Abstract
The major rubella envelope protein, E1, and a segment of it, comprising amino acids 207-353, have been separately expressed as fusion proteins with the IgG binding region of Staphylococcus aureus protein A in Escherichia coli. The proteins carry E1-specific antigenicity recognized by monoclonal antibodies raised against whole virus confirming that correct glycosylation is not required for antigenicity. The use of these bioengineered antigens in immunoassays for diagnosis of rubella infection and for immunization in experimental animals is described.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Antibodies, Viral / analysis
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Antigens, Viral / biosynthesis*
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Antigens, Viral / genetics
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Antigens, Viral / immunology
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Antigens, Viral / isolation & purification
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Base Sequence
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Cloning, Molecular
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Enzyme-Linked Immunosorbent Assay
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Escherichia coli / genetics
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Hemagglutination Inhibition Tests
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Humans
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Immunization
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Immunoblotting
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Immunoglobulin M / analysis
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Molecular Sequence Data
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Neutralization Tests
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Plasmids
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Rabbits
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Recombinant Fusion Proteins / biosynthesis*
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / immunology
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Recombinant Fusion Proteins / isolation & purification
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Recombinant Proteins / biosynthesis*
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Rubella / genetics
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Rubella / immunology*
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Staphylococcal Protein A / genetics
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Transformation, Bacterial
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Viral Envelope Proteins / biosynthesis*
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Viral Envelope Proteins / genetics
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Viral Envelope Proteins / immunology
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Viral Envelope Proteins / isolation & purification
Substances
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Antibodies, Viral
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Antigens, Viral
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Immunoglobulin M
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Recombinant Fusion Proteins
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Recombinant Proteins
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Staphylococcal Protein A
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Viral Envelope Proteins
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E1 envelope protein, Rubella virus