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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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Autores principales: Zhang, Zhifei, Yang, Jing, Wei, Junfei, Yang, Yaping, Chen, Xiaoqin, Zhao, Xi, Gu, Yuan, Cui, Shijuan, Zhu, Xinping
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3130009/
https://www.ncbi.nlm.nih.gov/pubmed/21750743
http://dx.doi.org/10.1371/journal.pntd.0001225
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author Zhang, Zhifei
Yang, Jing
Wei, Junfei
Yang, Yaping
Chen, Xiaoqin
Zhao, Xi
Gu, Yuan
Cui, Shijuan
Zhu, Xinping
author_facet Zhang, Zhifei
Yang, Jing
Wei, Junfei
Yang, Yaping
Chen, Xiaoqin
Zhao, Xi
Gu, Yuan
Cui, Shijuan
Zhu, Xinping
author_sort Zhang, Zhifei
collection PubMed
description 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.
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spelling pubmed-31300092011-07-12 Trichinella spiralis Paramyosin Binds to C8 and C9 and Protects the Tissue-Dwelling Nematode from Being Attacked by Host Complement Zhang, Zhifei Yang, Jing Wei, Junfei Yang, Yaping Chen, Xiaoqin Zhao, Xi Gu, Yuan Cui, Shijuan Zhu, Xinping PLoS Negl Trop Dis Research Article 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. Public Library of Science 2011-07-05 /pmc/articles/PMC3130009/ /pubmed/21750743 http://dx.doi.org/10.1371/journal.pntd.0001225 Text en Zhang et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Zhang, Zhifei
Yang, Jing
Wei, Junfei
Yang, Yaping
Chen, Xiaoqin
Zhao, Xi
Gu, Yuan
Cui, Shijuan
Zhu, Xinping
Trichinella spiralis Paramyosin Binds to C8 and C9 and Protects the Tissue-Dwelling Nematode from Being Attacked by Host Complement
title Trichinella spiralis Paramyosin Binds to C8 and C9 and Protects the Tissue-Dwelling Nematode from Being Attacked by Host Complement
title_full Trichinella spiralis Paramyosin Binds to C8 and C9 and Protects the Tissue-Dwelling Nematode from Being Attacked by Host Complement
title_fullStr Trichinella spiralis Paramyosin Binds to C8 and C9 and Protects the Tissue-Dwelling Nematode from Being Attacked by Host Complement
title_full_unstemmed Trichinella spiralis Paramyosin Binds to C8 and C9 and Protects the Tissue-Dwelling Nematode from Being Attacked by Host Complement
title_short Trichinella spiralis Paramyosin Binds to C8 and C9 and Protects the Tissue-Dwelling Nematode from Being Attacked by Host Complement
title_sort trichinella spiralis paramyosin binds to c8 and c9 and protects the tissue-dwelling nematode from being attacked by host complement
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3130009/
https://www.ncbi.nlm.nih.gov/pubmed/21750743
http://dx.doi.org/10.1371/journal.pntd.0001225
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