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Helminths develop strategies to escape host immune responses that facilitate their survival in the hostile host immune environment.  Trichinella spiralis , a tissue-dwelling nematode, has developed a sophisticated strategy to escape complement attack. Our previous study demonstrated that  T. spiralis  secretes calreticulin ( Ts CRT) to inhibit host classical complement activation through binding to C1q; however, the C1q binding site in  Ts CRT and the specific mechanism involved with complement-related immune evasion remains unknown. Using molecular docking modeling and fragment expression, we determined that  Ts CRT-S, a 153-aa domain of  Ts CRT, is responsible for C1q binding. Recombinant  Ts CRT-S protein expressed in  Escherichia coli  had the same capacity to bind and inhibit human C1q-induced complement and neutrophil activation, as full-length  Ts CRT.  Ts CRT-S inhibited neutrophil reactive oxygen species and elastase release by binding to C1q and reduced neutrophil killing of newborn  T. spiralis  larvae. Binding of  Ts CRT-S to C1q also inhibited formation of neutrophil extracellular traps (NETs), which are involved in autoimmune pathologies and have yet to be therapeutically targeted. These findings provide evidence that the  Ts CRT-S fragment, rather than the full-length  Ts CRT, is a potential target for vaccine or therapeutic development for trichinellosis, as well as for complement-related autoimmune disease therapies.

Trichinella spiralis Calreticulin S-Domain Binds to Human Complement C1q to Interfere With C1q-Mediated Immune Functions