Antigenic and biological characterization of influenza virus neuraminidase (N2) with monoclonal antibodies
Identifieur interne : 002530 ( Main/Exploration ); précédent : 002529; suivant : 002531Antigenic and biological characterization of influenza virus neuraminidase (N2) with monoclonal antibodies
Auteurs : R. G. Webster [États-Unis] ; L. E. Brown [États-Unis] ; W. G. Laver [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1984.
Descripteurs français
- KwdFr :
- MESH :
- analyse : Sialidase, Épitopes.
- enzymologie : Virus de la grippe A.
- immunologie : Sialidase.
- Pascal (Inist)
- MESH :
- Wicri :
- topic : Enzyme.
English descriptors
- KwdEn :
- Animals, Antibodies, Monoclonal, Antigen-Antibody Complex, Antigenic determinant, Chick Embryo, Chickens, Enzyme, Epitopes (analysis), Erythrocytes, Immunological method, Influenza A virus (enzymology), Influenzavirus A, Monoclonal antibody, Neuraminidase, Neuraminidase (analysis), Neuraminidase (immunology), Orthomyxoviridae, Radioimmunoassay, Radioimmunoassay (methods), Virus.
- MESH :
- chemical , analysis : Epitopes, Neuraminidase.
- chemical , immunology : Neuraminidase.
- enzymology : Influenza A virus.
- methods : Radioimmunoassay.
- Teeft :
- Academic press, Agar, Agar overlay, Animals, Antibodies, Monoclonal, Antibody, Antigen-Antibody Complex, Antigenic, Antigenic areas, Antigenic mapping, Antigenic region, Antigenic regions, Antigenic site, Antigenic sites, Antigenic variants, Assay, Biological activities, Biological activity, Bottom surface, Catalytic, Catalytic activity, Catalytic center, Chemical modification, Chick Embryo, Chickens, Competitive radioimmunoassays, Elisa, Embryonated, Embryonated eggs, Enzyme activity, Epitope, Erythrocytes, Fetuin, Fetuin substrate, Field strains, Hemagglutinin, Hemagglutinin activity, Hemolysis, Infectivity, Influenza, Influenza virus, Influenza virus neuraminidase, Influenza viruses, Large number, Laver, Mdck, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Monoclonal variants, Neuraminidase, Neuraminidase molecule, Neutralization, Present study, Serial dilutions, Solubilized crystals, Tnbs, Variant, Virus, Virus growth, Virus infectivity, Virus release, Weight substrates.
Abstract
Abstract: Competitive radioimmunoassays using monoclonal antibodies established that the neuraminidase of A/RI/5+/57 (H2N2) influenza can be divided into four overlapping antigenic regions. Antigenic regions 1 and 4 are sufficiently far apart so that there was no competition between antibodies for these sites. Region 1 is conserved in neuraminidases from N2 viruses over a 10-year period, while the other regions changed antigenically during this time. The antibodies belonging to groups 2 and 3 completely inhibited catalytic activity on fetuin substrate, whereas antibodies in groups 1 and 4 inhibited weakly or not at all. Antigenic region 2 can be further divided into four overlapping areas (2a, 2b, 2c, and 2d) based on the reactivity patterns of monoclonal antibodies with antigenic variants, chemically modified neuraminidase, and the ability of the antibodies to inhibit enzyme activity of different molecular weight substrates. Previous studies [R. G. Webster, V. S. Hinshaw, and W. G. Laver (1982)Virology117, 93–104; D. C. Jackson and R. G. Webster (1982)Virology123, 69–77] characterized only region 2 of the neuraminidase molecule. Each of the monoclonal antibodies inhibited virus release from MDCK cells when incorporated in an agar overlay, and some antibodies in each group inhibited hemagglutination by intact virus, but only antibodies in group 2 neutralized virus in embryonated eggs and permitted selection of antigenic variants. The results indicate that antibodies to some antigenic sites on the neuraminidase may inhibit virus release more efficiently than others, depending on their relation to the enzyme active center. None of the monoclonal antibodies inhibited the hemolytic activity of viruses possessing N2. Based on antigenic mapping and biological properties of the monoclonal antibodies, a topographical map of the neuraminidase can be constructed. It is proposed that antigenic regions 1 and 4 are spacially separated and, based on their failure to inhibit biological activity, may be located on the bottom surface of the molecule; region 3 may be on the top surface of the molecule but at some distance from the catalytic center. Antigenic region 2 probably encompasses most of the top surface of the molecule; region 2d being closest to the enzyme center, with subregions 2a and 2b adjacent to it on the top surface. Chemical treatment of the neuraminidase with trinitrobenzenesulfonic acid (TNBS) causes modification of the 2b region, confirming the antigenic mapping results.
