The antigenic structure of the influenza B virus hemagglutinin: Operational and topological mapping with monoclonal antibodies
Identifieur interne : 002424 ( Main/Exploration ); précédent : 002423; suivant : 002425The antigenic structure of the influenza B virus hemagglutinin: Operational and topological mapping with monoclonal antibodies
Auteurs : Michael T. Berton [États-Unis] ; Robert G. Webster [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1985.
English descriptors
- Teeft :
- Academic press, Acid substitutions, Amino, Amino acid substitutions, Antibody, Antigenic, Antigenic changes, Antigenic drift, Antigenic site, Antigenic sites, Antigenic structure, Antigenic variants, Antigenic variation, Antigenie, Ascites fluid, Assay, Berton, Competitive binding assay, Elisa, Embryonated chicken eggs, Epidemiological advantage, Epitope, Gerhard, Hemagglutinin, Infectivity, Infectivity reduction assays, Influenza, Influenza virus, Influenza virus hemagglutinin, Intact virus, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Neutralization titers, Nonoverlapping epitopes, Operational analysis, Parental virus, Polyclonal, Polyclonal antisera, Present study, Reactivity groups, Single antigenic site, Topological, Topological analysis, Variant, Virology, Virus, Virus hemagglutinin, Webster.
Abstract
Abstract: We have probed the antigenic structure of the influenza B virus hemagglutinin (HA) with monoclonal antibodies specific for the HA of influenza B virus, B/Oregon/5/80. Seventeen laboratory-selected antigenic variants of this virus were analyzed by hemagglutination-inhibition (HI) assays or ELISA and an operational antigenic map was constructed. In addition, the monoclonal antibodies were tested in a competitive binding assay to construct a topological map of the antigenic sites. In contrast to the influenza A virus HA, only a single immunodominant antigenic site composed of several overlapping clusters of epitopes was defined by the HI-positive antibodies. Three variants could be distinguished from the parental virus with polyclonal antisera by HI and infectivity reduction assays suggesting that changes in this antigenic site may be sufficient to provide an epidemiological advantage to influenza B viruses in nature. In addition, two nonoverlapping epitopes of unknown biological significance were identified in the competitive binding analysis by two monoclonal antibodies with no HI activity and little or no neutralizing activity. We previously identified single amino acid substitutions in the HAs of the antigenic variants used in this study (M. T. Berton, C. W. Naeve, and R. G. Webster 1984, J. Virol 52, 919–927). These changes occurred in regions of the molecule which, by amino acid sequence alignment, appeared to correspond to proposed antigenic sites A and B on the H3 HA of influenza A virus. Correlation with the antigenic map established in this report, however, demonstrates that the amino acid residues actually contribute to a single antigenic site on the influenza B virus HA and suggests significant differences in the antigenic structures of the influenza A and B virus HAs.
Url:
DOI: 10.1016/0042-6822(85)90396-4
Affiliations:
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Berton</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, University of Tennessee Center for the Health Sciences, 800 Madison Avenue, Memphis, Tennessee 38163</wicri:regionArea><wicri:noRegion>Tennessee 38163</wicri:noRegion></affiliation><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 North Lauderdale, P.O. Box 318, Memphis, Tennessee 38101</wicri:regionArea><wicri:noRegion>Tennessee 38101</wicri:noRegion></affiliation></author><author><name sortKey="Webster, Robert G" sort="Webster, Robert G" uniqKey="Webster R" first="Robert G." last="Webster">Robert G. 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Box 318, Memphis, Tennessee 38101</wicri:regionArea><wicri:noRegion>Tennessee 38101</wicri:noRegion></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="1985">1985</date><biblScope unit="volume">143</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="583">583</biblScope><biblScope unit="page" to="594">594</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>Academic press</term><term>Acid substitutions</term><term>Amino</term><term>Amino acid substitutions</term><term>Antibody</term><term>Antigenic</term><term>Antigenic changes</term><term>Antigenic drift</term><term>Antigenic site</term><term>Antigenic sites</term><term>Antigenic structure</term><term>Antigenic variants</term><term>Antigenic variation</term><term>Antigenie</term><term>Ascites fluid</term><term>Assay</term><term>Berton</term><term>Competitive binding assay</term><term>Elisa</term><term>Embryonated chicken eggs</term><term>Epidemiological advantage</term><term>Epitope</term><term>Gerhard</term><term>Hemagglutinin</term><term>Infectivity</term><term>Infectivity reduction assays</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus hemagglutinin</term><term>Intact virus</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Monoclonal antibody</term><term>Neutralization titers</term><term>Nonoverlapping epitopes</term><term>Operational analysis</term><term>Parental virus</term><term>Polyclonal</term><term>Polyclonal antisera</term><term>Present study</term><term>Reactivity groups</term><term>Single antigenic site</term><term>Topological</term><term>Topological analysis</term><term>Variant</term><term>Virology</term><term>Virus</term><term>Virus hemagglutinin</term><term>Webster</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: We have probed the antigenic structure of the influenza B virus hemagglutinin (HA) with monoclonal antibodies specific for the HA of influenza B virus, B/Oregon/5/80. Seventeen laboratory-selected antigenic variants of this virus were analyzed by hemagglutination-inhibition (HI) assays or ELISA and an operational antigenic map was constructed. In addition, the monoclonal antibodies were tested in a competitive binding assay to construct a topological map of the antigenic sites. In contrast to the influenza A virus HA, only a single immunodominant antigenic site composed of several overlapping clusters of epitopes was defined by the HI-positive antibodies. Three variants could be distinguished from the parental virus with polyclonal antisera by HI and infectivity reduction assays suggesting that changes in this antigenic site may be sufficient to provide an epidemiological advantage to influenza B viruses in nature. In addition, two nonoverlapping epitopes of unknown biological significance were identified in the competitive binding analysis by two monoclonal antibodies with no HI activity and little or no neutralizing activity. We previously identified single amino acid substitutions in the HAs of the antigenic variants used in this study (M. T. Berton, C. W. Naeve, and R. G. Webster 1984, J. Virol 52, 919–927). These changes occurred in regions of the molecule which, by amino acid sequence alignment, appeared to correspond to proposed antigenic sites A and B on the H3 HA of influenza A virus. Correlation with the antigenic map established in this report, however, demonstrates that the amino acid residues actually contribute to a single antigenic site on the influenza B virus HA and suggests significant differences in the antigenic structures of the influenza A and B virus HAs.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Berton, Michael T" sort="Berton, Michael T" uniqKey="Berton M" first="Michael T." last="Berton">Michael T. Berton</name></noRegion><name sortKey="Berton, Michael T" sort="Berton, Michael T" uniqKey="Berton M" first="Michael T." last="Berton">Michael T. Berton</name><name sortKey="Webster, Robert G" sort="Webster, Robert G" uniqKey="Webster R" first="Robert G." last="Webster">Robert G. Webster</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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