Ascaris suum: Cuticular binding of the third component of complement by early larval stages
Identifieur interne : 003873 ( Istex/Corpus ); précédent : 003872; suivant : 003874Ascaris suum: Cuticular binding of the third component of complement by early larval stages
Auteurs : Ruth Leventhal ; E. J. L. SoulsbySource :
- Experimental Parasitology [ 0014-4894 ] ; 1976.
Abstract
Binding of the third component of complement (C3) to infective or parasitic larvae of Ascaris suum was evaluated by the direct fluorescent antibody technique and by detection of radiolabeled-C3 binding. Ensheathed infective-stage larvae bound C3 as detected by both techniques. Fluorescence studies indicated C3 binding was over the entire surface of the infective-stage sheath. Day 1 parasitic larvae bound C3 spottily only over the head and tail regions. Day 2 parasitic larvae however bound C3 over the entire surface. C3 uptake as detected by fluorescence was inhibited in 56 C-heated serum, but not in 50 C-heated serum, when either normal or C4-deficient guinea pig serum (C4D) was used as the C3 source. Radiolabeled-C3 binding was enhanced in the presence of unheated C4D serum and inhibited by Ca2+ chelation. C3 binding appeared dependent on neither classical nor alternative pathway activation of complement in this study.
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DOI: 10.1016/0014-4894(77)90115-1
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Soulsby</name><affiliation><mods:affiliation>Department of Medical Technology, School of Allied Medical Professions, University of Pennsylvania, Philadelphia, Pennsylvania 19104, U.S.A.</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:7A7ED811A092BD609FB675D7D46F935FA115E9B7</idno><date when="1977" year="1977">1977</date><idno type="doi">10.1016/0014-4894(77)90115-1</idno><idno type="url">https://api.istex.fr/document/7A7ED811A092BD609FB675D7D46F935FA115E9B7/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">003873</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Ascaris suum: Cuticular binding of the third component of complement by early larval stages</title><author><name sortKey="Leventhal, Ruth" sort="Leventhal, Ruth" uniqKey="Leventhal R" first="Ruth" last="Leventhal">Ruth Leventhal</name><affiliation><mods:affiliation>Department of Pathobiolagy, School of Veterinary Medicine, and Pepper Laboratories, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, U.S.A.</mods:affiliation></affiliation></author><author><name sortKey="Soulsby, E J L" sort="Soulsby, E J L" uniqKey="Soulsby E" first="E. J. L." last="Soulsby">E. J. L. Soulsby</name><affiliation><mods:affiliation>Department of Medical Technology, School of Allied Medical Professions, University of Pennsylvania, Philadelphia, Pennsylvania 19104, U.S.A.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Experimental Parasitology</title><title level="j" type="abbrev">YEXPR</title><idno type="ISSN">0014-4894</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1976">1976</date><biblScope unit="volume">41</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="423">423</biblScope><biblScope unit="page" to="431">431</biblScope></imprint><idno type="ISSN">0014-4894</idno></series><idno type="istex">7A7ED811A092BD609FB675D7D46F935FA115E9B7</idno><idno type="DOI">10.1016/0014-4894(77)90115-1</idno><idno type="PII">0014-4894(77)90115-1</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0014-4894</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Binding of the third component of complement (C3) to infective or parasitic larvae of Ascaris suum was evaluated by the direct fluorescent antibody technique and by detection of radiolabeled-C3 binding. Ensheathed infective-stage larvae bound C3 as detected by both techniques. Fluorescence studies indicated C3 binding was over the entire surface of the infective-stage sheath. Day 1 parasitic larvae bound C3 spottily only over the head and tail regions. Day 2 parasitic larvae however bound C3 over the entire surface. C3 uptake as detected by fluorescence was inhibited in 56 C-heated serum, but not in 50 C-heated serum, when either normal or C4-deficient guinea pig serum (C4D) was used as the C3 source. Radiolabeled-C3 binding was enhanced in the presence of unheated C4D serum and inhibited by Ca2+ chelation. 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Soulsby</name><affiliations><json:string>Department of Medical Technology, School of Allied Medical Professions, University of Pennsylvania, Philadelphia, Pennsylvania 19104, U.S.A.