Trichinella spiralis paramyosin binds to C8 and C9 and protects the tissue-dwelling nematode from being attacked by host complement
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...
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| creator | Zhang, Zhifei Yang, Jing Wei, Junfei Yang, Yaping Chen, Xiaoqin Zhao, Xi Gu, Yuan Cui, Shijuan Zhu, Xinping |
| description | 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.
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.
These studies suggest that the outer membrane form of T. spiralis paramyosin plays an important role in the evasion of the host complement attack. |
| doi_str_mv | 10.1371/journal.pntd.0001225 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_plos_</sourceid><recordid>TN_cdi_plos_journals_1288103151</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A263784534</galeid><doaj_id>oai_doaj_org_article_c0df0aa647b640848cc85e4caa5c13ba</doaj_id><sourcerecordid>A263784534</sourcerecordid><originalsourceid>FETCH-LOGICAL-c623t-c6f5463f0ce5138003c6a2c24511fc2de5dfae73c084f3d676752a0cfa05d6c3</originalsourceid><addsrcrecordid>eNptUltr2zAUNmNj7bL9g7EJBttTMl0s23kZlLBLobCXvItjXRJltuRJckef98cnN25JRhFI4pzv-861KN4SvCKsJp8PfgwOutXgklphjAml_FlxSdaML2nN-POT_0XxKsYDxnzNG_KyuKCk5rgu2WXxdxus3Funuw5QHGyAzkY0QID-zkfrUGudiih5tGkQOIU26_tnCD5pmbJnr1GyMY56qf5kFet2yOkeklcameB71OrJBimB_KUVau_Q3seEpO-HTvfapdfFCwNd1G_md1Fsv33dbn4sb35-v95c3SxlRVnKt-FlxQyWmhPWYMxkBVTSkhNiJFWaKwO6ZhI3pWGqqquaU8DSAOaqkmxRvD_KDp2PYm5fFIQ2DcGMZM1FcX1EKA8HMQTbQ7gTHqy4N_iwExCSlZ0WEiuDAaqybqsyB2ykbLguJQCXhLWQtb7M0ca210rmOnNvz0TPPc7uxc7fCkZYnuY6C3yaBYL_PeqYRG-jnObktB-jaOqqIXxNp7Q__Id8urgZtYOcv3XG57By0hRXtGJ1U3JWZtTqCVQ-SvdWeqeNzfYzwscTwl5Dl_bRd2Oy3sVzYHkEyuBjDNo89oJgMW30Q9Zi2mgxb3SmvTvt4yPpYYXZP7sy9Eo</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1288103151</pqid></control><display><type>article</type><title>Trichinella spiralis paramyosin binds to C8 and C9 and protects the tissue-dwelling nematode from being attacked by host complement</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>PubMed Central Open Access</source><source>Public Library of Science (PLoS)</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><creator>Zhang, Zhifei ; Yang, Jing ; Wei, Junfei ; Yang, Yaping ; Chen, Xiaoqin ; Zhao, Xi ; Gu, Yuan ; Cui, Shijuan ; Zhu, Xinping</creator><contributor>Martins, Elizabeth Angelica Leme</contributor><creatorcontrib>Zhang, Zhifei ; Yang, Jing ; Wei, Junfei ; Yang, Yaping ; Chen, Xiaoqin ; Zhao, Xi ; Gu, Yuan ; Cui, Shijuan ; Zhu, Xinping ; Martins, Elizabeth Angelica Leme</creatorcontrib><description>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.
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.
