Distinct functions of antigenic sites of the HN glycoprotein of sendai virus
Identifieur interne : 000C18 ( Istex/Corpus ); précédent : 000C17; suivant : 000C19Distinct functions of antigenic sites of the HN glycoprotein of sendai virus
Auteurs : A. Portner ; R. A. Scroggs ; D. W. MetzgerSource :
- Virology [ 0042-6822 ] ; 1987.
English descriptors
- Teeft :
- Adsorption, Antibody, Antigenic, Antigenic site, Antigenic sites, Antigenic structure, Ascites fluids, Assay, Binding activity, Biological activities, Biological functions, Cell fusion, Choppin, Conformational changes, Elisa, Epitope, Glycoprotein, Hemagglutinating, Hemagglutination, Hemolysis, Hemolysis activity, Hemolysis inhibition, Host cells, Monoclonal, Monoclonal antibodies, Neuraminidase, Neuraminidase activities, Neuraminidase activity, Newcastle disease virus, Nonreciprocal competitions, Paramyxovirus, Paramyxovirus glycoproteins, Portner, Scheid, Sendai, Sendai virus, Viral, Virion, Virology, Virus, Virus adsorption, Virus growth, Virus infection, Virus penetration, Virus production, Virus release.
Abstract
Abstract: Monoclonal antibodies specific for the hemagglutinin-neuraminidase (HN) glycoprotein of Sendai virus were used to examine the antigenic structure of HN and its role in the initiation of infection and immunity. Using 10 anti-HN antibodies, four distinct antigenic sites designated I–IV were topographically mapped on the HN molecule by competitive-binding assays. To relate the biological functions of HN to its antigenic structure, anti-HN antibodies were analyzed for their inhibitory activity in neuraminidase, hemagglutination, and hemolysis inhibition tests. Antibodies to antigenic site I inhibited hemagglutination and one of these antibodies also inhibited neuraminidase activity. Antibodies to site II inhibited neither activity. However, hemolysis an F protein activity was inhibited, suggesting that these antibodies which bind to HN interfere with F-mediated fusion. Antigenic sites III and IV had different effects on the hemagglutinating and neuraminidase functions of HN: Site III antibodies inhibited hemagglutination while antibodies to site IV only inhibited neuraminidase activity. Antibodies to each antigenic site inhibited virus production. Since antibodies to sites I and III inhibited hemagglutination, it is likely that they block virus adsorption. Antibodies to HN site II only inhibited hemolysis, and therefore, may prevent virus penetration. Antibodies reacting with site IV inhibited virus production after virus penetration. Since neuraminidase activity was the only function inhibited, the viral enzyme may be involved in virus release. The fact that site IV antibodies inhibited neuraminidase but not hemagglutination suggests that these sites are distinct.
Url:
DOI: 10.1016/0042-6822(87)90238-8
Links to Exploration step
ISTEX:A2AAAE9CF1BC398FC034872B43CA3CFD2EA9D2A8Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Distinct functions of antigenic sites of the HN glycoprotein of sendai virus</title><author><name sortKey="Portner, A" sort="Portner, A" uniqKey="Portner A" first="A." last="Portner">A. Portner</name><affiliation><mods:affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</mods:affiliation></affiliation></author><author><name sortKey="Scroggs, R A" sort="Scroggs, R A" uniqKey="Scroggs R" first="R. A." last="Scroggs">R. A. Scroggs</name><affiliation><mods:affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</mods:affiliation></affiliation></author><author><name sortKey="Metzger, D W" sort="Metzger, D W" uniqKey="Metzger D" first="D. W." last="Metzger">D. W. Metzger</name><affiliation><mods:affiliation>Department of Immunology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:A2AAAE9CF1BC398FC034872B43CA3CFD2EA9D2A8</idno><date when="1987" year="1987">1987</date><idno type="doi">10.1016/0042-6822(87)90238-8</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-B54QKJ4Q-J/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000C18</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000C18</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Distinct functions of antigenic sites of the HN glycoprotein of sendai virus</title><author><name sortKey="Portner, A" sort="Portner, A" uniqKey="Portner A" first="A." last="Portner">A. Portner</name><affiliation><mods:affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</mods:affiliation></affiliation></author><author><name sortKey="Scroggs, R A" sort="Scroggs, R A" uniqKey="Scroggs R" first="R. A." last="Scroggs">R. A. Scroggs</name><affiliation><mods:affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</mods:affiliation></affiliation></author><author><name sortKey="Metzger, D W" sort="Metzger, D W" uniqKey="Metzger D" first="D. W." last="Metzger">D. W. Metzger</name><affiliation><mods:affiliation>Department of Immunology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="ISSN">0042-6822</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987">1987</date><biblScope unit="volume">158</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="61">61</biblScope><biblScope unit="page" to="68">68</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Adsorption</term><term>Antibody</term><term>Antigenic</term><term>Antigenic site</term><term>Antigenic sites</term><term>Antigenic structure</term><term>Ascites fluids</term><term>Assay</term><term>Binding