GidA, a tRNA Modification Enzyme, Contributes to the Growth, and Virulence of Streptococcus suis Serotype 2
文献类型: 外文期刊
作者: Gao, Ting 1 ; Tan, Meifang 1 ; Liu, Wanquan 1 ; Zhang, Chunyan 1 ; Zhang, Tengfei 2 ; Zheng, Linlin 1 ; Zhu, Jiawen 1 ; L 1 ;
作者机构: 1.Huazhong Agr Univ, Coll Vet Med, State Key Lab Agr Microbiol, Wuhan, Peoples R China
2.Hubei Acad Agr Sci, Inst Anim Husb & Vet Sci, Vet Med Lab, Wuhan, Peoples R China
3.Wuhan Chopper Biol Co Ltd, Wuhan, Peoples R China
4.Cooperat Innovat Ctr Sustainable Pig Prod, Wuhan, Peoples R China
5.Cooperat Innovat Ctr Sustainable Pig Prod, Wuhan, Pe
关键词: Streptococcus suis (S. suis);glucose-inhibited division protein (GidA);tRNA modification;iTRAQ;growth;capsule synthesis;virulence
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: 2016 年 6 卷
页码:
收录情况: SCI
摘要: Glucose-inhibited division protein (GidA), is a tRNA modification enzyme functioning together with MnmE in the addition of a carboxymethylaminomethyl group to position 5 of the anticodon wobble uridine of tRNA. Here, we report a GidA homolog from a Chinese isolate SC-19 of the zoonotic Streptococcus suis serotype 2 (SS2). gidA disruption led to a defective growth, increased capsule thickness, and reduced hemolytic activity. Moreover, the gidA deletion mutant (zioidA) displayed reduced mortality and bacterial loads in mice, reduced ability of adhesion to and invasion in epithelial cells, and increased sensitivity to phagocytosis. The iTRAQ analysis identified 372 differentially expressed (182 up- and 190 down-regulated) proteins in Delta gidA and SC-19. Numerous DNA replication, cell division, and virulence associated proteins were downregulated, whereas many capsule synthesis enzymes were upregulated by gidA disruption. This is consistent with the phenotypes of the mutant. Thus, GidA is a translational regulator that plays an important role in the growth, cell division, capsule biosynthesis, and virulence of SS2. Our findings provide new insight into the regulatory function of GidA in bacterial pathogens.
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