These studies suggest that the outer membrane form of T. spiralis paramyosin plays an important role in the evasion of the host complement attack.</description><identifier>ISSN: 1935-2735</identifier><identifier>ISSN: 1935-2727</identifier><identifier>EISSN: 1935-2735</identifier><identifier>DOI: 10.1371/journal.pntd.0001225</identifier><identifier>PMID: 21750743</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Animals ; Antigens ; Blotting, Western ; Care and treatment ; Complement C8 - antagonists & inhibitors ; Complement C8 - immunology ; Complement C8 - metabolism ; Complement C9 - antagonists & inhibitors ; Complement C9 - immunology ; Complement C9 - metabolism ; Complement Membrane Attack Complex - antagonists & inhibitors ; Developmental stages ; Diagnosis ; Erythrocytes ; Female ; Fluorescent Antibody Technique ; Gene Expression Profiling ; Health aspects ; Hemolysis ; Immune Evasion ; Infections ; Invertebrates ; Laboratory animals ; Larvae ; Medicine ; Mice ; Mice, Inbred ICR ; Microscopy, Immunoelectron ; Molecular Sequence Data ; Nematoda ; Parasites ; Parasitic diseases ; Polymerization ; Protein Binding ; Proteins ; Rabbits ; Reverse Transcriptase Polymerase Chain Reaction ; RNA, Helminth - genetics ; RNA, Messenger - genetics ; Sequence Analysis, DNA ; Trichinella spiralis - immunology ; Trichinosis ; Tropical diseases ; Tropomyosin - immunology ; Tropomyosin - metabolism ; Worms</subject><ispartof>PLoS neglected tropical diseases, 2011-07, Vol.5 (7), p.e1225-e1225</ispartof><rights>COPYRIGHT 2011 Public Library of Science</rights><rights>2011 Zhang et al. 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 credited: Zhang Z, Yang J, Wei J, Yang Y, Chen X, et al. (2011) Trichinella spiralis Paramyosin Binds to C8 and C9 and Protects the Tissue-Dwelling Nematode from Being Attacked by Host Complement. PLoS Negl Trop Dis 5(7): e1225. doi:10.1371/journal.pntd.0001225</rights><rights>Zhang et al. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c623t-c6f5463f0ce5138003c6a2c24511fc2de5dfae73c084f3d676752a0cfa05d6c3</citedby><cites>FETCH-LOGICAL-c623t-c6f5463f0ce5138003c6a2c24511fc2de5dfae73c084f3d676752a0cfa05d6c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3130009/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3130009/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21750743$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Martins, Elizabeth Angelica Leme</contributor><creatorcontrib>Zhang, Zhifei</creatorcontrib><creatorcontrib>Yang, Jing</creatorcontrib><creatorcontrib>Wei, Junfei</creatorcontrib><creatorcontrib>Yang, Yaping</creatorcontrib><creatorcontrib>Chen, Xiaoqin</creatorcontrib><creatorcontrib>Zhao, Xi</creatorcontrib><creatorcontrib>Gu, Yuan</creatorcontrib><creatorcontrib>Cui, Shijuan</creatorcontrib><creatorcontrib>Zhu, Xinping</creatorcontrib><title>Trichinella spiralis paramyosin binds to C8 and C9 and protects the tissue-dwelling nematode from being attacked by host complement</title><title>PLoS neglected tropical diseases</title><addtitle>PLoS Negl Trop Dis</addtitle><description>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.
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.