activity</term><term>Biological activities</term><term>Biological functions</term><term>Cell fusion</term><term>Choppin</term><term>Conformational changes</term><term>Elisa</term><term>Epitope</term><term>Glycoprotein</term><term>Hemagglutinating</term><term>Hemagglutination</term><term>Hemolysis</term><term>Hemolysis activity</term><term>Hemolysis inhibition</term><term>Host cells</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Neuraminidase</term><term>Neuraminidase activities</term><term>Neuraminidase activity</term><term>Newcastle disease virus</term><term>Nonreciprocal competitions</term><term>Paramyxovirus</term><term>Paramyxovirus glycoproteins</term><term>Portner</term><term>Scheid</term><term>Sendai</term><term>Sendai virus</term><term>Viral</term><term>Virion</term><term>Virology</term><term>Virus</term><term>Virus adsorption</term><term>Virus growth</term><term>Virus infection</term><term>Virus penetration</term><term>Virus production</term><term>Virus release</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Monoclonal antibodies specific for the hemagglutinin-neuraminidase (HN) glycoprotein of Sendai virus were used to examine the antigenic structure of HN and its role in the initiation of infection and immunity. Using 10 anti-HN antibodies, four distinct antigenic sites designated I–IV were topographically mapped on the HN molecule by competitive-binding assays. To relate the biological functions of HN to its antigenic structure, anti-HN antibodies were analyzed for their inhibitory activity in neuraminidase, hemagglutination, and hemolysis inhibition tests. Antibodies to antigenic site I inhibited hemagglutination and one of these antibodies also inhibited neuraminidase activity. Antibodies to site II inhibited neither activity. However, hemolysis an F protein activity was inhibited, suggesting that these antibodies which bind to HN interfere with F-mediated fusion. Antigenic sites III and IV had different effects on the hemagglutinating and neuraminidase functions of HN: Site III antibodies inhibited hemagglutination while antibodies to site IV only inhibited neuraminidase activity. Antibodies to each antigenic site inhibited virus production. Since antibodies to sites I and III inhibited hemagglutination, it is likely that they block virus adsorption. Antibodies to HN site II only inhibited hemolysis, and therefore, may prevent virus penetration. Antibodies reacting with site IV inhibited virus production after virus penetration. Since neuraminidase activity was the only function inhibited, the viral enzyme may be involved in virus release. The fact that site IV antibodies inhibited neuraminidase but not hemagglutination suggests that these sites are distinct.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>antigenic</json:string><json:string>neuraminidase</json:string><json:string>sendai</json:string><json:string>glycoprotein</json:string><json:string>hemolysis</json:string><json:string>epitope</json:string><json:string>sendai virus</json:string><json:string>monoclonal</json:string><json:string>antigenic sites</json:string><json:string>virology</json:string><json:string>monoclonal antibodies</json:string><json:string>hemagglutination</json:string><json:string>neuraminidase activity</json:string><json:string>elisa</json:string><json:string>virion</json:string><json:string>viral</json:string><json:string>adsorption</json:string><json:string>scheid</json:string><json:string>choppin</json:string><json:string>antigenic site</json:string><json:string>hemagglutinating</json:string><json:string>virus penetration</json:string><json:string>portner</json:string><json:string>paramyxovirus</json:string><json:string>biological activities</json:string><json:string>neuraminidase activities</json:string><json:string>antibody</json:string><json:string>virus adsorption</json:string><json:string>newcastle disease virus</json:string><json:string>virus production</json:string><json:string>assay</json:string><json:string>antigenic structure</json:string><json:string>virus release</json:string><json:string>conformational changes</json:string><json:string>biological functions</json:string><json:string>virus growth</json:string><json:string>virus</json:string><json:string>cell fusion</json:string><json:string>ascites fluids</json:string><json:string>hemolysis inhibition</json:string><json:string>binding activity</json:string><json:string>virus infection</json:string><json:string>nonreciprocal competitions</json:string><json:string>hemolysis activity</json:string><json:string>host cells</json:string><json:string>paramyxovirus glycoproteins</json:string></teeft></keywords><author><json:item><name>A. Portner</name><affiliations><json:string>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</json:string></affiliations></json:item><json:item><name>R.A. Scroggs</name><affiliations><json:string>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</json:string></affiliations></json:item><json:item><name>D.W. Metzger</name><affiliations><json:string>Department of Immunology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-B54QKJ4Q-J</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Monoclonal antibodies specific for the hemagglutinin-neuraminidase (HN) glycoprotein of Sendai virus were used to examine the antigenic structure of HN and its role in