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Type III secretion system effector YfiD inhibits the activation of host poly(ADP-ribose) polymerase-1 to promote

Mengqing Zhou1, Yabo Liu1, Yibei Zhang1,2,3

  • 1State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.

Communications Biology
|February 8, 2024
PubMed

Insights

Pathogenic bacteria like Edwardsiella piscicida use effector YfiD to block host cell death by inhibiting poly(ADP-ribose) polymerase-1 (PARP1). This bacterial strategy enhances infection and virulence.

Area of Science:

  • Microbiology
  • Immunology
  • Cell Biology

Background:

  • Pathogenic bacteria modulate host cell death to survive and replicate.
  • Intracellular pathogens utilize type III secretion systems (T3SS) to deliver effector proteins that disrupt host immune responses.
  • Regulated cell death pathways are crucial for controlling bacterial infections.

Purpose of the Study:

  • To investigate the mechanism by which Edwardsiella piscicida evades host immune responses.
  • To elucidate the role of poly(ADP-ribose) polymerase-1 (PARP1) in controlling E. piscicida proliferation.
  • To characterize the function of the T3SS effector YfiD in modulating PARP1 activity and host cell death.

Main Methods:

  • Utilized mouse monocyte macrophages (J774A.1) to study E. piscicida infection.
  • Investigated the activation of PARP1 and the accumulation of poly(ADP-ribose) (PAR) during infection.
  • Analyzed the interaction between E. piscicida's T3SS effector YfiD and PARP1's ADP-ribosyl transferase (ART) domain.
  • Assessed the impact of YfiD on inflammatory response, cell death, and bacterial virulence in vitro and in vivo.

Main Results:

  • PARP1-dependent cell death restrains E. piscicida proliferation by inducing PAR accumulation and inflammatory responses.
  • E. piscicida's T3SS effector YfiD inhibits PARP1 activity and suppresses PAR accumulation.
  • YfiD translocates to the host nucleus and binds to the ART domain of PARP1, mimicking the action of PARP1 inhibitors.
  • YfiD impairs macrophage inflammatory response and cell death, promoting E. piscicida colonization and virulence.

Conclusions:

  • YfiD functions as a novel bacterial inhibitor of PARP1, crucial for E. piscicida pathogenesis.
  • The interaction between YfiD and PARP1's ART domain involves the unfolding of the helical domain.
  • Understanding YfiD's mechanism provides insights into host defense strategies against intracellular bacterial infections.

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