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Updated: May 24, 2026

Experimental Analysis of Apoptotic Thymocyte Engulfment by Macrophages
Published on: May 24, 2019
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.
Abstract:
Streptococcus equi ssp. zooepidemicus (S. zooepidemicus, S.z) is one of the common pathogens that can cause septicemia, meningitis, and mammitis in domesticated species. M-like protein (SzP) is an important virulence factor of S. zooepidemicus and contributes to bacterial infection and antiphagocytosis. The interaction between SzP of S. zooepidemicus and porcine thioredoxin (TRX) was identified by the yeast two-hybrid and further confirmed by co-immunoprecipitation. SzP interacted with both reduced and the oxidized forms of TRX without inhibiting TRX activity. Membrane anchored SzP was able to recruit TRX to the surface, which would facilitate the antiphagocytosis of the bacteria. Further experiments revealed that TRX regulated the alternative complement pathway by inhibiting C3 convertase activity and associating with factor H (FH). TRX alone inhibited C3 cleavage and C3a production, and the inhibitory effect was additive when FH was also present. TRX inhibited C3 deposition on the bacterial surface when it was recruited by SzP. These new findings indicated that S. zooepidemicus used SzP to recruit TRX and regulated the alternative complement pathways to evade the host immune phagocytosis.
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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