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Distinct functions of antigenic sites of the HN glycoprotein of sendai virus

Identifieur interne : 002417 ( Main/Merge ); précédent : 002416; suivant : 002418

Distinct functions of antigenic sites of the HN glycoprotein of sendai virus

Auteurs : A. Portner [États-Unis] ; R. A. Scroggs [États-Unis] ; D. W. Metzger [États-Unis]

Source :

Virology [ 0042-6822 ] ; 1987.

RBID : ISTEX:A2AAAE9CF1BC398FC034872B43CA3CFD2EA9D2A8

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:

https://api.istex.fr/ark:/67375/6H6-B54QKJ4Q-J/fulltext.pdf

DOI: 10.1016/0042-6822(87)90238-8

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Le document en format XML

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<author><name sortKey="Metzger, D W" sort="Metzger, D W" uniqKey="Metzger D" first="D. W." last="Metzger">D. W. Metzger</name>
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<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>
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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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Distinct functions of antigenic sites of the HN glycoprotein of sendai virus

Distinct functions of antigenic sites of the HN glycoprotein of sendai virus

Source :

English descriptors

Abstract

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Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri