Productive interaction between transmembrane mutants of the bovine papillomavirus E5 protein and the platelet-derived growth factor beta receptor

J Virol. 2005 Feb;79(3):1924-9. doi: 10.1128/JVI.79.3.1924-1929.2005.

Abstract

The bovine papillomavirus E5 protein is a 44-amino-acid transmembrane protein that transforms cells by binding to the transmembrane region of the cellular platelet-derived growth factor (PDGF) beta receptor, resulting in sustained receptor signaling. However, there are published reports that certain mutants with amino acid substitutions in the membrane-spanning segment of the E5 protein transform cells without activating the PDGF beta receptor. We re-examined several of these transmembrane mutants, and here we present five lines of evidence that these mutants do in fact activate the PDGF beta receptor, resulting in cellular signaling and transformation.

Publication types

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

MeSH terms

  • Animals
  • Bovine papillomavirus 1 / metabolism
  • Cattle
  • Cell Line
  • Cell Line, Transformed
  • Cell Transformation, Viral*
  • Mice
  • Mutation, Missense*
  • NIH 3T3 Cells
  • Oncogene Proteins, Viral / genetics
  • Oncogene Proteins, Viral / metabolism*
  • Phosphorylation
  • Receptor, Platelet-Derived Growth Factor beta / metabolism*
  • Signal Transduction
  • Tyrosine / metabolism

Substances

  • Oncogene Proteins, Viral
  • oncogene protein E5, Bovine papillomavirus type 1
  • Tyrosine
  • Receptor, Platelet-Derived Growth Factor beta