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Journal of Virology, February 2005, p. 1924-1929, Vol. 79, No. 3
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.3.1924-1929.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Productive Interaction between Transmembrane Mutants of the Bovine Papillomavirus E5 Protein and the Platelet-Derived Growth Factor ß Receptor

Char-Chang Lai, Anne P. B. Edwards, and Daniel DiMaio^*

Department of Genetics, Yale University School of Medicine, New Haven, Connecticut 06510

Received 4 August 2004/ Accepted 24 September 2004

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) ß 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 ß 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 ß receptor, resulting in cellular signaling and transformation.

Present address: Department of Medical Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.

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