the initiation of infection and immunity. Using 10 anti-HN antibodies, four distinct antigenic sites designated I–IV were topographically mapped on the HN molecule by competitive-binding assays. To relate the biological functions of HN to its antigenic structure, anti-HN antibodies were analyzed for their inhibitory activity in neuraminidase, hemagglutination, and hemolysis inhibition tests. Antibodies to antigenic site I inhibited hemagglutination and one of these antibodies also inhibited neuraminidase activity. Antibodies to site II inhibited neither activity. However, hemolysis an F protein activity was inhibited, suggesting that these antibodies which bind to HN interfere with F-mediated fusion. Antigenic sites III and IV had different effects on the hemagglutinating and neuraminidase functions of HN: Site III antibodies inhibited hemagglutination while antibodies to site IV only inhibited neuraminidase activity. Antibodies to each antigenic site inhibited virus production. Since antibodies to sites I and III inhibited hemagglutination, it is likely that they block virus adsorption. Antibodies to HN site II only inhibited hemolysis, and therefore, may prevent virus penetration. Antibodies reacting with site IV inhibited virus production after virus penetration. Since neuraminidase activity was the only function inhibited, the viral enzyme may be involved in virus release. The fact that site IV antibodies inhibited neuraminidase but not hemagglutination suggests that these sites are distinct.</abstract><qualityIndicators><score>9.221</score><pdfWordCount>4413</pdfWordCount><pdfCharCount>29068</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>8</pdfPageCount><pdfPageSize>612.28 x 792.28 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>234</abstractWordCount><abstractCharCount>1699</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Distinct functions of antigenic sites of the HN glycoprotein of sendai virus</title><pmid><json:string>2437698</json:string></pmid><pii><json:string>0042-6822(87)90238-8</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. USA</title><language><json:string>unknown</json:string></language><volume>79</volume><pages><first>5862</first><last>5866</last></pages></serie><host><title>Virology</title><language><json:string>unknown</json:string></language><publicationDate>1987</publicationDate><issn><json:string>0042-6822</json:string></issn><pii><json:string>S0042-6822(00)X0306-6</json:string></pii><volume>158</volume><issue>1</issue><pages><first>61</first><last>68</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1987</json:string><json:string>35S</json:string></date><geogName><json:string>Ill</json:string></geogName><orgName><json:string>Academic Press, Inc</json:string><json:string>DuPont Co., Wilmington</json:string><json:string>American Lebanese Syrian Associated Charities of St</json:string><json:string>Jude Children’s Research Hospital</json:string><json:string>National Cancer Institute</json:string><json:string>Salk Institute, La Jolla, California</json:string><json:string>National Institute of Allergy and Infectious Diseases</json:string><json:string>Grand Island Biological Co.</json:string><json:string>Academtc Press, Inc.</json:string><json:string>Calbiochem</json:string><json:string>Public Health Service Research Grant Al</json:string><json:string>Cancer Center Support Grant CA 21765</json:string></orgName><orgName_funder><json:string>Public Health Service Research Grant Al</json:string><json:string>Cancer Center Support Grant CA 21765</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Van Wyke</json:string><json:string>P.O. Box</json:string><json:string>Previous</json:string><json:string>The</json:string><json:string>Glenith D. White</json:string><json:string>Marlene Jacks</json:string></persName><placeName><json:string>NY</json:string><json:string>SENDAI</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Poste and Pasternak, 1978</json:string><json:string>lorio and Bratt, 1984</json:string><json:string>Smith and Hightower, 1983</json:string><json:string>Heath et al., 1983</json:string><json:string>Scheid et al., 1972</json:string><json:string>Hsu et al., 1982</json:string><json:string>Scheid and Choppin, 1974, 1977</json:string><json:string>Scheid and Choppin, 1973</json:string><json:string>Portner et al., 1980</json:string><json:string>Miura et al., 1982</json:string><json:string>Jackson and Webster, 1982</json:string><json:string>Hsu et al. (1979)</json:string><json:string>Tozawa et al., 1973</json:string><json:string>Pot-trier and Kingsbury, 1976</json:string><json:string>Gitman and Loyter, 1984</json:string><json:string>Deshpande and Partner, 1984, 1985</json:string><json:string>Homma and Ohuchi, 1973</json:string><json:string>Lubeck and Gerhard, 1982</json:string><json:string>Partner, 1981</json:string><json:string>Heath et al., 1986</json:string><json:string>Laemmli, 1970</json:string><json:string>&vell and Grandien, 1982</json:string><json:string>Murti and Goorha (1983)</json:string><json:string>Yewdell and Gerhard, 1982</json:string><json:string>Nagai et al., 1976</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-B54QKJ4Q-J</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - virology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - virology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Immunology