Expression of influenza neuraminidase in baculovirus-infected cells
Identifieur interne : 001F53 ( Main/Exploration ); précédent : 001F52; suivant : 001F54Expression of influenza neuraminidase in baculovirus-infected cells
Auteurs : Karen A. Mather ; Jacinta F. White [Australie] ; Peter J. Hudson [Australie] ; Jennifer L. Mckimm-BreschkinSource :
- Virus Research [ 0168-1702 ] ; 1992.
English descriptors
- Teeft :
- Acnpv, Allantoic fluid, Arrow points, Arrows point, Baculovirus, Baculovirus system, Cell pellet, Cell surface, Culture medium, Different loadings, Electron microscopy, Enzyme activity, Extracellular, Extracellular medium, Extracellular virus, Foreign proteins, Gene product, Horseradish peroxidase, Influenza, Influenza neuraminidase, Influenza virus, Insect cells, Lysed cell pellets, Membrane capsule, Monoclonal, Monoclonal antibodies, Native influenza, Native influenza virus, Neuraminic acid, Neuraminidase, Neuraminidase gene, Parainfluenza type, Partial purification, Pellet, Phase contrast image, Polyclonal, Polyclonal antisera, Polyclonal sera, Recombinant, Recombinant acnpv, Recombinant baculovirus, Recombinant cells, Recombinant insect cells, Recombinant product, Recombinant protein, Recombinant proteins, Recombinant virus, Restriction enzyme analysis, Right panel, Room temperature, Same cells, Shuttle vector, Smaller form, Subtype, Supernatant, Supernatant form, Unfixed cells, Uranyl acetate, Viral pellet, Wyke coelingh.
Abstract
Abstract: Recombinant influenza neuraminidase (NA, subtype 2, A/NT/60/68) was produced by recombinant baculovirus-infected insect cells. The recombinant NA retained enzyme activity and was located on the cell surface. Enzyme activity was both cell-associated and in the cell free supernatant; maximal NA activity was found in the supernatant. Recombinant NA was recognised by polyclonal antisera and by three monoclonal antibodies specific for NA (subtype 2). Enzyme activity was also neutralised by polyclonal antisera. Recombinant NA thus retains most of the immunological and activity properties of authentic influenza NA. Immunoprecipitation of [35S]Methionine-labelled cells and supernatant and partial purification of NA indicated that a ~ 50-kDa form of NA was present in the supernatant, whilst the expected size (~ 67-kDa) was cell-associated. Purified recombinant extracellular virus was also enzymatically active, and contained the 67-kDa NA which was located on the membrane capsule of the virus. This suggests that the virus had acquired the cell-associated form of recombinant NA during the budding process from the cell.
Url:
DOI: 10.1016/0168-1702(92)90152-Y
Affiliations:
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Le document en format XML
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<sourceDesc><biblStruct><analytic><title level="a">Expression of influenza neuraminidase in baculovirus-infected cells</title>
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<author><name sortKey="Mckimm Breschkin, Jennifer L" sort="Mckimm Breschkin, Jennifer L" uniqKey="Mckimm Breschkin J" first="Jennifer L." last="Mckimm-Breschkin">Jennifer L. Mckimm-Breschkin</name>
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<term>Baculovirus system</term>
<term>Cell pellet</term>
<term>Cell surface</term>
<term>Culture medium</term>
<term>Different loadings</term>
<term>Electron microscopy</term>
<term>Enzyme activity</term>
<term>Extracellular</term>
<term>Extracellular medium</term>
<term>Extracellular virus</term>
<term>Foreign proteins</term>
<term>Gene product</term>
<term>Horseradish peroxidase</term>
<term>Influenza</term>
<term>Influenza neuraminidase</term>
<term>Influenza virus</term>
<term>Insect cells</term>
<term>Lysed cell pellets</term>
<term>Membrane capsule</term>
<term>Monoclonal</term>
<term>Monoclonal antibodies</term>
<term>Native influenza</term>
<term>Native influenza virus</term>
<term>Neuraminic acid</term>
<term>Neuraminidase</term>
<term>Neuraminidase gene</term>
<term>Parainfluenza type</term>
<term>Partial purification</term>
<term>Pellet</term>
<term>Phase contrast image</term>
<term>Polyclonal</term>
<term>Polyclonal antisera</term>
<term>Polyclonal sera</term>
<term>Recombinant</term>
<term>Recombinant acnpv</term>
<term>Recombinant baculovirus</term>
<term>Recombinant cells</term>
<term>Recombinant insect cells</term>
<term>Recombinant product</term>
<term>Recombinant protein</term>
<term>Recombinant proteins</term>
<term>Recombinant virus</term>
<term>Restriction enzyme analysis</term>
<term>Right panel</term>
<term>Room temperature</term>
<term>Same cells</term>
<term>Shuttle vector</term>
<term>Smaller form</term>
<term>Subtype</term>
<term>Supernatant</term>
<term>Supernatant form</term>
<term>Unfixed cells</term>
<term>Uranyl acetate</term>
<term>Viral pellet</term>
<term>Wyke coelingh</term>
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<front><div type="abstract" xml:lang="en">Abstract: Recombinant influenza neuraminidase (NA, subtype 2, A/NT/60/68) was produced by recombinant baculovirus-infected insect cells. The recombinant NA retained enzyme activity and was located on the cell surface. Enzyme activity was both cell-associated and in the cell free supernatant; maximal NA activity was found in the supernatant. Recombinant NA was recognised by polyclonal antisera and by three monoclonal antibodies specific for NA (subtype 2). Enzyme activity was also neutralised by polyclonal antisera. Recombinant NA thus retains most of the immunological and activity properties of authentic influenza NA. Immunoprecipitation of [35S]Methionine-labelled cells and supernatant and partial purification of NA indicated that a ~ 50-kDa form of NA was present in the supernatant, whilst the expected size (~ 67-kDa) was cell-associated. Purified recombinant extracellular virus was also enzymatically active, and contained the 67-kDa NA which was located on the membrane capsule of the virus. This suggests that the virus had acquired the cell-associated form of recombinant NA during the budding process from the cell.</div>
</front>
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<tree><noCountry><name sortKey="Mather, Karen A" sort="Mather, Karen A" uniqKey="Mather K" first="Karen A." last="Mather">Karen A. Mather</name>
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<name sortKey="Hudson, Peter J" sort="Hudson, Peter J" uniqKey="Hudson P" first="Peter J." last="Hudson">Peter J. Hudson</name>
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