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Background  Paramyosin is a thick myofibrillar protein found exclusively in invertebrates. Evidence suggested that paramyosin from helminths serves not only as a structural protein but also as an immunomodulatory agent. We previously reported that recombinant  Trichinella spiralis  paramyosin ( Ts -Pmy) elicited a partial protective immunity in mice. In this study, the ability of  Ts -Pmy to bind host complement components and protect against host complement attack was investigated.    Methods and Findings  In this study, the transcriptional and protein expression levels of  Ts -Pmy were determined in  T. spiralis  newborn larva (NBL), muscle larva (ML) and adult worm developmental stages by RT-PCR and western blot analysis. Expression of  Ts -Pmy at the outer membrane was observed in NBL and adult worms using immunogold electron microscopy and immunofluorescence staining. Functional analysis revealed that recombinant  Ts -Pmy(r Ts -Pmy) strongly bound to complement components C8 and C9 and inhibited the polymerization of C9 during the formation of the membrane attack complex (MAC). r Ts -Pmy also inhibited the lysis of rabbit erythrocytes (E R ) elicited by an alternative pathway-activated complement from guinea pig serum. Inhibition of native  Ts -Pmy on the surface of NBL with a specific antiserum reduced larvae viability when under the attack of complement  in vitro .  In vivo  passive transfer of anti- Ts -Pmy antiserum and complement-treated larvae into mice also significantly reduced the number of larvae that developed to ML.    Conclusion  These studies suggest that the outer membrane form of  T. spiralis  paramyosin plays an important role in the evasion of the host complement attack.

Trichinella spiralis Paramyosin Binds to C8 and C9 and Protects the Tissue-Dwelling Nematode from Being Attacked by Host Complement