Quantitative relationships between an influenza virus and neutralizing antibody
Identifieur interne : 002295 ( Main/Exploration ); précédent : 002294; suivant : 002296Quantitative relationships between an influenza virus and neutralizing antibody
Auteurs : H. P. Taylor [Royaume-Uni] ; S. J. Armstrong [Royaume-Uni] ; N. J. Dimmock [Royaume-Uni]Source :
- Virology [ 0042-6822 ] ; 1987.
English descriptors
- Teeft :
- Academic press, Aggregation, Animal viruses, Antibody, Antibody molecule, Antibody molecules, Antigenic, Antigenic sites, Aqueous suspension, Assay, Average diameter, Biological activities, Cause neutralization, Cell surface, Chicken erythrocytes, Different rabbits, Dimmock, Electron microscopy, Extinction coefficient, Haemagglutinin, Haemagglutinin spike, Hclo, Hyperimmune sera, Immunoglobulin, Inactivation, Inactivation kinetics, Infectious virus, Infectivity, Influenza, Influenza virus, Influenza virus neutralization, Influenza virus particle, Influenza viruses, Intact virus, Integral membrane protein, Interspike distance, Kinetic data, Kinetic studies, Kinetics, Latex beads, Linear regression analysis, Linear sucrose gradient, Maximum number, Minimum number, Molecular weight, Molecule, Molecules binding, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Monoclonal iggs, Neutralization, Neutralization kinetics, Neutralizing, Neutralizing antibody, Nonspecific binding, Plaque assay, Polyclonal, Polyclonal antisera, Radiochemical data, Radiolabelled immunoglobulins, Reassortant influenza virus, Residual infectivity, Room temperature, Same manner, Sample calculation, Saturating conditions, Specific activities, Specific activity, Spike, Standard deviation, Surface projections, Unpublished data, Various dilutions, Viral, Viral core, Virology, Virus, Virus particle, Virus particles, Virus surface.
Abstract
Abstract: In this quantitative study of the interaction of influenza virus with neutralizing antibody we have determined the maximum number of antibody molecules which can bind to the haemagglutinin (HA) of native influenza A/FPV/Rostock/34 (H7N1) particles in aqueous suspension and the minimum number which is required to cause neutralization. Using radiolabelled immunoglobulins approximately one IgG molecule, whether of monoclonal or polyclonal origin, binds per HA spike under conditions of antibody saturation. In the same manner, we have determined that when infectivity is neutralized by 63% ( 1 e) about 70 molecules of monoclonal IgGs HC2 and HC10 were bound per virus particle and this is supported by independent evidence from electron microscopy. However, the kinetics of neutralization were single-hit or at most, under critical conditions of low temperature (4°) and minimal neutralizing concentrations of antibody, two-hit. This apparent conflict is reconciled by a hypothesis which proposes that neutralization occurs only when antibody binds to certain “neutralization relevant” HA spikes which are in the minority. It is suggested that these only differ from the majority of “neutralization irrelevant” HA spikes by their transmembrane interaction with the core of the virion.
Url:
DOI: 10.1016/0042-6822(87)90466-1
Affiliations:
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Dimmock</name><affiliation wicri:level="1"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL West Midlands</wicri:regionArea><wicri:noRegion>CV4 7AL West Midlands</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="1987">1987</date><biblScope unit="volume">159</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="288">288</biblScope><biblScope unit="page" to="298">298</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>Aggregation</term><term>Animal viruses</term><term>Antibody</term><term>Antibody molecule</term><term>Antibody molecules</term><term>Antigenic</term><term>Antigenic sites</term><term>Aqueous suspension</term><term>Assay</term><term>Average diameter</term><term>Biological activities</term><term>Cause neutralization</term><term>Cell surface</term><term>Chicken erythrocytes</term><term>Different rabbits</term><term>Dimmock</term><term>Electron microscopy</term><term>Extinction coefficient</term><term>Haemagglutinin</term><term>Haemagglutinin spike</term><term>Hclo</term><term>Hyperimmune sera</term><term>Immunoglobulin</term><term>Inactivation</term><term>Inactivation kinetics</term><term>Infectious virus</term><term>Infectivity</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus neutralization</term><term>Influenza virus particle</term><term>Influenza viruses</term><term>Intact virus</term><term>Integral membrane protein</term><term>Interspike distance</term><term>Kinetic data</term><term>Kinetic studies</term><term>Kinetics</term><term>Latex beads</term><term>Linear regression analysis</term><term>Linear sucrose gradient</term><term>Maximum number</term><term>Minimum number</term><term>Molecular weight</term><term>Molecule</term><term>Molecules binding</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Monoclonal antibody</term><term>Monoclonal iggs</term><term>Neutralization</term><term>Neutralization kinetics</term><term>Neutralizing</term><term>Neutralizing antibody</term><term>Nonspecific binding</term><term>Plaque assay</term><term>Polyclonal</term><term>Polyclonal antisera</term><term>Radiochemical data</term><term>Radiolabelled immunoglobulins</term><term>Reassortant influenza virus</term><term>Residual infectivity</term><term>Room temperature</term><term>Same manner</term><term>Sample calculation</term><term>Saturating conditions</term><term>Specific activities</term><term>Specific activity</term><term>Spike</term><term>Standard deviation</term><term>Surface projections</term><term>Unpublished data</term><term>Various dilutions</term><term>Viral</term><term>Viral core</term><term>Virology</term><term>Virus</term><term>Virus particle</term><term>Virus particles</term><term>Virus surface</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: In this quantitative study of the interaction of influenza virus with neutralizing antibody we have determined the maximum number of antibody molecules which can bind to the haemagglutinin (HA) of native influenza A/FPV/Rostock/34 (H7N1) particles in aqueous suspension and the minimum number which is required to cause neutralization. Using radiolabelled immunoglobulins approximately one IgG molecule, whether of monoclonal or polyclonal origin, binds per HA spike under conditions of antibody saturation. In the same manner, we have determined that when infectivity is neutralized by 63% ( 1 e) about 70 molecules of monoclonal IgGs HC2 and HC10 were bound per virus particle and this is supported by independent evidence from electron microscopy. However, the kinetics of neutralization were single-hit or at most, under critical conditions of low temperature (4°) and minimal neutralizing concentrations of antibody, two-hit. This apparent conflict is reconciled by a hypothesis which proposes that neutralization occurs only when antibody binds to certain “neutralization relevant” HA spikes which are in the minority. It is suggested that these only differ from the majority of “neutralization irrelevant” HA spikes by their transmembrane interaction with the core of the virion.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><country name="Royaume-Uni"><noRegion><name sortKey="Taylor, H P" sort="Taylor, H P" uniqKey="Taylor H" first="H. P." last="Taylor">H. P. Taylor</name></noRegion><name sortKey="Armstrong, S J" sort="Armstrong, S J" uniqKey="Armstrong S" first="S. J." last="Armstrong">S. J. Armstrong</name><name sortKey="Dimmock, N J" sort="Dimmock, N J" uniqKey="Dimmock N" first="N. J." last="Dimmock">N. J. Dimmock</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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