A topographic map of the enzyme active center and antigenic sites on the neuraminidase of influenza virus A/Tokyo/3/67 (H2N2)
Identifieur interne : 002682 ( Main/Exploration ); précédent : 002681; suivant : 002683A topographic map of the enzyme active center and antigenic sites on the neuraminidase of influenza virus A/Tokyo/3/67 (H2N2)
Auteurs : David C. Jackson [États-Unis] ; R. G. Webster [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1982.
Descripteurs français
- KwdFr :
- MESH :
- antagonistes et inhibiteurs : Sialidase.
- enzymologie : Virus de la grippe A.
- immunologie : Hémagglutinines virales, Sialidase.
- Anticorps monoclonaux, Conformation des protéines, Sites de fixation, Sous-type H2N2 du virus de la grippe A, Épitopes.
English descriptors
- KwdEn :
- MESH :
- chemical , antagonists & inhibitors : Neuraminidase.
- chemical , immunology : Hemagglutinins, Viral, Neuraminidase.
- enzymology : Influenza A virus.
- Teeft :
- Academic press, Active center, Active site, Antibodies, Monoclonal, Antibody, Antigenic, Antigenic determinants, Antigenic site, Antigenic sites, Antigenic variants, Ascitic, Ascitic fluid, Ascitic fluids, Assay, Binding Sites, Competitive radioimmunoassays, Conformational change, Conformational changes, Enzyme activity, Epitopes, Fetuin, Hemagglutinin, Hemagglutinin molecule, Hindrance, Hong kong, Influenza, Influenza A Virus, H2N2 Subtype, Influenza virus, Influenza virus hemagglutinin, Influenza virus neuraminidase, Influenza viruses, Lactose, Laver, Molecular weight, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Monoclone, Neuraminidase, Neuraminidase activity, Neuraminidase molecule, Neuraminyl, Neuraminyl lactose, Other members, Percentage inhibition, Protein Conformation, Radioimmunoassay, Serial dilutions, Steric, Steric hindrance, Virology.
Abstract
Abstract: The antigenic structure of an influenza virus neuraminidase was probed with a panel of eight monoclonal antibodies and two different-sized substrates, fetuin and N-acetylneuraminyl lactose. Results of competitive radioimmunoassays between monoclonal antibodies indicated the existence of three overlapping antigenic sites. The effects of the same panel of monoclonal antibodies on the enzyme-catalyzed hydrolysis of sialic acid from fetuin (molecular weight 50,000 daltons) and from N-acetylneuraminyl lactose (molecular weight 600) were also examined. These results indicated that each of the antibodies prevented the approach of fetuin to the enzyme active center, whereas only three inhibited hydrolysis of N-acetylneuraminyl lactose. Taken together, the results suggest a topological map for the arrangement of the enzyme active center and three overlapping antigenic sites of the neuraminidase.
Url:
DOI: 10.1016/0042-6822(82)90295-1
Affiliations:
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Box 318, Memphis</wicri:cityArea></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="1982">1982</date><biblScope unit="volume">123</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="69">69</biblScope><biblScope unit="page" to="77">77</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Binding Sites</term><term>Epitopes</term><term>Hemagglutinins, Viral (immunology)</term><term>Influenza A Virus, H2N2 Subtype</term><term>Influenza A virus (enzymology)</term><term>Neuraminidase (antagonists & inhibitors)</term><term>Neuraminidase (immunology)</term><term>Protein Conformation</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Anticorps monoclonaux</term><term>Conformation des protéines</term><term>Hémagglutinines virales (immunologie)</term><term>Sialidase (antagonistes et inhibiteurs)</term><term>Sialidase (immunologie)</term><term>Sites de fixation</term><term>Sous-type H2N2 du virus de la grippe A</term><term>Virus de la grippe A (enzymologie)</term><term>Épitopes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Neuraminidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Hemagglutinins, Viral</term><term>Neuraminidase</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Sialidase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Hémagglutinines virales</term><term>Sialidase</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Active center</term><term>Active site</term><term>Antibodies, Monoclonal</term><term>Antibody</term><term>Antigenic</term><term>Antigenic determinants</term><term>Antigenic site</term><term>Antigenic sites</term><term>Antigenic variants</term><term>Ascitic</term><term>Ascitic fluid</term><term>Ascitic fluids</term><term>Assay</term><term>Binding Sites</term><term>Competitive radioimmunoassays</term><term>Conformational change</term><term>Conformational changes</term><term>Enzyme activity</term><term>Epitopes</term><term>Fetuin</term><term>Hemagglutinin</term><term>Hemagglutinin molecule</term><term>Hindrance</term><term>Hong kong</term><term>Influenza</term><term>Influenza A Virus, H2N2 Subtype</term><term>Influenza virus</term><term>Influenza virus hemagglutinin</term><term>Influenza virus neuraminidase</term><term>Influenza viruses</term><term>Lactose</term><term>Laver</term><term>Molecular weight</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Monoclonal antibody</term><term>Monoclone</term><term>Neuraminidase</term><term>Neuraminidase activity</term><term>Neuraminidase molecule</term><term>Neuraminyl</term><term>Neuraminyl lactose</term><term>Other members</term><term>Percentage inhibition</term><term>Protein Conformation</term><term>Radioimmunoassay</term><term>Serial dilutions</term><term>Steric</term><term>Steric hindrance</term><term>Virology</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Anticorps monoclonaux</term><term>Conformation des protéines</term><term>Sites de fixation</term><term>Sous-type H2N2 du virus de la grippe A</term><term>Épitopes</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The antigenic structure of an influenza virus neuraminidase was probed with a panel of eight monoclonal antibodies and two different-sized substrates, fetuin and N-acetylneuraminyl lactose. Results of competitive radioimmunoassays between monoclonal antibodies indicated the existence of three overlapping antigenic sites. The effects of the same panel of monoclonal antibodies on the enzyme-catalyzed hydrolysis of sialic acid from fetuin (molecular weight 50,000 daltons) and from N-acetylneuraminyl lactose (molecular weight 600) were also examined. These results indicated that each of the antibodies prevented the approach of fetuin to the enzyme active center, whereas only three inhibited hydrolysis of N-acetylneuraminyl lactose. Taken together, the results suggest a topological map for the arrangement of the enzyme active center and three overlapping antigenic sites of the neuraminidase.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Tennessee</li></region></list><tree><country name="États-Unis"><region name="Tennessee"><name sortKey="Jackson, David C" sort="Jackson, David C" uniqKey="Jackson D" first="David C." last="Jackson">David C. Jackson</name></region><name sortKey="Webster, R G" sort="Webster, R G" uniqKey="Webster R" first="R. G." last="Webster">R. G. Webster</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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