Isolation of cross-reactive, subtype-specific monoclonal antibodies against influenza virus HA1 and HA2 hemagglutinin subunits
Identifieur interne : 002322 ( Main/Exploration ); précédent : 002321; suivant : 002323Isolation of cross-reactive, subtype-specific monoclonal antibodies against influenza virus HA1 and HA2 hemagglutinin subunits
Auteurs : Alicia Sánchez-Fauquier [Espagne] ; Nieves Villanueva [Espagne] ; J. A. Melero [Espagne]Source :
- Archives of Virology [ 0304-8608 ] ; 1987-09-01.
English descriptors
- Teeft :
- Allantoic fluid, Antibody, Antigenic, Antigenic drift, Antiha2 antibodies, Assay, Cell membranes, Corresponding subunit, Denatured subunits, Different conformations, Different mabs, Different strenght, Different subtypes, Embryonated eggs, Epitope, Fluorescence staining, Hand margin, Hemagglutinin, Hemagglutinin subunits, High frequency, Immune complexes, Immunization, Immunize mice, Immunizing strain, Influenza, Influenza hemagglutinin, Influenza virus, Influenza virus hemagglutinin, Influenza viruses, Intact virus, Mabs, Mdck, Mdck cells, Molecular weight markers, Monoclonal, Monoclonal antibodies, Native molecule, Neutralization tests, Nitrocellulose paper, Polyclonal antisera, Positive cultures, Proc natl acad, Reference strains, Room temperature, Same subtype, Short peptides, Subunit, Supernatant, Uninfected cells, Virus, Virus panel.
Abstract
Summary: The large (HA1) and small (HA2) subunits of influenza virus A/Vict/3/75 hemagglutinin were purified in denatured form by preparative electrophoresis. Both polypeptides were used to immunize mice from which monoclonal antibodies were obtained. These antibodies reacted not only with the corresponding hemagglutinin subunit but also with purified virions. When tested by radioimmunoassay against a panel of human viruses, most anti-HA1 and -HA2 antibodies behaved as subtype-specific, whereas anti-HA antibodies, raised against purified virus, were more restricted. The anti-subunit antibodies were negative in hemagglutination-inhibition and neutralization tests. The interest of these antibodies as reagents for research and diagnosis is discussed.
Url:
DOI: 10.1007/BF01314425
Affiliations:
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Le document en format XML
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<term>Antiha2 antibodies</term>
<term>Assay</term>
<term>Cell membranes</term>
<term>Corresponding subunit</term>
<term>Denatured subunits</term>
<term>Different conformations</term>
<term>Different mabs</term>
<term>Different strenght</term>
<term>Different subtypes</term>
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<term>Fluorescence staining</term>
<term>Hand margin</term>
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<term>Hemagglutinin subunits</term>
<term>High frequency</term>
<term>Immune complexes</term>
<term>Immunization</term>
<term>Immunize mice</term>
<term>Immunizing strain</term>
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<term>Influenza hemagglutinin</term>
<term>Influenza virus</term>
<term>Influenza virus hemagglutinin</term>
<term>Influenza viruses</term>
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<term>Room temperature</term>
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<front><div type="abstract" xml:lang="en">Summary: The large (HA1) and small (HA2) subunits of influenza virus A/Vict/3/75 hemagglutinin were purified in denatured form by preparative electrophoresis. Both polypeptides were used to immunize mice from which monoclonal antibodies were obtained. These antibodies reacted not only with the corresponding hemagglutinin subunit but also with purified virions. When tested by radioimmunoassay against a panel of human viruses, most anti-HA1 and -HA2 antibodies behaved as subtype-specific, whereas anti-HA antibodies, raised against purified virus, were more restricted. The anti-subunit antibodies were negative in hemagglutination-inhibition and neutralization tests. The interest of these antibodies as reagents for research and diagnosis is discussed.</div>
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