Interaction between M-like protein and macrophage thioredoxin facilitates antiphagocytosis for Streptococcus equi

Zhe Ma1, Hui Zhang, Junxi Zheng

  • 1College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, China.

Plos One
|March 3, 2012
PubMed

Insights

Streptococcus zooepidemicus uses its M-like protein (SzP) to recruit porcine thioredoxin (TRX). This interaction helps bacteria evade host immune defenses by regulating the complement pathway, preventing phagocytosis.

Area of Science:

  • Microbiology
  • Immunology
  • Veterinary Science

Background:

  • Streptococcus equi ssp. zooepidemicus (S. zooepidemicus) is a significant veterinary pathogen.
  • M-like protein (SzP) is a key virulence factor in S. zooepidemicus infections.
  • Bacterial evasion of host immunity is crucial for pathogenesis.

Purpose of the Study:

  • To investigate the interaction between S. zooepidemicus SzP and porcine thioredoxin (TRX).
  • To elucidate the role of this interaction in bacterial virulence and immune evasion.
  • To understand how SzP-TRX interaction affects the complement system.

Main Methods:

  • Yeast two-hybrid assay to identify protein interactions.
  • Co-immunoprecipitation to confirm SzP-TRX interaction.
  • Functional assays to assess TRX activity and complement pathway regulation.

Main Results:

  • SzP directly interacts with both reduced and oxidized forms of TRX.
  • Membrane-bound SzP recruits TRX to the bacterial surface.
  • TRX inhibits alternative complement pathway activity by targeting C3 convertase and associating with Factor H (FH).
  • SzP-recruited TRX reduces C3 deposition on bacteria, hindering phagocytosis.

Conclusions:

  • S. zooepidemicus employs SzP to recruit TRX, a host protein.
  • This recruitment modulates the alternative complement pathway, facilitating immune evasion.
  • The SzP-TRX interaction is a novel mechanism for S. zooepidemicus to evade host phagocytosis.

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