Trichinella spiralis paramyosin binds to C8 and C9 and protects the tissue-dwelling nematode from being attacked by host complement.

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)...

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Bibliographic Details
Published in:PLoS Neglected Tropical Diseases
Main Authors: Zhifei Zhang, Jing Yang, Junfei Wei, Yaping Yang, Xiaoqin Chen, Xi Zhao, Yuan Gu, Shijuan Cui, Xinping Zhu
Format: Article in Journal/Newspaper
Language:English
Published: Public Library of Science (PLoS) 2011
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Online Access:https://doi.org/10.1371/journal.pntd.0001225
https://doaj.org/article/c0df0aa647b640848cc85e4caa5c13ba
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Summary: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(rTs-Pmy) strongly bound to complement components C8 and C9 and inhibited the polymerization of C9 during the formation of the membrane attack complex (MAC). rTs-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.