and Microbiology</json:string><json:string>3 - Virology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1987</publicationDate><copyrightDate>1987</copyrightDate><doi><json:string>10.1016/0042-6822(87)90238-8</json:string></doi><id>A2AAAE9CF1BC398FC034872B43CA3CFD2EA9D2A8</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-B54QKJ4Q-J/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-B54QKJ4Q-J/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-B54QKJ4Q-J/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Distinct functions of antigenic sites of the HN glycoprotein of sendai virus</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1987</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Distinct functions of antigenic sites of the HN glycoprotein of sendai virus</title><author xml:id="author-0000"><persName><forename type="first">A.</forename><surname>Portner</surname></persName><note type="biography">To whom requests for reprints should be addressed.</note><affiliation>To whom requests for reprints should be addressed.</affiliation><affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</affiliation></author><author xml:id="author-0001"><persName><forename type="first">R.A.</forename><surname>Scroggs</surname></persName><affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</affiliation></author><author xml:id="author-0002"><persName><forename type="first">D.W.</forename><surname>Metzger</surname></persName><affiliation>Department of Immunology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</affiliation></author><idno type="istex">A2AAAE9CF1BC398FC034872B43CA3CFD2EA9D2A8</idno><idno type="ark">ark:/67375/6H6-B54QKJ4Q-J</idno><idno type="DOI">10.1016/0042-6822(87)90238-8</idno><idno type="PII">0042-6822(87)90238-8</idno></analytic><monogr><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="pISSN">0042-6822</idno><idno type="PII">S0042-6822(00)X0306-6</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987"></date><biblScope unit="volume">158</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="61">61</biblScope><biblScope unit="page" to="68">68</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1987</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Monoclonal antibodies specific for the hemagglutinin-neuraminidase (HN) glycoprotein of Sendai virus were used to examine the antigenic structure of HN and its role in the initiation of infection and immunity. Using 10 anti-HN antibodies, four distinct antigenic sites designated I–IV were topographically mapped on the HN molecule by competitive-binding assays. To relate the biological functions of HN to its antigenic structure, anti-HN antibodies were analyzed for their inhibitory activity in neuraminidase, hemagglutination, and hemolysis inhibition tests. Antibodies to antigenic site I inhibited hemagglutination and one of these antibodies also inhibited neuraminidase activity. Antibodies to site II inhibited neither activity. However, hemolysis an F protein activity was inhibited, suggesting that these antibodies which bind to HN interfere with F-mediated fusion. Antigenic sites III and IV had different effects on the hemagglutinating and neuraminidase functions of HN: Site III antibodies inhibited hemagglutination while antibodies to site IV only inhibited neuraminidase activity. Antibodies to each antigenic site inhibited virus production. Since antibodies to sites I and III inhibited hemagglutination, it is likely that they block virus adsorption. Antibodies to HN site II only inhibited hemolysis, and therefore, may prevent virus penetration. Antibodies reacting with site IV inhibited virus production after virus penetration. Since neuraminidase activity was the only function inhibited, the viral enzyme may be involved in virus release. The fact that site IV antibodies inhibited neuraminidase but not hemagglutination suggests that these sites are distinct.</p></abstract></profileDesc><revisionDesc><change when="1987">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-B54QKJ4Q-J/fulltext.txt</uri></json:item></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>YVIRO</jid><aid>87902388</aid><ce:pii>0042-6822(87)90238-8</ce:pii><ce:doi>10.1016/0042-6822(87)90238-8</ce:doi><ce:copyright type="unknown" year="1987"></ce:copyright></item-info><head><ce:title>Distinct functions of antigenic sites of the HN glycoprotein of sendai virus</ce:title><ce:author-group><ce:author><ce:given-name>A.</ce:given-name><ce:surname>Portner</ce:surname><ce:cross-ref refid="COR1"><ce:sup>1</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>R.A.</ce:given-name><ce:surname>Scroggs</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>D.W.</ce:given-name><ce:surname>Metzger</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 Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Department of Immunology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>1</ce:label><ce:text>To whom requests for reprints should be addressed.