Three antibody molecules can bind simultaneously to each monomer of the tetramer of influenza virus neuraminidase and the trimer of influenza virus hemagglutinin
Identifieur interne : 001216 ( Istex/Curation ); précédent : 001215; suivant : 001217Three antibody molecules can bind simultaneously to each monomer of the tetramer of influenza virus neuraminidase and the trimer of influenza virus hemagglutinin
Auteurs : D. C. Jackson [Australie] ; B. S. Crabb [Australie] ; P. Poumbourios [Australie] ; W. R. Tulip ; W. G. Laver [Australie]Source :
- Archives of Virology [ 0304-8608 ] ; 1991-03-01.
English descriptors
- Teeft :
- Amino acid sequences, Antibody, Antibody binding, Antibody fragments, Antibody molecules, Antigenic, Antigenic determinants, Antigenic sites, Antigenic structure, Available surface area, Avian virus, Carbohydrate side chains, Clear evidence, Conformational changes, Constant amount, Dimensional structure, Elution profiles, Elution time, Epitope, Final concentration, Flow rate, Fplc system, Gradient length, Hemagglutinin, Immune, Immune complexes, Immunol, Individual fractions, Influenza, Influenza virus, Influenza virus hemagglutinin, Influenza virus neuraminidase, Influenza viruses, Large number, Laver, Linear sucrose gradients, Molecular mass, Molecular weight, Monoclonal, Monoclonal antibodies, Monovalent, Monovalent antibody, Monovalent antibody fragments, Neuraminidase, Normal rabbit, Pbsa, Permeation chromatography, Physical properties, Polyclonal antibody preparation, Present study, Protein surface, Relative mobilities, Room temperature, Saturating conditions, Sedimentation, Sedimentation coefficient, Sedimentation coefficients, Species stokes, Standard proteins, Steric constraints, Steric hindrance, Stokes, Sucrose, Surface area, Varghese, Velocity sedimentation experiments, Virology.
Abstract
Summary: Trimeric hemagglutinin and tetrameric neuraminidase molecules isolated from influenza virus bind an average of 9 and 13 molecules respectively of monovalent antibody fragments prepared from IgG isolated from polyclonal sera. In each case this represents an average of approximately three molecules of antibody binding to each protomer. Although there is compelling evidence for the presence of multiple adjacent and overlapping epitopes covering the surface of these two viral antigens, steric hindrance ensures that even under saturating conditions only three molecules of monovalent antibody fragments can be simultaneously accommodated on each monomer.
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DOI: 10.1007/BF01319230
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W. R. Tulip<affiliation><mods:affiliation>CSIRO Division of Biomolecular Engineering, Parkville, Victoria</mods:affiliation><wicri:noCountry code="subField">Victoria</wicri:noCountry></affiliation>Le document en format XML
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Tulip</name><affiliation><mods:affiliation>CSIRO Division of Biomolecular Engineering, Parkville, Victoria</mods:affiliation><wicri:noCountry code="subField">Victoria</wicri:noCountry></affiliation></author><author><name sortKey="Laver, W G" sort="Laver, W G" uniqKey="Laver W" first="W. G." last="Laver">W. G. 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C." last="Jackson">D. C. Jackson</name><affiliation wicri:level="4"><mods:affiliation>Department of Microbiology, University of Melbourne, Parkville</mods:affiliation><orgName type="university">Université de Melbourne</orgName><country>Australie</country><placeName><settlement type="city">Melbourne</settlement><region type="état">Victoria (État)</region></placeName></affiliation></author><author><name sortKey="Crabb, B S" sort="Crabb, B S" uniqKey="Crabb B" first="B. S." last="Crabb">B. S. Crabb</name><affiliation wicri:level="4"><mods:affiliation>Department of Microbiology, University of Melbourne, Parkville</mods:affiliation><orgName type="university">Université de Melbourne</orgName><country>Australie</country><placeName><settlement type="city">Melbourne</settlement><region type="état">Victoria (État)</region></placeName></affiliation></author><author><name sortKey="Poumbourios, P" sort="Poumbourios, P" uniqKey="Poumbourios P" first="P." last="Poumbourios">P. Poumbourios</name><affiliation wicri:level="4"><mods:affiliation>Department of Microbiology, University of