ArticleFrontiers in cellular and infection microbiology2016
GidA, a tRNA Modification Enzyme, Contributes to the Growth, and Virulence of Streptococcus suis Serotype 2.
Article in Frontiers in cellular and infection microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 46 citations in OpenAlex.
- tRNA Modification Landscapes in Streptococci: Shared Losses and Clade-Specific Adaptations.bioRxiv : the preprint server for biology · 2025Article
- tRNA modifying enzymes MnmE and MnmG are essential forbioRxiv : the preprint server for biology · 2025Article
- AI-2 quorum sensing-induced galactose metabolism activation in Streptococcus suis enhances capsular polysaccharide-associated virulence.Veterinary research · 2024Article
- Modeling Co-Infection byAnimals : an open access journal from MDPI · 2023Article
- Theaflavin AmelioratesInternational journal of molecular sciences · 2023Article
- A tRNA modifying enzyme as a tunable regulatory nexus for bacterial stress responses and virulence.Nucleic acids research · 2022Article
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- Peptidomics Analysis of Virulent Peptides Involved inAnimals : an open access journal from MDPI · 2021Article
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- A Comprehensive Evolutionary Scenario of Cell Division and Associated Processes in the Firmicutes.Molecular biology and evolution · 2021Article
- YSIRK-G/S-directed translocation is required forVirulence · 2020Article
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- Proteomic and Metabolomic Analyses Provide Insights into the Mechanism on Arginine Metabolism Regulated by tRNA Modification Enzymes GidA and MnmE ofFrontiers in cellular and infection microbiology · 2020Article
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- HP1717 Contributes to Streptococcus suis Virulence by Inducing an Excessive Inflammatory Response and Influencing the Biosynthesis of the Capsule.Microorganisms · 2019Article
- MnmE, a Central tRNA-Modifying GTPase, Is Essential for the Growth, Pathogenicity, and Arginine Metabolism ofFrontiers in cellular and infection microbiology · 2019Article
- Wobbling Forth and Drifting Back: The Evolutionary History and Impact of Bacterial tRNA Modifications.Molecular biology and evolution · 2018Article
- Unique Features and Anti-microbial Targeting of Folate- and Flavin-Dependent Methyltransferases Required for Accurate Maintenance of Genetic Information.Frontiers in microbiology · 2018Review
- The involvement of MsmK in pathogenesis of the Streptococcus suis serotype 2.MicrobiologyOpen · 2017Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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