Epitope mapping of monoclonal antibodies raised to recombinant Mengo 3D polymerase
Identifieur interne : 001134 ( Istex/Curation ); précédent : 001133; suivant : 001135Epitope mapping of monoclonal antibodies raised to recombinant Mengo 3D polymerase
Auteurs : Hernando Duque [États-Unis] ; Ann C. Palmenberg [États-Unis]Source :
- Virus Genes [ 0920-8569 ] ; 1996-01-01.
English descriptors
- KwdEn :
- Teeft :
- Antibody, Antibody binding, Antibody samples, Ascitic fluid, Cell extracts, Convalescent animals, Different epitopes, Duqueand palmenberg, Elisa, Epitope, Epitope mapping, Fmdv, Horseradish peroxidase, Inclusion bodies, Mabs, Mengo, Molecular mass, Monoclonal, Monoclonal antibodies, Native protein, Natural mengo, Other antibodies, Other hand, Other picornaviruses, Other viruses, Palmenberg, Picornavirus, Polymerase, Recombinant, Recombinant mengo, Rm3d, Rm3d mabs, Rm3d protein, Sodium deoxycholate, Strong reactivity, Urea, Vaccinated animals, Vaccine, Viral, Weak reactivity, Western analysis, Western blots.
Abstract
Abstract: The cDNA coding sequence of the RNA-dependent RNA polymerase (3Dpol) of Mengovirus was cloned and expressed in a bacterial system. Eleven monoclonal antibodies were raised against the recombinant Mengo 3Dpol (rM3D). All of them recognized the recombinant and the viral-induced form of the protein. The panel of monoclonals belonged to the IgG1 and IgG2a isotypes and were mapped to four different epitopes in the 3D molecule by competition assays. All monoclonals recognized Mengo 3Dpol in western blots and cross-reacted with the homologous polymerases of seven other cardioviruses but failed to react with 3Dpol from poliovirus type 1 and 3 or rhinovirus type 14 and 16.
Url:
DOI: 10.1007/BF00568908
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Palmenberg</name><affiliation wicri:level="1"><mods:affiliation>Institute for Molecular Virology, University of Wisconsin-Madison, 1655 Linden Drive, 53706, Madison, Wisconsin, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Institute for Molecular Virology, University of Wisconsin-Madison, 1655 Linden Drive, 53706, Madison, Wisconsin</wicri:regionArea></affiliation><affiliation wicri:level="1"><mods:affiliation>Department of Animal Health & Biomedical Sciences, University of Wisconsin-Madison, 1655 Linden Drive, 53706, Madison, Wisconsin, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Animal Health & Biomedical Sciences, University of Wisconsin-Madison, 1655 Linden Drive, 53706, Madison, Wisconsin</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Virus Genes</title><title level="j" type="abbrev">Virus Genes</title><idno type="ISSN">0920-8569</idno><idno type="eISSN">1572-994X</idno><imprint><publisher>Kluwer Academic Publishers</publisher><pubPlace>Dordrecht</pubPlace><date type="published" when="1996-01-01">1996-01-01</date><biblScope unit="volume">13</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="159">159</biblScope><biblScope unit="page" to="168">168</biblScope></imprint><idno type="ISSN">0920-8569</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0920-8569</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>3D polymerase</term><term>Mengo virus</term><term>mapping</term><term>monoclonal antibody</term><term>picornavirus</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Antibody</term><term>Antibody binding</term><term>Antibody samples</term><term>Ascitic fluid</term><term>Cell extracts</term><term>Convalescent animals</term><term>Different epitopes</term><term>Duqueand palmenberg</term><term>Elisa</term><term>Epitope</term><term>Epitope mapping</term><term>Fmdv</term><term>Horseradish peroxidase</term><term>Inclusion bodies</term><term>Mabs</term><term>Mengo</term><term>Molecular mass</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Native protein</term><term>Natural mengo</term><term>Other antibodies</term><term>Other hand</term><term>Other picornaviruses</term><term>Other viruses</term><term>Palmenberg</term><term>Picornavirus</term><term>Polymerase</term><term>Recombinant</term><term>Recombinant mengo</term><term>Rm3d</term><term>Rm3d mabs</term><term>Rm3d protein</term><term>Sodium deoxycholate</term><term>Strong reactivity</term><term>Urea</term><term>Vaccinated animals</term><term>Vaccine</term><term>Viral</term><term>Weak reactivity</term><term>Western analysis</term><term>Western blots</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The cDNA coding sequence of the RNA-dependent RNA polymerase (3Dpol) of Mengovirus was cloned and expressed in a bacterial system. Eleven monoclonal antibodies were raised against the recombinant Mengo 3Dpol (rM3D). All of them recognized the recombinant and the viral-induced form of the protein. The panel of monoclonals belonged to the IgG1 and IgG2a isotypes and were mapped to four different epitopes in the 3D molecule by competition assays. All monoclonals recognized Mengo 3Dpol in western blots and cross-reacted with the homologous polymerases of seven other cardioviruses but failed to react with 3Dpol from poliovirus type 1 and 3 or rhinovirus type 14 and 16.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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