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J Gen Virol 66 (1985), 827-837; DOI 10.1099/0022-1317-66-4-827
© 1985 Society for General Microbiology
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Isolation of Monoclonal Antibodies Specific for Rous Sarcoma Virus Structural, Polymerase and Transforming Proteins and Their Use for the Study of Mutant Virus-infected Cells

Reinhard Kurth, Terukazu Tanaka{dagger} and Karin Moelling1

Paul-Ehrlich-Institut, Paul-Ehrlich-Strasse 42-44, 6000 Frankfurt 70
and1 Max Planck-Institut für Molekulare Genetik, Ihnestrasse 63-73, 1000 Berlin 33, Federal Republic of Germany

Monoclonal antibodies were developed that are specific for Rous sarcoma virus structural, polymerase (reverse transcriptase) and transforming proteins. The monoclonal antibodies were shown to bind to purified virus proteins in an indirect 125I-labelled Protein A binding assay suitable for screening even very large numbers of hybridomas. Additional tests for specificity included radioimmunoprecipitation of purified virus structural proteins P12 and P27, of reverse transcriptase subunits {alpha} and beta, and of the transforming protein pp60v-src. Pilot immunofluorescence and protein kinase assays of the expression of virus proteins in avian and mammalian cells infected by wild-type virus as well as by temperature-sensitive, transformation-defective virus mutants revealed that synthesis of virus structural and transforming proteins is hardly affected by changes in temperature, whereas the pp60v-src-associated kinase activity is temperature-sensitive in cells infected by most, but not all the virus mutants.

Keywords: RSV, monoclonal antibodies, expression

{dagger} Present address: 1st Department of Internal Medicine, Kagawa Medical School, Kagawa, Japan.

Received 14 August 1984; accepted 17 December 1984.




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Copyright © 1985 by the Society for General Microbiology.