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GidA, a tRNA Modification Enzyme, Contributes to the Growth, and Virulence of Streptococcus suis Serotype 2.

Gao T, Tan M, Liu W, Zhang C, Zhang T, Zheng L, Zhu J, Li L, Zhou R - Front Cell Infect Microbiol (2016)

Bottom Line: 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.This is consistent with the phenotypes of the mutant.Our findings provide new insight into the regulatory function of GidA in bacterial pathogens.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural UniversityWuhan, China; Veterinary Medicine Laboratory, Institute of Animal Husbandry and Veterinary Science, Hubei Academy of Agricultural ScienceWuhan, China; Wuhan Chopper Biology Co., Ltd.Wuhan, China.

ABSTRACT
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 (ΔgidA) 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 ΔgidA 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.

No MeSH data available.


Related in: MedlinePlus

Distribution of differentially expressed proteins according to GO annotation.
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Figure 5: Distribution of differentially expressed proteins according to GO annotation.

Mentions: These DE proteins were annotated using Blast2GO according to biological process, molecular function, and cellular component (Figure 5). In terms of biological process, the 372 DE proteins were classified into 11 categories. The top categories with the highest number of DE proteins were metabolic process (246, 66.1%), cellular process (203, 54.6%), and single-organism process (163, 43.8%); these three functional categories are the most important in S. suis response to environmental stresses. In terms of molecular function, the 372 DE proteins were classified into nine categories. The top two categories with the highest number of DE proteins were catalytic activity (213, 57.3%) and binding (152, 40.9%). In terms of cellular component, the 372 DE proteins were classified into six categories. The top three categories with the highest number of DE proteins were cell (133, 35.8%), membrane (62, 16.7%), and macromolecular complex (54, 14.5%).


GidA, a tRNA Modification Enzyme, Contributes to the Growth, and Virulence of Streptococcus suis Serotype 2.

Gao T, Tan M, Liu W, Zhang C, Zhang T, Zheng L, Zhu J, Li L, Zhou R - Front Cell Infect Microbiol (2016)

Distribution of differentially expressed proteins according to GO annotation.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4835480&req=5

Figure 5: Distribution of differentially expressed proteins according to GO annotation.
Mentions: These DE proteins were annotated using Blast2GO according to biological process, molecular function, and cellular component (Figure 5). In terms of biological process, the 372 DE proteins were classified into 11 categories. The top categories with the highest number of DE proteins were metabolic process (246, 66.1%), cellular process (203, 54.6%), and single-organism process (163, 43.8%); these three functional categories are the most important in S. suis response to environmental stresses. In terms of molecular function, the 372 DE proteins were classified into nine categories. The top two categories with the highest number of DE proteins were catalytic activity (213, 57.3%) and binding (152, 40.9%). In terms of cellular component, the 372 DE proteins were classified into six categories. The top three categories with the highest number of DE proteins were cell (133, 35.8%), membrane (62, 16.7%), and macromolecular complex (54, 14.5%).

Bottom Line: 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.This is consistent with the phenotypes of the mutant.Our findings provide new insight into the regulatory function of GidA in bacterial pathogens.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural UniversityWuhan, China; Veterinary Medicine Laboratory, Institute of Animal Husbandry and Veterinary Science, Hubei Academy of Agricultural ScienceWuhan, China; Wuhan Chopper Biology Co., Ltd.Wuhan, China.

ABSTRACT
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 (ΔgidA) 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 ΔgidA 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.

No MeSH data available.


Related in: MedlinePlus