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="11" month="9" year="1986"></ce:date-received><ce:date-accepted day="14" month="12" year="1986"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Monoclonal antibodies specific for the hemagglutinin-neuraminidase (HN) glycoprotein of Sendai virus were used to examine the antigenic structure of HN and its role in the initiation of infection and immunity. Using 10 anti-HN antibodies, four distinct antigenic sites designated I–IV were topographically mapped on the HN molecule by competitive-binding assays. To relate the biological functions of HN to its antigenic structure, anti-HN antibodies were analyzed for their inhibitory activity in neuraminidase, hemagglutination, and hemolysis inhibition tests. Antibodies to antigenic site I inhibited hemagglutination and one of these antibodies also inhibited neuraminidase activity. Antibodies to site II inhibited neither activity. However, hemolysis an F protein activity was inhibited, suggesting that these antibodies which bind to HN interfere with F-mediated fusion. Antigenic sites III and IV had different effects on the hemagglutinating and neuraminidase functions of HN: Site III antibodies inhibited hemagglutination while antibodies to site IV only inhibited neuraminidase activity. Antibodies to each antigenic site inhibited virus production. Since antibodies to sites I and III inhibited hemagglutination, it is likely that they block virus adsorption. Antibodies to HN site II only inhibited hemolysis, and therefore, may prevent virus penetration. Antibodies reacting with site IV inhibited virus production after virus penetration. Since neuraminidase activity was the only function inhibited, the viral enzyme may be involved in virus release. The fact that site IV antibodies inhibited neuraminidase but not hemagglutination suggests that these sites are distinct.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Distinct functions of antigenic sites of the HN glycoprotein of sendai virus</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Distinct functions of antigenic sites of the HN glycoprotein of sendai virus</title></titleInfo><name type="personal"><namePart type="given">A.</namePart><namePart type="family">Portner</namePart><affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</affiliation><description>To whom requests for reprints should be addressed.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">R.A.</namePart><namePart type="family">Scroggs</namePart><affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">D.W.</namePart><namePart type="family">Metzger</namePart><affiliation>Department of Immunology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1987</dateIssued><copyrightDate encoding="w3cdtf">1987</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Monoclonal antibodies specific for the hemagglutinin-neuraminidase (HN) glycoprotein of Sendai virus were used to examine the antigenic structure of HN and its role in the initiation of infection and immunity. Using 10 anti-HN antibodies, four distinct antigenic sites designated I–IV were topographically mapped on the HN molecule by competitive-binding assays. To relate the biological functions of HN to its antigenic structure, anti-HN antibodies were analyzed for their inhibitory activity in neuraminidase, hemagglutination, and hemolysis inhibition tests. Antibodies to antigenic site I inhibited hemagglutination and one of these antibodies also inhibited neuraminidase activity. Antibodies to site II inhibited neither activity. However, hemolysis an F protein activity was inhibited, suggesting that these antibodies which bind to HN interfere with F-mediated fusion. Antigenic sites III and IV had different effects on the hemagglutinating and neuraminidase functions of HN: Site III antibodies inhibited hemagglutination while antibodies to site IV only inhibited neuraminidase activity. Antibodies to each antigenic site inhibited virus production. Since antibodies to sites I and III inhibited hemagglutination, it is likely that they block virus adsorption. Antibodies to HN site II only inhibited hemolysis, and therefore, may prevent virus penetration. Antibodies reacting with site IV inhibited virus production after virus penetration. Since neuraminidase activity was the only function inhibited, the viral enzyme may be involved in virus release. The fact that site IV antibodies inhibited neuraminidase but not hemagglutination suggests that these sites are distinct.</abstract><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><titleInfo type="abbreviated"><title>YVIRO</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1987</dateIssued></originInfo><identifier type="ISSN">0042-6822</identifier><identifier type="PII">S0042-6822(00)X0306-6</identifier><part><date>1987</date><detail type="volume"><number>158</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>264</end></extent><extent unit="pages"><start>61</start><end>68</end></extent></part></relatedItem><identifier type="istex">A2AAAE9CF1BC398FC034872B43CA3CFD2EA9D2A8</identifier><identifier type="ark">ark:/67375/6H6-B54QKJ4Q-J</identifier><identifier type="DOI">10.1016/0042-6822(87)90238-8</identifier><identifier type="PII">0042-6822(87)90238-8</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-B54QKJ4Q-J/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000C18 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 000C18 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= H2N2V1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:A2AAAE9CF1BC398FC034872B43CA3CFD2EA9D2A8
|texte= Distinct functions of antigenic sites of the HN glycoprotein of sendai virus
}}
| This area was generated with Dilib version V0.6.33. |  |