Post-translational Modifications in Oral Bacteria and Their Functional Impact

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 s...

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Autores principales:	Qizhao Ma, Qiong Zhang, Yang Chen, Shuxing Yu, Jun Huang, Yaqi Liu, Tao Gong, Yuqing Li, Jing Zou
Formato:	article
Lenguaje:	EN
Publicado:	Frontiers Media S.A. 2021
Materias:	post-translational modifications bacteria physiology bacterial virulence Streptococcus mutans Porphyromonas gingivalis Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/2db323a0bc0e49fdaf71d80d7804ebe9
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spelling	oai:doaj.org-article:2db323a0bc0e49fdaf71d80d7804ebe92021-12-02T09:17:37ZPost-translational Modifications in Oral Bacteria and Their Functional Impact1664-302X10.3389/fmicb.2021.784923https://doaj.org/article/2db323a0bc0e49fdaf71d80d7804ebe92021-12-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fmicb.2021.784923/fullhttps://doaj.org/toc/1664-302XOral 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 Porphyromonas gingivalis EPS production and community development with the antecedent oral biofilm constituent Streptococcus gordonii, 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 Streptococcus mutans, 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 P. gingivalis virulence factors (gingipains, fimbriae, RagB, and PorR), and cysteine glutathionylation in thioredoxin-like protein (Tlp) in response to oxidative stress in S. mutans. 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.Qizhao MaQizhao MaQiong ZhangQiong ZhangYang ChenYang ChenShuxing YuShuxing YuJun HuangJun HuangYaqi LiuYaqi LiuTao GongYuqing LiJing ZouJing ZouFrontiers Media S.A.articlepost-translational modificationsbacteriaphysiologybacterial virulenceStreptococcus mutansPorphyromonas gingivalisMicrobiologyQR1-502ENFrontiers in Microbiology, Vol 12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	post-translational modifications bacteria physiology bacterial virulence Streptococcus mutans Porphyromonas gingivalis Microbiology QR1-502
spellingShingle	post-translational modifications bacteria physiology bacterial virulence Streptococcus mutans Porphyromonas gingivalis Microbiology QR1-502 Qizhao Ma Qizhao Ma Qiong Zhang Qiong Zhang Yang Chen Yang Chen Shuxing Yu Shuxing Yu Jun Huang Jun Huang Yaqi Liu Yaqi Liu Tao Gong Yuqing Li Jing Zou Jing Zou Post-translational Modifications in Oral Bacteria and Their Functional Impact
description	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 Porphyromonas gingivalis EPS production and community development with the antecedent oral biofilm constituent Streptococcus gordonii, 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 Streptococcus mutans, 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 P. gingivalis virulence factors (gingipains, fimbriae, RagB, and PorR), and cysteine glutathionylation in thioredoxin-like protein (Tlp) in response to oxidative stress in S. mutans. 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.
format	article
author	Qizhao Ma Qizhao Ma Qiong Zhang Qiong Zhang Yang Chen Yang Chen Shuxing Yu Shuxing Yu Jun Huang Jun Huang Yaqi Liu Yaqi Liu Tao Gong Yuqing Li Jing Zou Jing Zou
author_facet	Qizhao Ma Qizhao Ma Qiong Zhang Qiong Zhang Yang Chen Yang Chen Shuxing Yu Shuxing Yu Jun Huang Jun Huang Yaqi Liu Yaqi Liu Tao Gong Yuqing Li Jing Zou Jing Zou
author_sort	Qizhao Ma
title	Post-translational Modifications in Oral Bacteria and Their Functional Impact
title_short	Post-translational Modifications in Oral Bacteria and Their Functional Impact
title_full	Post-translational Modifications in Oral Bacteria and Their Functional Impact
title_fullStr	Post-translational Modifications in Oral Bacteria and Their Functional Impact
title_full_unstemmed	Post-translational Modifications in Oral Bacteria and Their Functional Impact
title_sort	post-translational modifications in oral bacteria and their functional impact
publisher	Frontiers Media S.A.
publishDate	2021
url	https://doaj.org/article/2db323a0bc0e49fdaf71d80d7804ebe9
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Post-translational Modifications in Oral Bacteria and Their Functional Impact

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