ArticleMolecular microbiology2013
PTS phosphorylation of Mga modulates regulon expression and virulence in the group A streptococcus.
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 72 citations in OpenAlex.
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- Carbon catabolite repression on the Rgg2/3 quorum sensing system in Streptococcus pyogenes is mediated by PTSMolecular microbiology · 2022Article
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- Novel Tyrosine Kinase-Mediated Phosphorylation With Dual Specificity Plays a Key Role in the Modulation ofFrontiers in microbiology · 2021Article
- PRD-Containing Virulence Regulators (PCVRs) in Pathogenic Bacteria.Frontiers in cellular and infection microbiology · 2021Review
- Subpopulation behaviors in lactose metabolism by Streptococcus mutans.Molecular microbiology · 2021Article
- Transporters of glucose and other carbohydrates in bacteria.Pflugers Archiv : European journal of physiology · 2020Review
- AtxA-Controlled Small RNAs ofFrontiers in microbiology · 2020Article
- In silico characterisation of stand-alone response regulators of Streptococcus pyogenes.PloS one · 2020Article
- The group A Streptococcus accessory protein RocA: regulatory activity, interacting partners and influence on disease potential.Molecular microbiology · 2020Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The ability of a bacterial pathogen to monitor available carbon sources in host tissues provides a clear fitness advantage. In the group A streptococcus (GAS), the virulence regulator Mga contains homology to phosphotransferase system (PTS) regulatory domains (PRDs) found in sugar operon regulators. Here we show that Mga was phosphorylated in vitro by the PTS components EI/HPr at conserved PRD histidines. A ΔptsI (EI-deficient) GAS mutant exhibited decreased Mga activity. However, PTS-mediated phosphorylation inhibited Mga-dependent transcription of emm in vitro. Using alanine (unphosphorylated) and aspartate (phosphomimetic) mutations of PRD histidines, we establish that a doubly phosphorylated PRD1 phosphomimetic (D/DMga4) is completely inactive in vivo, shutting down expression of the Mga regulon. Although D/DMga4 is still able to bind DNA in vitro, homo-multimerization of Mga is disrupted and the protein is unable to activate transcription. PTS-mediated regulation of Mga activity appears to be important for pathogenesis, as bacteria expressing either non-phosphorylated (A/A) or phosphomimetic (D/D) PRD1 Mga mutants were attenuated in a model of GAS invasive skin disease. Thus, PTS-mediated phosphorylation of Mga may allow the bacteria to modulate virulence gene expression in response to carbohydrate status. Furthermore, PRD-containing virulence regulators (PCVRs) appear to be widespread in Gram-positive pathogens.
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