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J Virol. 1980 February; 33(2): 887-901

Antigenic and Immunogenic Characteristics of Nuclear and Membrane-Associated Simian Virus 40 Tumor Antigen

Department of Virology and Epidemiology, Baylor College of Medicine, Houston, Texas 77030

ABSTRACT

Antisera were prepared in syngeneic hosts against subcellular fractions of simian virus 40 (SV40)-transformed cells (MoPM, MoNuc), glutaraldehydefixed SV40-transformed cells (HaH-50-G, MoVLM-G), and electrophoretically purified denatured SV40 tumor antigen (T-ag) (RaT). Immune sera were also collected from animals bearing tumors induced by SV40-transformed cells (HaT, MoT, HAF) and from SV40-immunized animals that had rejected a transplant of SV40-transformed cells (HaS, MoS). Immunological reagents prepared against cell surface (MoPM, HaS, MoS, HaH-50-G, MoVLM-G) reacted exclusively with the surface of SV40-transformed cells by indirect immunofluorescence or protein A surface antigen radioimmunoassay. Immunological reagents prepared against the nuclear fraction (MoNuc) or whole-cell determinants (HaT, MoT, HAF, RaT) reacted with both the nuclei and surface of SV40-transformed or -infected cells. All reagents were capable of immunoprecipitating 96,000-molecular weight large T-ag from solubilized whole cell extracts of SV40-transformed cells. The exclusive surface reactivity of HaS exhibited in immunofluorescence tests was abolished by solubilization of subcellular fractions, which then allowed immunoprecipitation of T-ag by HaS from both nuclear and plasma membrane preparations. Specificity was established by the fact that all T-reactive reagents failed to react in serological tests against chemically transformed mouse cells, and sera from mice bearing transplants chemically transformed mouse cells (MoDMBA-2) failed to react with SV40-transformed mouse or hamster cells. Reagents demonstrating positive surface immunofluorescence and protein A radioimmunoassay reactions against SV40-transformed cells were capable of blocking the surface binding of RaT to SV40-transformed cells in a double-antibody surface antigen radioimmunoassay. This blocking ability demonstrated directly that a component specificity of each surface-reactive reagent is directed against SV40 T-ag. A model is presented which postulates that the differential detection of T-ag by the various serological reagents is a reflection of immunogenic and antigenic differences between T-ag polypeptides localized in nuclei and plasma membranes.

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