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Background   Trichinella spiralis  is a tissue-dwelling parasite has developed the ability to evade the host immune attack to establish parasitism in a host. One of the strategies evolved by the nematode is to produce proteins that immunomodulate the host immune system.  Ts Pmy is a paramyosin secreted by  T. spiralis  on the surface of larvae and adult worms that can interact with complement components C1q and C8/C9 to compromise their activation and functions. To better understand the mechanism of  Ts Pmy involved in the C1q inactivation and immune evasion, the C1q-binding site on  Ts Pmy was investigated.    Methods  The  Ts Pmy C1q-binding site was investigated by sequential narrow-down fragment expression in bacteria and peptide binding screening. C1q binding activity was identified by Far-Western blotting and ELISA assays.    Results  After several runs of sequential fragment expression, the C1q binding site was narrowed down to fragments of N-terminal  Ts Pmy226-280aa and  Ts Pmy231-315aa, suggesting the final C1q binding site is probably located to  Ts Pmy231-280aa. A total of nine peptides covering different amino acid sequences within  Ts Pmy231-280aa were synthesized. The binding assay to C1q determined that only P2 peptide covering  Ts Pmy241-280aa binds to C1q, indicating that the C1q binding domain may need both the linearized sequence and conformational structure required for binding to C1q. The binding of peptide P2 to C1q significantly inhibited both C1q-initiated complement classical activation and C1q-induced macrophage chemotaxis.    Conclusions  This study identifies the C1q binding site within  Ts Pmy which provides helpful information for developing a vaccine against trichinellosis by targeting the C1q-binding activity of  Ts Pmy.

Mapping of the complement C1q binding site on Trichinella spiralis paramyosin