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MnmE, a Central tRNA-Modifying GTPase, Is Essential for the Growth, Pathogenicity, and Arginine Metabolism of Streptococcus suis Serotype 2

文献类型： 外文期刊

作者： Gao, Ting 1 ; Yuan, Fangyan 1 ; Liu, Zewen 1 ; Liu, Wei 1 ; Zhou, Danna 1 ; Yang, Keli 1 ; Duan, Zhengying 1 ; Guo, Rui 1 ;

作者机构： 1.Hubei Acad Agr Sci, Key Lab Prevent & Control Agents Anim Bacteriosis, Minist Agr & Rural Affairs, Inst Anim Husb & Vet, Wuhan, Hubei, Peoples R China

2.Huazhong Agr Univ, Coll Vet Med, State Key Lab Agr Microbiol, Wuhan, Hubei, Peoples R China

3.Cooperat Innovat Ctr Sustainable Pig Prod, Wuhan, Hubei, Peoples R China

关键词： Streptococcus suis (S. suis); MnmE; tRNA modifying guanosine triphosphatase; tandem mass tag-based quantitative proteomics; growth; pathogenicity; arginine deiminase system

期刊名称：FRONTIERS IN CELLULAR AND INFECTION MICROBIOLOGY （ 影响因子：5.293； 五年影响因子：5.882 ）

ISSN： 2235-2988

年卷期： 2019 年 9 卷

页码：

收录情况： SCI

摘要： Streptococcus suis is an important pathogen in pigs and can also cause severe infections in humans. However, little is known about proteins associated with cell growth and pathogenicity of S. suis. In this study, a guanosine triphosphatase (GTPase) MnmE homolog was identified in a Chinese isolate (SC19) that drives a tRNA modification reaction. A mnmE deletion strain (1 mnmE) and a complementation strain (C 1 mnmE) were constructed to systematically decode the characteristics and functions of MnmE both in vitro and in vivo studies via proteomic analysis. Phenotypic analysis revealed that the 1 mnmE strain displayed deficient growth, attenuated pathogenicity, and perturbation of the arginine metabolic pathway mediated by the arginine deiminase system (ADS). Consistently, tandem mass tag -based quantitative proteomics analysis confirmed that 365 proteins were differentially expressed (174 up-and 191 down-regulated) between strains 1 mnmE and SC19. Many proteins associated with DNA replication, cell division, and virulence were down-regulated. Particularly, the core enzymes of the ADS were significantly down-regulated in strain 1 mnmE. These data also provide putative molecular mechanisms for MnmE in cell growth and survival in an acidic environment. Therefore, we propose that MnmE, by its function as a central tRNA-modifying GTPase, is essential for cell growth, pathogenicity, as well as arginine metabolism of S.

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