Abstract
BackgroundTrichinella 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. TsPmy 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 TsPmy involved in the C1q inactivation and immune evasion, the C1q-binding site on TsPmy was investigated.MethodsThe TsPmy 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.ResultsAfter several runs of sequential fragment expression, the C1q binding site was narrowed down to fragments of N-terminal TsPmy226-280aa and TsPmy231-315aa, suggesting the final C1q binding site is probably located to TsPmy231-280aa. A total of nine peptides covering different amino acid sequences within TsPmy231-280aa were synthesized. The binding assay to C1q determined that only P2 peptide covering TsPmy241-280aa 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.ConclusionsThis study identifies the C1q binding site within TsPmy which provides helpful information for developing a vaccine against trichinellosis by targeting the C1q-binding activity of TsPmy.
Highlights
Trichinella spiralis is a tissue-dwelling parasite has developed the ability to evade the host immune attack to establish parasitism in a host
The results demonstrated that C1q was able to bind onto full-length Trichinella spiralis paramyosin (TsPmy) on the membrane (Fig. 1)
The binding of recombinant fragments to human complement C1q was determined by Enzyme-linked immunosorbent assay (ELISA) with C1q coated on a plate
Summary
Trichinella spiralis is a tissue-dwelling parasite has developed the ability to evade the host immune attack to establish parasitism in a host. Trichinellosis is a worldwide foodborne zoonotic disease caused by the ingestion of undercooked or raw meat infected with infective larvae of T. spiralis [2]. This tissue-dwelling parasite has developed the ability to evade the host immune attack in order to become established in the host [3,4,5]. The mechanism by which Trichinella evades the host immune response and survives in a hostile environment is not well understood [6, 7].
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