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Streptococcus pneumoniae Infection Promotes Histone H3 Dephosphorylation by Modulating Host PP1 Phosphatase

Wenyang Dong1, Orhan Rasid2, Christine Chevalier2

  • 1G5 Chromatine et Infection, Institut Pasteur, Paris 75015, France; Université de Paris, Sorbonne Paris Cité, Paris, France.

Cell Reports
|March 27, 2020
PubMed

Insights

Streptococcus pneumoniae infection causes histone H3 dephosphorylation via pneumolysin and H2O2, activating PP1 phosphatase. This epigenetic change enhances bacterial survival within host cells.

Area of Science:

  • Microbiology
  • Epigenetics
  • Cell Biology

Background:

  • Pathogenic bacteria manipulate host gene expression via histone modifications.
  • Streptococcus pneumoniae is a common respiratory pathogen.

Purpose of the Study:

  • To investigate how Streptococcus pneumoniae alters host cell epigenetics.
  • To identify the bacterial factors and host mechanisms involved in histone modification during infection.

Main Methods:

  • Analysis of histone modifications in infected respiratory epithelial cells.
  • Investigating the roles of pneumolysin (PLY) and H2O2.
  • Assessing the involvement of protein phosphatase 1 (PP1).

Main Results:

  • S. pneumoniae induces dephosphorylation of histone H3 on serine 10 (H3S10).
  • Pneumolysin and H2O2 are key bacterial factors mediating H3S10 dephosphorylation.
  • Host PP1 phosphatase is activated by bacterial infection, leading to H3S10 dephosphorylation.
  • Impaired intracellular S. pneumoniae survival in cells with catalytically deficient PP1.
  • PP1 activation and H3S10 dephosphorylation are general mechanisms for bacterial survival.

Conclusions:

  • S. pneumoniae utilizes PLY and H2O2 to trigger host PP1 activation and H3S10 dephosphorylation.
  • This epigenomic modification by PP1 is crucial for intracellular bacterial survival.
  • The findings suggest a conserved mechanism employed by various pathogens to evade host defenses.
Keywords:
H3S10 dephosphorylationSpxBStreptococcus pneumoniaebacterial infectionhistone modificationpneumolysinprotein phosphatase 1

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