Url:
DOI: 10.1016/0042-6822(84)90114-4
Affiliations:
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Le document en format XML
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<term>Chick Embryo</term>
<term>Chickens</term>
<term>Enzyme</term>
<term>Epitopes (analysis)</term>
<term>Erythrocytes</term>
<term>Immunological method</term>
<term>Influenza A virus (enzymology)</term>
<term>Influenzavirus A</term>
<term>Monoclonal antibody</term>
<term>Neuraminidase</term>
<term>Neuraminidase (analysis)</term>
<term>Neuraminidase (immunology)</term>
<term>Orthomyxoviridae</term>
<term>Radioimmunoassay</term>
<term>Radioimmunoassay (methods)</term>
<term>Virus</term>
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<term>Anticorps monoclonaux</term>
<term>Complexe antigène-anticorps</term>
<term>Dosage radioimmunologique ()</term>
<term>Embryon de poulet</term>
<term>Poulets</term>
<term>Sialidase (analyse)</term>
<term>Sialidase (immunologie)</term>
<term>Virus de la grippe A (enzymologie)</term>
<term>Épitopes (analyse)</term>
<term>Érythrocytes</term>
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<term>Neuraminidase</term>
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<term>Épitopes</term>
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<term>Méthode radioimmunologique</term>
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<term>Antigenic mapping</term>
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<term>Influenza</term>
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<term>Influenza virus neuraminidase</term>
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<front><div type="abstract" xml:lang="en">Abstract: Competitive radioimmunoassays using monoclonal antibodies established that the neuraminidase of A/RI/5+/57 (H2N2) influenza can be divided into four overlapping antigenic regions. Antigenic regions 1 and 4 are sufficiently far apart so that there was no competition between antibodies for these sites. Region 1 is conserved in neuraminidases from N2 viruses over a 10-year period, while the other regions changed antigenically during this time. The antibodies belonging to groups 2 and 3 completely inhibited catalytic activity on fetuin substrate, whereas antibodies in groups 1 and 4 inhibited weakly or not at all. Antigenic region 2 can be further divided into four overlapping areas (2a, 2b, 2c, and 2d) based on the reactivity patterns of monoclonal antibodies with antigenic variants, chemically modified neuraminidase, and the ability of the antibodies to inhibit enzyme activity of different molecular weight substrates. Previous studies [R. G. Webster, V. S. Hinshaw, and W. G. Laver (1982)Virology117, 93–104; D. C. Jackson and R. G. Webster (1982)Virology123, 69–77] characterized only region 2 of the neuraminidase molecule. Each of the monoclonal antibodies inhibited virus release from MDCK cells when incorporated in an agar overlay, and some antibodies in each group inhibited hemagglutination by intact virus, but only antibodies in group 2 neutralized virus in embryonated eggs and permitted selection of antigenic variants. The results indicate that antibodies to some antigenic sites on the neuraminidase may inhibit virus release more efficiently than others, depending on their relation to the enzyme active center. None of the monoclonal antibodies inhibited the hemolytic activity of viruses possessing N2. Based on antigenic mapping and biological properties of the monoclonal antibodies, a topographical map of the neuraminidase can be constructed. It is proposed that antigenic regions 1 and 4 are spacially separated and, based on their failure to inhibit biological activity, may be located on the bottom surface of the molecule; region 3 may be on the top surface of the molecule but at some distance from the catalytic center. Antigenic region 2 probably encompasses most of the top surface of the molecule; region 2d being closest to the enzyme center, with subregions 2a and 2b adjacent to it on the top surface. Chemical treatment of the neuraminidase with trinitrobenzenesulfonic acid (TNBS) causes modification of the 2b region, confirming the antigenic mapping results.</div>
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