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.
Highlights
Trichinellosis is a serious zoonotic disease caused by the ingestion of undercooked meat contaminated with the larvae of Trichinella spiralis
Our 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
T. spiralis paramyosin (Ts-Pmy) inhibited C1q binding to THP-1-derived macrophages and C1q-induced macrophages migration. These results suggest that Trichinella spiralis paramyosin is a potential immunomodulator involved in the evasion of the host complement attack by binding to C1q in addition to C8/C9, and is a potent vaccine target against trichinellosis
Summary
Trichinellosis is a serious zoonotic disease caused by the ingestion of undercooked meat contaminated with the larvae of Trichinella spiralis. The human astrovirus coat protein inhibited classical and lectin pathway activation by binding to C1q and mannan binding lectin (MBL) [5,6]. Schistosoma mansoni paramyosin protected the parasites against host attack by binding to complement C8 and C9 [12,15]. Further investigations into its role in the survival of parasites in the host demonstrated its inhibitory effect on the formation of the complement membrane attack complex (MAC) by interacting with complement C8 and C9. The invaded T. spiralis could evade the host complement attack by inhibiting MAC formation [13,18]. Ts-Pmy is a functional protein with binding activity to human complement C8 and C9 and plays a role in evading the attack of the host’s immune system. The binding activity of Ts-Pmy to human complement C1q and its ability to inhibit classical complement activation were investigated
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