Time-dependent maturation of the simian virus 40 large T antigen-p53 complex studied by using monoclonal antibodies

J Virol. 1982 Nov;44(2):565-73. doi: 10.1128/JVI.44.2.565-573.1982.

Abstract

Newly synthesized simian virus 40 large tumor antigen (T Ag) slowly forms a stable complex with the host tumor antigen, "p53." By the use of immunological and temporal separations and inhibition of aggregation and processing by A locus mutation, we have distinguished specific steps in the reaction sequence leading to formation of the rapidly sedimenting oligomeric complex. The monoclonal antibody PAb101 bound only a fraction of the total soluble pulse-labeled T Ag bound by antitumor serum. After a chase, all T Ag had matured to the form recognized by PAb101. All p53 in the mouse line SVA31E7 was precipitated by the T Ag-specific monoclonal antibody PAb101, even after a short pulse, and is therefore entirely bound to mature T Ag. The p53-specific monoclonal antibody PAb122 precipitates nearly all of the mature T Ag recognized by PAb101, except A locus mutant T Ag, synthesized at the nonpermissive temperature. A locus mutation inhibited entry of newly synthesized T Ag into the oligomeric greater than 28S complex of T Ag and p53.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antibodies, Monoclonal
  • Antigens, Neoplasm* / immunology
  • Antigens, Viral* / immunology
  • Antigens, Viral, Tumor
  • Cell Line
  • Cell Transformation, Neoplastic
  • Cell Transformation, Viral
  • Centrifugation, Density Gradient
  • Kinetics
  • Mice
  • Mutation
  • Simian virus 40 / genetics
  • Simian virus 40 / immunology*

Substances

  • Antibodies, Monoclonal
  • Antigens, Neoplasm
  • Antigens, Viral
  • Antigens, Viral, Tumor