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A new SV40 mutant that encodes a small fragment of T antigen transforms established rat and mouse cells

L Sompayrac1, K J Danna

  • 1Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder 80309.

Virology
|April 1, 1988
PubMed

Insights

A new Simian virus 40 (SV40) mutant, T147, produces a truncated large T antigen. Despite reduced viral origin binding, this mutant efficiently transforms cells, indicating its oncogenic potential.

Area of Science:

  • Molecular Biology
  • Virology
  • Cancer Research

Background:

  • Simian virus 40 (SV40) large T antigen is a key viral oncoprotein.
  • Understanding the structure-function relationship of large T antigen is crucial for cancer research.

Purpose of the Study:

  • To investigate the properties and transforming activity of a novel, truncated SV40 large T antigen (T147).
  • To assess the impact of a 147-amino acid truncation on T antigen stability, DNA binding, and cellular transformation.

Main Methods:

  • Construction and characterization of the SV40 T147 mutant.
  • Biochemical analysis of T147 T antigen stability and phosphoprotein status.
  • Assessment of SV40 viral origin binding activity.
  • Cellular transformation assays using rat F111 and mouse C3H10T1/2 cells.

Main Results:

  • The T147 T antigen is a stable phosphoprotein, comparable to wild-type.
  • SV40 viral origin binding activity of T147 T antigen is reduced over 100-fold.
  • Cloned T147 DNA efficiently transforms rat F111 cells to anchorage independence.
  • Cloned T147 DNA also efficiently transforms mouse C3H10T1/2 cells in a focus assay.

Conclusions:

  • Truncated SV40 T147 T antigen retains significant cellular transforming capabilities despite impaired DNA binding.
  • The study highlights that regions outside the DNA-binding domain may be critical for SV40-mediated transformation.
  • T147 represents a valuable tool for dissecting the oncogenic mechanisms of SV40 T antigen.

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