Antigenic reactivity and electrophoretic migrational heterogeneity of the three polymerase proteins of type A human and animal influenza viruses
Identifieur interne : 002124 ( Main/Exploration ); précédent : 002123; suivant : 002125Antigenic reactivity and electrophoretic migrational heterogeneity of the three polymerase proteins of type A human and animal influenza viruses
Auteurs : R. K. Akkina [États-Unis]Source :
- Archives of Virology [ 0304-8608 ] ; 1990-09-01.
English descriptors
- Teeft :
- Additional forms, Akkina, Antigenic, Antigenic reactivity, Antiserum, Cell lysate, Cell lysates, Colorado state university, Considerable heterogeneity, Different subtype influenza viruses, Different viruses, Electrophoretic, Electrophoretic migrational heterogeneity, Heterogeneity, Human influenza, Human influenza virus, Immunoprecipitated, Immunoprecipitates, Immunoprecipitation, Influenza, Influenza virus, Influenza viruses, Internal proteins, Lysate, Lysates, Lysis buffer, Monospecific, Monospecific antisera, Nucleic acids, Nucleotide sequence, Nucleotide sequences, Palese, Polymerase, Polymerase antisera, Polymerase protein, Polymerase proteins, Polypeptide, Protein, Replication, Sequence analysis, Subtypes, Unimmunoprecipitated virus, Viral, Viral proteins, Viral subtypes, Virus, Virus polymerase proteins.
Abstract
Summary: Antigenic reactivity of the three polymerase proteins PB1, PB2, and PA of type A influenza viruses of animal and human origin were analysed by radioimmunoprecipitation using monospecific antisera. Each of the polymerase monospecific antisera made against the polymerase proteins of the human A/WSN/33 (H1N1) influenza virus reacted efficiently with the homologous proteins of all the known thirteen HA subtype viruses of avian influenza virus, three subtypes of human influenza virus, swine and equine influenza viruses. This broad reactivity of each of the antisera indicated that the polymerase proteins are antigenically related among the type A influenza viruses and therefore can be considered as type specific antigens similar to the other viral internal proteins nucleoprotein (NP) and matrix protein (M). No electrophoretic migrational heterogeneity was found among the PB2 proteins of different subtype viruses, whereas PB1 protein exhibited minor variation. However, PA protein from among various viral subtypes showed considerable heterogeneity. Each of the polymerase antisera also immunoprecipitated additional antigenically related polypeptides with distinct electrophoretic mobilities from cells infected with each of the influenza viral subtypes.
Url:
DOI: 10.1007/BF01311053
Affiliations:
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K." last="Akkina">R. K. Akkina</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, Colorado</wicri:regionArea><placeName><region type="state">Colorado</region></placeName></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="1990-09-01">1990-09-01</date><biblScope unit="volume">111</biblScope><biblScope unit="issue">3-4</biblScope><biblScope unit="page" from="187">187</biblScope><biblScope unit="page" to="197">197</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>Additional forms</term><term>Akkina</term><term>Antigenic</term><term>Antigenic reactivity</term><term>Antiserum</term><term>Cell lysate</term><term>Cell lysates</term><term>Colorado state university</term><term>Considerable heterogeneity</term><term>Different subtype influenza viruses</term><term>Different viruses</term><term>Electrophoretic</term><term>Electrophoretic migrational heterogeneity</term><term>Heterogeneity</term><term>Human influenza</term><term>Human influenza virus</term><term>Immunoprecipitated</term><term>Immunoprecipitates</term><term>Immunoprecipitation</term><term>Influenza</term><term>Influenza virus</term><term>Influenza viruses</term><term>Internal proteins</term><term>Lysate</term><term>Lysates</term><term>Lysis buffer</term><term>Monospecific</term><term>Monospecific antisera</term><term>Nucleic acids</term><term>Nucleotide sequence</term><term>Nucleotide sequences</term><term>Palese</term><term>Polymerase</term><term>Polymerase antisera</term><term>Polymerase protein</term><term>Polymerase proteins</term><term>Polypeptide</term><term>Protein</term><term>Replication</term><term>Sequence analysis</term><term>Subtypes</term><term>Unimmunoprecipitated virus</term><term>Viral</term><term>Viral proteins</term><term>Viral subtypes</term><term>Virus</term><term>Virus polymerase proteins</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Summary: Antigenic reactivity of the three polymerase proteins PB1, PB2, and PA of type A influenza viruses of animal and human origin were analysed by radioimmunoprecipitation using monospecific antisera. Each of the polymerase monospecific antisera made against the polymerase proteins of the human A/WSN/33 (H1N1) influenza virus reacted efficiently with the homologous proteins of all the known thirteen HA subtype viruses of avian influenza virus, three subtypes of human influenza virus, swine and equine influenza viruses. This broad reactivity of each of the antisera indicated that the polymerase proteins are antigenically related among the type A influenza viruses and therefore can be considered as type specific antigens similar to the other viral internal proteins nucleoprotein (NP) and matrix protein (M). No electrophoretic migrational heterogeneity was found among the PB2 proteins of different subtype viruses, whereas PB1 protein exhibited minor variation. However, PA protein from among various viral subtypes showed considerable heterogeneity. Each of the polymerase antisera also immunoprecipitated additional antigenically related polypeptides with distinct electrophoretic mobilities from cells infected with each of the influenza viral subtypes.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Colorado</li></region></list><tree><country name="États-Unis"><region name="Colorado"><name sortKey="Akkina, R K" sort="Akkina, R K" uniqKey="Akkina R" first="R. K." last="Akkina">R. K. Akkina</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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