These studies suggest that the outer membrane form of T. spiralis paramyosin plays an important role in the evasion of the host complement attack.</description><subject>Animals</subject><subject>Antigens</subject><subject>Blotting, Western</subject><subject>Care and treatment</subject><subject>Complement C8 - antagonists & inhibitors</subject><subject>Complement C8 - immunology</subject><subject>Complement C8 - metabolism</subject><subject>Complement C9 - antagonists & inhibitors</subject><subject>Complement C9 - immunology</subject><subject>Complement C9 - metabolism</subject><subject>Complement Membrane Attack Complex - antagonists & inhibitors</subject><subject>Developmental stages</subject><subject>Diagnosis</subject><subject>Erythrocytes</subject><subject>Female</subject><subject>Fluorescent Antibody Technique</subject><subject>Gene Expression Profiling</subject><subject>Health aspects</subject><subject>Hemolysis</subject><subject>Immune Evasion</subject><subject>Infections</subject><subject>Invertebrates</subject><subject>Laboratory animals</subject><subject>Larvae</subject><subject>Medicine</subject><subject>Mice</subject><subject>Mice, Inbred ICR</subject><subject>Microscopy, Immunoelectron</subject><subject>Molecular Sequence Data</subject><subject>Nematoda</subject><subject>Parasites</subject><subject>Parasitic diseases</subject><subject>Polymerization</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA, Helminth - genetics</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Analysis, DNA</subject><subject>Trichinella spiralis - immunology</subject><subject>Trichinosis</subject><subject>Tropical diseases</subject><subject>Tropomyosin - immunology</subject><subject>Tropomyosin - metabolism</subject><subject>Worms</subject><issn>1935-2735</issn><issn>1935-2727</issn><issn>1935-2735</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>DOA</sourceid><recordid>eNptUltr2zAUNmNj7bL9g7EJBttTMl0s23kZlLBLobCXvItjXRJltuRJckef98cnN25JRhFI4pzv-861KN4SvCKsJp8PfgwOutXgklphjAml_FlxSdaML2nN-POT_0XxKsYDxnzNG_KyuKCk5rgu2WXxdxus3Funuw5QHGyAzkY0QID-zkfrUGudiih5tGkQOIU26_tnCD5pmbJnr1GyMY56qf5kFet2yOkeklcameB71OrJBimB_KUVau_Q3seEpO-HTvfapdfFCwNd1G_md1Fsv33dbn4sb35-v95c3SxlRVnKt-FlxQyWmhPWYMxkBVTSkhNiJFWaKwO6ZhI3pWGqqquaU8DSAOaqkmxRvD_KDp2PYm5fFIQ2DcGMZM1FcX1EKA8HMQTbQ7gTHqy4N_iwExCSlZ0WEiuDAaqybqsyB2ykbLguJQCXhLWQtb7M0ca210rmOnNvz0TPPc7uxc7fCkZYnuY6C3yaBYL_PeqYRG-jnObktB-jaOqqIXxNp7Q__Id8urgZtYOcv3XG57By0hRXtGJ1U3JWZtTqCVQ-SvdWeqeNzfYzwscTwl5Dl_bRd2Oy3sVzYHkEyuBjDNo89oJgMW30Q9Zi2mgxb3SmvTvt4yPpYYXZP7sy9Eo</recordid><startdate>20110701</startdate><enddate>20110701</enddate><creator>Zhang, Zhifei</creator><creator>Yang, Jing</creator><creator>Wei, Junfei</creator><creator>Yang, Yaping</creator><creator>Chen, Xiaoqin</creator><creator>Zhao, Xi</creator><creator>Gu, Yuan</creator><creator>Cui, Shijuan</creator><creator>Zhu, Xinping</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7SS</scope><scope>7T2</scope><scope>7T7</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8C1</scope><scope>8FD</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F1W</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>H94</scope><scope>H95</scope><scope>H97</scope><scope>K9.</scope><scope>L.G</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20110701</creationdate><title>Trichinella spiralis paramyosin binds to C8 and C9 and protects the tissue-dwelling nematode from being attacked by host complement</title><author>Zhang, Zhifei ; Yang, Jing ; Wei, Junfei ; Yang, Yaping ; Chen, Xiaoqin ; Zhao, Xi ; Gu, Yuan ; Cui, Shijuan ; Zhu, Xinping</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c623t-c6f5463f0ce5138003c6a2c24511fc2de5dfae73c084f3d676752a0cfa05d6c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animals</topic><topic>Antigens</topic><topic>Blotting, Western</topic><topic>Care and treatment</topic><topic>Complement C8 - antagonists & inhibitors</topic><topic>Complement C8 - immunology</topic><topic>Complement C8 - metabolism</topic><topic>Complement C9 - antagonists & inhibitors</topic><topic>Complement C9 - immunology</topic><topic>Complement C9 - metabolism</topic><topic>Complement Membrane Attack Complex - antagonists & inhibitors</topic><topic>Developmental stages</topic><topic>Diagnosis</topic><topic>Erythrocytes</topic><topic>Female</topic><topic>Fluorescent Antibody Technique</topic><topic>Gene Expression Profiling</topic><topic>Health aspects</topic><topic>Hemolysis</topic><topic>Immune Evasion</topic><topic>Infections</topic><topic>Invertebrates</topic><topic>Laboratory animals</topic><topic>Larvae</topic><topic>Medicine</topic><topic>Mice</topic><topic>Mice, Inbred ICR</topic><topic>Microscopy, Immunoelectron</topic><topic>Molecular Sequence Data</topic><topic>Nematoda</topic><topic>Parasites</topic><topic>Parasitic diseases</topic><topic>Polymerization</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA, Helminth - genetics</topic><topic>RNA, Messenger - genetics</topic><topic>Sequence Analysis, DNA</topic><topic>Trichinella spiralis - immunology</topic><topic>Trichinosis</topic><topic>Tropical diseases</topic><topic>Tropomyosin - immunology</topic><topic>Tropomyosin - metabolism</topic><topic>Worms</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Zhifei</creatorcontrib><creatorcontrib>Yang, Jing</creatorcontrib><creatorcontrib>Wei, Junfei</creatorcontrib><creatorcontrib>Yang, Yaping</creatorcontrib><creatorcontrib>Chen, Xiaoqin</creatorcontrib><creatorcontrib>Zhao, Xi</creatorcontrib><creatorcontrib>Gu, Yuan</creatorcontrib><creatorcontrib>Cui, Shijuan</creatorcontrib><creatorcontrib>Zhu, Xinping</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Health and Safety Science Abstracts (Full archive)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PLoS neglected tropical diseases</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Zhifei</au><au>Yang, Jing</au><au>Wei, Junfei</au><au>Yang, Yaping</au><au>Chen, Xiaoqin</au><au>Zhao, Xi</au><au>Gu, Yuan</au><au>Cui, Shijuan</au><au>Zhu, Xinping</au><au>Martins, Elizabeth Angelica Leme</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Trichinella spiralis paramyosin binds to C8 and C9 and protects the tissue-dwelling nematode from being attacked by host complement</atitle><jtitle>PLoS neglected tropical diseases</jtitle><addtitle>PLoS Negl Trop Dis</addtitle><date>2011-07-01</date><risdate>2011</risdate><volume>5</volume><issue>7</issue><spage>e1225</spage><epage>e1225</epage><pages>e1225-e1225</pages><issn>1935-2735</issn><issn>1935-2727</issn><eissn>1935-2735</eissn><abstract>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.
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.
These studies suggest that the outer membrane form of T. spiralis paramyosin plays an important role in the evasion of the host complement attack.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>21750743</pmid><doi>10.1371/journal.pntd.0001225</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Antigens Blotting, Western Care and treatment Complement C8 - antagonists & inhibitors Complement C8 - immunology Complement C8 - metabolism Complement C9 - antagonists & inhibitors Complement C9 - immunology Complement C9 - metabolism Complement Membrane Attack Complex - antagonists & inhibitors Developmental stages Diagnosis Erythrocytes Female Fluorescent Antibody Technique Gene Expression Profiling Health aspects Hemolysis Immune Evasion Infections Invertebrates Laboratory animals Larvae Medicine Mice Mice, Inbred ICR Microscopy, Immunoelectron Molecular Sequence Data Nematoda Parasites Parasitic diseases Polymerization Protein Binding Proteins Rabbits Reverse Transcriptase Polymerase Chain Reaction RNA, Helminth - genetics RNA, Messenger - genetics Sequence Analysis, DNA Trichinella spiralis - immunology Trichinosis Tropical diseases Tropomyosin - immunology Tropomyosin - metabolism Worms |
| title | Trichinella spiralis paramyosin binds to C8 and C9 and protects the tissue-dwelling nematode from being attacked by host complement |
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