Epitope mapping of monoclonal antibodies raised to recombinant Mengo 3D polymerase
Identifieur interne : 003F82 ( Main/Exploration ); précédent : 003F81; suivant : 003F83Epitope 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
Affiliations:
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Le document en format XML
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<term>Convalescent animals</term>
<term>Different epitopes</term>
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<term>Epitope mapping</term>
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<term>Sodium deoxycholate</term>
<term>Strong reactivity</term>
<term>Urea</term>
<term>Vaccinated animals</term>
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<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>
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