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
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<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>
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<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>
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<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>
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<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>
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<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>
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<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>
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<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>
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