</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Ascaris suum</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Nematodes</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Larva</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Cuticle</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Sheath</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Fluorescent antibody test</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Guinea pig serum</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Complement</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>C3</value></json:item></subject><language><json:string>eng</json:string></language><abstract>Binding of the third component of complement (C3) to infective or parasitic larvae of Ascaris suum was evaluated by the direct fluorescent antibody technique and by detection of radiolabeled-C3 binding. Ensheathed infective-stage larvae bound C3 as detected by both techniques. Fluorescence studies indicated C3 binding was over the entire surface of the infective-stage sheath. Day 1 parasitic larvae bound C3 spottily only over the head and tail regions. Day 2 parasitic larvae however bound C3 over the entire surface. C3 uptake as detected by fluorescence was inhibited in 56 C-heated serum, but not in 50 C-heated serum, when either normal or C4-deficient guinea pig serum (C4D) was used as the C3 source. Radiolabeled-C3 binding was enhanced in the presence of unheated C4D serum and inhibited by Ca2+ chelation. 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Ensheathed infective-stage larvae bound C3 as detected by both techniques. Fluorescence studies indicated C3 binding was over the entire surface of the infective-stage sheath. Day 1 parasitic larvae bound C3 spottily only over the head and tail regions. Day 2 parasitic larvae however bound C3 over the entire surface. C3 uptake as detected by fluorescence was inhibited in 56 C-heated serum, but not in 50 C-heated serum, when either normal or C4-deficient guinea pig serum (C4D) was used as the C3 source. Radiolabeled-C3 binding was enhanced in the presence of unheated C4D serum and inhibited by Ca2+ chelation. C3 binding appeared dependent on neither classical nor alternative pathway activation of complement in this study.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Ascaris suum</term></item><item><term>Nematodes</term></item><item><term>Larva</term></item><item><term>Cuticle</term></item><item><term>Sheath</term></item><item><term>Fluorescent antibody test</term></item><item><term>Guinea pig serum</term></item><item><term>Complement</term></item><item><term>C3</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1976-07-13">Registration</change><change when="1976">Published</change></revisionDesc></teiHeader></istex:fulltextTEI></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>YEXPR</jid><aid>77901151</aid><ce:pii>0014-4894(77)90115-1</ce:pii><ce:doi>10.1016/0014-4894(77)90115-1</ce:doi><ce:copyright type="unknown" year="1977"></ce:copyright></item-info><head><ce:title><ce:italic>Ascaris suum:</ce:italic> Cuticular binding of the third component of complement by early larval stages</ce:title><ce:author-group><ce:author><ce:given-name>Ruth</ce:given-name><ce:surname>Leventhal</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>E.J.L.</ce:given-name><ce:surname>Soulsby</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Pathobiolagy, School of Veterinary Medicine, and Pepper Laboratories, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, U.S.A.</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Department of Medical Technology, School of Allied Medical Professions, University of Pennsylvania, Philadelphia, Pennsylvania 19104, U.S.A.</ce:textfn></ce:affiliation></ce:author-group><ce:date-accepted day="13" month="7" year="1976"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Binding of the third component of complement (C3) to infective or parasitic larvae of <ce:italic>Ascaris suum</ce:italic> was evaluated by the direct fluorescent antibody technique and by detection of radiolabeled-C3 binding. Ensheathed infective-stage larvae bound C3 as detected by both techniques. Fluorescence studies indicated C3 binding was over the entire surface of the infective-stage sheath. Day 1 parasitic larvae bound C3 spottily only over the head and tail regions. Day 2 parasitic larvae however bound C3 over the entire surface. C3 uptake as detected by fluorescence was inhibited in 56 C-heated serum, but not in 50 C-heated serum, when either normal or C4-deficient guinea pig serum (C4D) was used as the C3 source. Radiolabeled-C3 binding was enhanced in the presence of unheated C4D serum and inhibited by Ca<ce:sup>2+</ce:sup> chelation. C3 binding appeared dependent on neither classical nor alternative pathway activation of complement in this study.