Melbourne, Parkville</mods:affiliation><orgName type="university">Université de Melbourne</orgName><country>Australie</country><placeName><settlement type="city">Melbourne</settlement><region type="état">Victoria (État)</region></placeName></affiliation></author><author><name sortKey="Tulip, W R" sort="Tulip, W R" uniqKey="Tulip W" first="W. R." last="Tulip">W. R. Tulip</name><affiliation><mods:affiliation>CSIRO Division of Biomolecular Engineering, Parkville, Victoria</mods:affiliation><wicri:noCountry code="subField">Victoria</wicri:noCountry></affiliation></author><author><name sortKey="Laver, W G" sort="Laver, W G" uniqKey="Laver W" first="W. G." last="Laver">W. G. Laver</name><affiliation wicri:level="1"><mods:affiliation>John Curtin School of Medical Research, Australian National University, Canberra, ACT, Australia</mods:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>John Curtin School of Medical Research, Australian National University, Canberra, ACT</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Archives of Virology</title><title level="j" type="abbrev">Archives of Virology</title><idno type="ISSN">0304-8608</idno><idno type="eISSN">1432-8798</idno><imprint><publisher>Springer-Verlag</publisher><pubPlace>Vienna</pubPlace><date type="published" when="1991-03-01">1991-03-01</date><biblScope unit="volume">116</biblScope><biblScope unit="issue">1-4</biblScope><biblScope unit="page" from="45">45</biblScope><biblScope unit="page" to="56">56</biblScope></imprint><idno type="ISSN">0304-8608</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0304-8608</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Amino acid sequences</term><term>Antibody</term><term>Antibody binding</term><term>Antibody fragments</term><term>Antibody molecules</term><term>Antigenic</term><term>Antigenic determinants</term><term>Antigenic sites</term><term>Antigenic structure</term><term>Available surface area</term><term>Avian virus</term><term>Carbohydrate side chains</term><term>Clear evidence</term><term>Conformational changes</term><term>Constant amount</term><term>Dimensional structure</term><term>Elution profiles</term><term>Elution time</term><term>Epitope</term><term>Final concentration</term><term>Flow rate</term><term>Fplc system</term><term>Gradient length</term><term>Hemagglutinin</term><term>Immune</term><term>Immune complexes</term><term>Immunol</term><term>Individual fractions</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus hemagglutinin</term><term>Influenza virus neuraminidase</term><term>Influenza viruses</term><term>Large number</term><term>Laver</term><term>Linear sucrose gradients</term><term>Molecular mass</term><term>Molecular weight</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Monovalent</term><term>Monovalent antibody</term><term>Monovalent antibody fragments</term><term>Neuraminidase</term><term>Normal rabbit</term><term>Pbsa</term><term>Permeation chromatography</term><term>Physical properties</term><term>Polyclonal antibody preparation</term><term>Present study</term><term>Protein surface</term><term>Relative mobilities</term><term>Room temperature</term><term>Saturating conditions</term><term>Sedimentation</term><term>Sedimentation coefficient</term><term>Sedimentation coefficients</term><term>Species stokes</term><term>Standard proteins</term><term>Steric constraints</term><term>Steric hindrance</term><term>Stokes</term><term>Sucrose</term><term>Surface area</term><term>Varghese</term><term>Velocity sedimentation experiments</term><term>Virology</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Summary: Trimeric hemagglutinin and tetrameric neuraminidase molecules isolated from influenza virus bind an average of 9 and 13 molecules respectively of monovalent antibody fragments prepared from IgG isolated from polyclonal sera. In each case this represents an average of approximately three molecules of antibody binding to each protomer. Although there is compelling evidence for the presence of multiple adjacent and overlapping epitopes covering the surface of these two viral antigens, steric hindrance ensures that even under saturating conditions only three molecules of monovalent antibody fragments can be simultaneously accommodated on each monomer.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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