Document Detail


Antigenic and immunogenic characteristics of nuclear and membrane-associated simian virus 40 tumor antigen.
MedLine Citation:
PMID:  6157837     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Antisera were prepared in syngeneic hosts against subcellular fractions of simian virus 40 (SV40)-transformed cells (MoalphaPM, MoalphaNuc), glutaraldehydefixed SV40-transformed cells (HaalphaH-50-G, MoalphaVLM-G), and electrophoretically purified denatured SV40 tumor antigen (T-ag) (RaalphaT). Immune sera were also collected from animals bearing tumors induced by SV40-transformed cells (HaalphaT, MoalphaT, HAF) and from SV40-immunized animals that had rejected a transplant of SV40-transformed cells (HaalphaS, MoalphaS). Immunological reagents prepared against cell surface (MoalphaPM, HaalphaS, MoalphaS, HaalphaH-50-G, MoalphaVLM-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 (MoalphaNuc) or whole-cell determinants (HaalphaT, MoalphaT, HAF, RaalphaT) 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 HaalphaS exhibited in immunofluorescence tests was abolished by solubilization of subcellular fractions, which then allowed immunoprecipitation of T-ag by HaalphaS 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 (MoalphaDMBA-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 RaalphaT 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.
Authors:
H R Soule; R E Lanford; J S Butel
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of virology     Volume:  33     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  1980 Feb 
Date Detail:
Created Date:  1980-11-20     Completed Date:  1980-11-20     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  887-901     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Antigens, Neoplasm / immunology*
Antigens, Surface / immunology
Antigens, Viral / immunology*
Antigens, Viral, Tumor
Cell Fractionation
Cell Membrane / immunology
Cell Nucleus / immunology
Cell Transformation, Viral
Cricetinae
Epitopes / immunology
Fluorescent Antibody Technique
Mesocricetus
Mice
Mice, Inbred BALB C
Precipitin Tests
Radioimmunoassay
Simian virus 40 / immunology*
Grant Support
ID/Acronym/Agency:
CA 22555/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Antigens, Neoplasm; 0/Antigens, Surface; 0/Antigens, Viral; 0/Antigens, Viral, Tumor; 0/Epitopes
Comments/Corrections

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