylates Ptk1 and rapidly causes the conversion of Ptk1 to a state of low tyrosine phosphorylation. Protein acetylation is also widespread in oral bacteria. In the acetylome of , 973 acetylation sites were identified in 445 proteins, accounting for 22.7% of overall proteins involving virulence factors and pathogenic processes. Other PTMs in oral bacteria include serine or threonine glycosylation in Cnm involving intracerebral hemorrhage, arginine citrullination in peptidylarginine deiminases (PADs), leading to inflammation, lysine succinylation in virulence factors (gingipains, fimbriae, RagB, and PorR), and cysteine glutathionylation in thioredoxin-like protein (Tlp) in response to oxidative stress in . Here we review oral bacterial PTMs, focusing on acetylation, phosphorylation, glycosylation, citrullination, succinylation, and glutathionylation, and corresponding modifying enzymes. We describe different PTMs in association with some examples, discussing their potential role and function in oral bacteria physiological processes and regulatory networks. Identification and characterization of PTMs not only contribute to understanding their role in oral bacterial virulence, adaption, and resistance but will open new avenues to treat oral infectious diseases.

摘要

口腔细菌定殖于口腔这一复杂多变的环境中。翻译后修饰(PTMs)是一种在所有生命领域都存在的高效生化机制。面对外部刺激时,口腔细菌可能依赖翻译后修饰来快速调节其代谢过程。近年来,由于富集策略的进步,口腔细菌中已被鉴定和表征的翻译后修饰的数量和种类有所增加。由多种酶共价修饰的翻译后修饰发生在靶底物的氨基酸残基上,改变参与不同生物过程的蛋白质的功能。例如,Ptk1在酪氨酸残基159和161上对Php1进行相互磷酸化,这是与先前的口腔生物膜成分产生胞外多糖(EPS)和群落发育所必需的,反过来,Php1使Ptk1去磷酸化,并迅速导致Ptk1转变为低酪氨酸磷酸化状态。蛋白质乙酰化在口腔细菌中也很普遍。在[具体细菌名称]的乙酰化蛋白质组中,在445种蛋白质中鉴定出973个乙酰化位点,占涉及毒力因子和致病过程的总蛋白质的22.7%。口腔细菌中的其他翻译后修饰包括与脑出血相关的Cnm中的丝氨酸或苏氨酸糖基化、肽基精氨酸脱氨酶(PADs)中的精氨酸瓜氨酸化(导致炎症)、毒力因子(牙龈蛋白酶、菌毛、RagB和PorR)中的赖氨酸琥珀酰化,以及在[具体细菌名称]中响应氧化应激的硫氧还蛋白样蛋白(Tlp)中的半胱氨酸谷胱甘肽化。在此,我们综述口腔细菌的翻译后修饰,重点关注乙酰化、磷酸化、糖基化、瓜氨酸化、琥珀酰化和谷胱甘肽化以及相应的修饰酶。我们结合一些实例描述不同的翻译后修饰,讨论它们在口腔细菌生理过程和调控网络中的潜在作用和功能。翻译后修饰的鉴定和表征不仅有助于理解它们在口腔细菌毒力、适应性和抗性中的作用,还将为治疗口腔传染病开辟新途径。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bf11/8674579/4c3ca2347aec/fmicb-12-784923-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bf11/8674579/f6e1c4a29516/fmicb-12-784923-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bf11/8674579/07a3181065ac/fmicb-12-784923-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bf11/8674579/6ef57fe2f0fb/fmicb-12-784923-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bf11/8674579/4c3ca2347aec/fmicb-12-784923-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bf11/8674579/f6e1c4a29516/fmicb-12-784923-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bf11/8674579/07a3181065ac/fmicb-12-784923-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bf11/8674579/6ef57fe2f0fb/fmicb-12-784923-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bf11/8674579/4c3ca2347aec/fmicb-12-784923-g004.jpg

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