Alterations in the hemagglutinin associated with adaptation of influenza B virus to growth in eggs
Identifieur interne : 002457 ( Main/Exploration ); précédent : 002456; suivant : 002458Alterations in the hemagglutinin associated with adaptation of influenza B virus to growth in eggs
Auteurs : James S. Robertson [Royaume-Uni] ; Clayton W. Naeve [États-Unis] ; Robert G. Webster [États-Unis] ; Janet S. Bootman [Royaume-Uni] ; Robert Newman [Royaume-Uni] ; Geoffrey C. Schild [Royaume-Uni]Source :
- Virology [ 0042-6822 ] ; 1985.
English descriptors
- Teeft :
- Academic press, Adjacent receptor binding site, Allantoic, Allantoic cavity, Allantois cells, Amino, Amino acid residues, Amino acid substitutions, Amino acids, Antigenic, Antigenic characterization, Antigenic drift, Antigenic site, Antigenic sites, Buffer system, Carbohydrate, Carbohydrate side chain, Clinical specimens, Coding regions, Confluent monolayers, Corresponding viruses, Dideoxy technique, Different isolation, Eggadapted, Eggadapted virus, Eggadapted viruses, Embryonated eggs, Fertile hens, Glycosylated, Glycosylation, Glycosylation site, Haemagglutinin, Hemagglutinin, Higher titers, Host cell selection, Human influenza virus, Important implications, Influenza, Influenza virus, Initial passage, Mammalian cell culture, Mammalian cells, Mdck, Mdck cells, Mdck line, Mdck plaque, Mdckderived virus, Molecular changes, Monoclonal, Monoclonal antibodies, Monoclonal antibody, National institute, Neutralization tests, Nucleotide sequences, Oligosaccharide structure, Passage histories, Polyacrylamide, Polyclonal sera, Potential glycosylation sequence, Potential glycosylation site, Potential glycosylation sites, Radioimmune assays, Receptor, Receptor binding site, Receptor specificity, Room temperature, Same source, Schild, Silver staining, Single nucleotide difference, Specific glycosylation site, Substitution, Total virion, Vaccine production, Virus, Virus particles.
Abstract
Abstract: In 1943 Burnet reported on changes in the hemagglutinating properties of human influenza virus which occurred during adaptation of the virus to growth in chicken eggs. Only recently has direct evidence been presented that these changes affect the antigenic properties of the virus. Schild et al. (G. C. Schild, J. S. Oxford, J. C. deJong, and R. G. Webster (1983), Nature (London)303, 706–709) demonstrated that egg adaptation of influenza B virus selects variants which are antigenically distinct from virus grown from the same source in mammalian cells. The molecular changes in the hemagglutinin (HA) of influenza B virus associated with adaptation to growth in eggs have now been identified. A specific glycosylation site at the distal tip of the HA of influenza B virus grown exclusively in mammalian cell culture is lost or altered during egg adaptation. Since the HA functions in adsorption of virus to cells, it is concluded that removal or modification of an oligosaccharide structure at this position is required for influenza B virus to attach to and infect the allantois cells of the egg and that this has important implications for the antigenic configuration of the molecule.
Url:
DOI: 10.1016/0042-6822(85)90105-9
Affiliations:
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Le document en format XML
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<term>Allantoic cavity</term>
<term>Allantois cells</term>
<term>Amino</term>
<term>Amino acid residues</term>
<term>Amino acid substitutions</term>
<term>Amino acids</term>
<term>Antigenic</term>
<term>Antigenic characterization</term>
<term>Antigenic drift</term>
<term>Antigenic site</term>
<term>Antigenic sites</term>
<term>Buffer system</term>
<term>Carbohydrate</term>
<term>Carbohydrate side chain</term>
<term>Clinical specimens</term>
<term>Coding regions</term>
<term>Confluent monolayers</term>
<term>Corresponding viruses</term>
<term>Dideoxy technique</term>
<term>Different isolation</term>
<term>Eggadapted</term>
<term>Eggadapted virus</term>
<term>Eggadapted viruses</term>
<term>Embryonated eggs</term>
<term>Fertile hens</term>
<term>Glycosylated</term>
<term>Glycosylation</term>
<term>Glycosylation site</term>
<term>Haemagglutinin</term>
<term>Hemagglutinin</term>
<term>Higher titers</term>
<term>Host cell selection</term>
<term>Human influenza virus</term>
<term>Important implications</term>
<term>Influenza</term>
<term>Influenza virus</term>
<term>Initial passage</term>
<term>Mammalian cell culture</term>
<term>Mammalian cells</term>
<term>Mdck</term>
<term>Mdck cells</term>
<term>Mdck line</term>
<term>Mdck plaque</term>
<term>Mdckderived virus</term>
<term>Molecular changes</term>
<term>Monoclonal</term>
<term>Monoclonal antibodies</term>
<term>Monoclonal antibody</term>
<term>National institute</term>
<term>Neutralization tests</term>
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<term>Oligosaccharide structure</term>
<term>Passage histories</term>
<term>Polyacrylamide</term>
<term>Polyclonal sera</term>
<term>Potential glycosylation sequence</term>
<term>Potential glycosylation site</term>
<term>Potential glycosylation sites</term>
<term>Radioimmune assays</term>
<term>Receptor</term>
<term>Receptor binding site</term>
<term>Receptor specificity</term>
<term>Room temperature</term>
<term>Same source</term>
<term>Schild</term>
<term>Silver staining</term>
<term>Single nucleotide difference</term>
<term>Specific glycosylation site</term>
<term>Substitution</term>
<term>Total virion</term>
<term>Vaccine production</term>
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<front><div type="abstract" xml:lang="en">Abstract: In 1943 Burnet reported on changes in the hemagglutinating properties of human influenza virus which occurred during adaptation of the virus to growth in chicken eggs. Only recently has direct evidence been presented that these changes affect the antigenic properties of the virus. Schild et al. (G. C. Schild, J. S. Oxford, J. C. deJong, and R. G. Webster (1983), Nature (London)303, 706–709) demonstrated that egg adaptation of influenza B virus selects variants which are antigenically distinct from virus grown from the same source in mammalian cells. The molecular changes in the hemagglutinin (HA) of influenza B virus associated with adaptation to growth in eggs have now been identified. A specific glycosylation site at the distal tip of the HA of influenza B virus grown exclusively in mammalian cell culture is lost or altered during egg adaptation. Since the HA functions in adsorption of virus to cells, it is concluded that removal or modification of an oligosaccharide structure at this position is required for influenza B virus to attach to and infect the allantois cells of the egg and that this has important implications for the antigenic configuration of the molecule.</div>
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