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text><ce:italic>Ascaris suum</ce:italic></ce:text></ce:keyword><ce:keyword><ce:text>Nematodes</ce:text></ce:keyword><ce:keyword><ce:text>Larva</ce:text></ce:keyword><ce:keyword><ce:text>Cuticle</ce:text></ce:keyword><ce:keyword><ce:text>Sheath</ce:text></ce:keyword><ce:keyword><ce:text>Fluorescent antibody test</ce:text></ce:keyword><ce:keyword><ce:text>Guinea pig serum</ce:text></ce:keyword><ce:keyword><ce:text>Complement</ce:text></ce:keyword><ce:keyword><ce:text>C3</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Ascaris suum: Cuticular binding of the third component of complement by early larval stages</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Cuticular binding of the third component of complement by early larval stages</title></titleInfo><name type="personal"><namePart type="given">Ruth</namePart><namePart type="family">Leventhal</namePart><affiliation>Department of Pathobiolagy, School of Veterinary Medicine, and Pepper Laboratories, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, U.S.A.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">E.J.L.</namePart><namePart type="family">Soulsby</namePart><affiliation>Department of Medical Technology, School of Allied Medical Professions, University of Pennsylvania, Philadelphia, Pennsylvania 19104, U.S.A.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1976</dateIssued><dateValid encoding="w3cdtf">1976-07-13</dateValid><copyrightDate encoding="w3cdtf">1977</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">Binding of the third component of complement (C3) to infective or parasitic larvae of Ascaris suum was evaluated by the direct fluorescent antibody technique and by detection of radiolabeled-C3 binding. Ensheathed infective-stage larvae bound C3 as detected by both techniques. Fluorescence studies indicated C3 binding was over the entire surface of the infective-stage sheath. Day 1 parasitic larvae bound C3 spottily only over the head and tail regions. Day 2 parasitic larvae however bound C3 over the entire surface. C3 uptake as detected by fluorescence was inhibited in 56 C-heated serum, but not in 50 C-heated serum, when either normal or C4-deficient guinea pig serum (C4D) was used as the C3 source. Radiolabeled-C3 binding was enhanced in the presence of unheated C4D serum and inhibited by Ca2+ chelation. C3 binding appeared dependent on neither classical nor alternative pathway activation of complement in this study.</abstract><subject><genre>Keywords</genre><topic>Ascaris suum</topic><topic>Nematodes</topic><topic>Larva</topic><topic>Cuticle</topic><topic>Sheath</topic><topic>Fluorescent antibody test</topic><topic>Guinea pig serum</topic><topic>Complement</topic><topic>C3</topic></subject><relatedItem type="host"><titleInfo><title>Experimental Parasitology</title></titleInfo><titleInfo type="abbreviated"><title>YEXPR</title></titleInfo><genre type="Journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">197704</dateIssued></originInfo><identifier type="ISSN">0014-4894</identifier><identifier type="PII">S0014-4894(00)X0273-1</identifier><part><date>197704</date><detail type="volume"><number>41</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue pages"><start>253</start><end>493</end></extent><extent unit="pages"><start>423</start><end>431</end></extent></part></relatedItem><identifier type="istex">7A7ED811A092BD609FB675D7D46F935FA115E9B7</identifier><identifier type="DOI">10.1016/0014-4894(77)90115-1</identifier><identifier type="PII">0014-4894(77)90115-1</identifier><recordInfo><recordContentSource>ELSEVIER</recordContentSource></recordInfo></mods></metadata><enrichments><istex:catWosTEI uri="https://api.istex.fr/document/7A7ED811A092BD609FB675D7D46F935FA115E9B7/enrichments/catWos"><teiHeader><profileDesc><textClass><classCode scheme="WOS">PARASITOLOGY</classCode></textClass></profileDesc></teiHeader></istex:catWosTEI></enrichments></istex></record>Pour manipuler ce document sous Unix (Dilib)
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