Group A Streptococcus co-ordinates manganese import and iron efflux in response to hydrogen peroxide stress

Andrew G Turner1, Karrera Y Djoko1,2, Cheryl-Lynn Y Ong1,3

  • 1School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia 4072, Australia.

The Biochemical Journal
|January 24, 2019
PubMed

Insights

Group A Streptococcus uses manganese import (MtsABC) and iron export (PmtA) to ensure its superoxide dismutase (SodA) is correctly activated with manganese, crucial for combating oxidative stress during infection.

Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Oxidative Stress Response

Background:

  • Bacterial pathogens face challenges like metal imbalance and oxidative stress during infection.
  • Group A Streptococcus (GAS) must manage intracellular metal levels for survival and virulence.

Purpose of the Study:

  • To investigate how GAS regulates manganese and iron homeostasis under oxidative stress.
  • To elucidate the role of specific transporters and regulators in maintaining superoxide dismutase function.

Main Methods:

  • Analysis of MtsABC manganese import system regulated by MtsR.
  • Investigation of the PerR-regulated iron efflux system PmtA.
  • Assessment of SodA activity under varying metal conditions and stress.

Main Results:

  • GAS utilizes MtsABC for Mn(II) import under hydrogen peroxide stress.
  • SodA requires manganese for optimal activity; iron incorporation reduces its function.
  • PmtA is essential for reducing intracellular iron and preventing SodA "mismetallation" under high iron conditions.

Conclusions:

  • MtsR-regulated Mn(II) import and PerR-regulated Fe(II) efflux work coordinately.
  • This coordinated action ensures proper Mn(II) metallation of SodA for effective superoxide dismutase function in GAS.

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