Archives of Virology

, Volume 149, Issue 9, pp 1745–1759 | Cite as

Human papillomavirus type 16 E5 protein colocalizes with the antiapoptotic Bcl-2 protein

  • E. Auvinen
  • A. Alonso
  • P. Auvinen


Human papillomavirus type 16 E5 protein contributes to cellular transformation by increasing the mitogenic stimulus from growth factor receptors to the nucleus. In order to study the biological mechanisms of the E5 protein we performed site-directed mutagenesis of the E5 gene. Wild-type as well as mutant E5 proteins were transiently expressed in human cervical epithelial cells, and cell morphology, expression of proteins involved in cell adhesion, and localization of the different proteins were studied. Little differences in cell morphology or expression kinetics were observed between the different E5 proteins, except for relocalization of a mutant E5 protein where a hydrophobic leucine membrane anchor was mutated to positively charged amino acids. This mutant E5 protein localized to lamellipodia, which are motility-associated structures at the leading edge of motile cells. In our experimental conditions, 100% of E5-expressing epithelial cells died by four days of expression, possibly due to toxicity or disturbance of the membrane compartment by the E5 protein. Most interestingly, a remarkable colocalization of the E5 protein with the Bcl-2 antiapoptotic protein on intracellular membranes was established.


Leucine Cell Morphology Charge Amino Acid Antiapoptotic Protein Intracellular Membrane 
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Copyright information

© Springer-Verlag/Wien 2004

Authors and Affiliations

  • E. Auvinen
    • 1
  • A. Alonso
    • 2
  • P. Auvinen
    • 3
  1. 1.Department of VirologyHelsinki University Central Hospital, University of HelsinkiHelsinkiFinland
  2. 2.Applied Tumor Virology, German Cancer Research CenterHeidelbergGermany
  3. 3.Institute of Biotechnology, University of HelsinkiHelsinkiFinland

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