Trichinella spiralis Paramyosin Binds Human Complement C1q and Inhibits Classical Complement Activation |
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| Authors: | Ran Sun Xi Zhao Zixia Wang Jing Yang Limei Zhao Bin Zhan Xinping Zhu |
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| Institution: | 1. Department of Parasitology, School of Basic Medical Sciences, Capital Medical University, Beijing, PR China.; 2. Department of Pediatrics, National School of Tropical Medicine, Baylor College of Medicine, Houston, Texas, United States of America.; Instituto Butantan, BRAZIL, |
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| Abstract: | Background
Trichinella spiralis expresses paramyosin (Ts-Pmy) as a defense mechanism. Ts-Pmy is a functional protein with binding activity to human complement C8 and C9 and thus plays a role in evading the attack of the host’s immune system. In the present study, the binding activity of Ts-Pmy to human complement C1q and its ability to inhibit classical complement activation were investigated.Methods and FindingsThe binding of recombinant and natural Ts-Pmy to human C1q were determined by ELISA, Far Western blotting and immunoprecipitation, respectively. Binding of recombinant Ts-Pmy (rTs-Pmy) to C1q inhibited C1q binding to IgM and consequently inhibited C3 deposition. The lysis of antibody-sensitized erythrocytes (EAs) elicited by the classical complement pathway was also inhibited in the presence of rTs-Pmy. In addition to inhibiting classical complement activation, rTs-Pmy also suppressed C1q binding to THP-1-derived macrophages, thereby reducing C1q-induced macrophages migration.ConclusionOur results suggest that T. spiralis paramyosin plays an important role in immune evasion by interfering with complement activation through binding to C1q in addition to C8 and C9. |
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