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Complementation of a p300/CBP defective-binding mutant of adenovirus E1a by human papillomavirus E6 proteins

Agnieszka Bernat1, Paola Massimi1, Lawrence Banks1

  • 1International Centre for Genetic Engineering and Biotechnology, Padriciano 99, I-34012 Trieste, Italy1.

Insights

Human papillomavirus (HPV) E6 proteins from both high-risk and low-risk types bind to the p300 co-activator. This interaction is crucial for HPV E6

Area of Science:

  • Oncology
  • Virology
  • Molecular Biology

Background:

  • The human papillomavirus (HPV) type 16 E6 protein interacts with p300/CBP, inhibiting its transcriptional co-activator function.
  • Limited data exists on the biological impact of this interaction and whether it is specific to high-risk HPV E6 proteins.

Purpose of the Study:

  • To investigate the interaction of HPV-18 and HPV-11 E6 proteins with p300.
  • To determine the role of the E6-p300 interaction in HPV-mediated cell transformation.

Main Methods:

  • Comparative analysis of E6 protein interactions with p300 across different HPV types (HPV-16, HPV-18, HPV-11).
  • Cell transformation assays using a transformation-deficient adenovirus E1a mutant complemented by various HPV E6 proteins and mutants.
  • Assessment of HPV-16 E6 mutant lacking p300 binding capability in complementing the E1a mutant.

Main Results:

  • Both high-risk (HPV-16, HPV-18) and low-risk (HPV-11) E6 proteins bind to p300.
  • HPV-16, HPV-18, and HPV-11 E6 proteins could complement the transformation-deficient adenovirus E1a mutant.
  • An HPV-16 E6 mutant that does not bind p300 failed to rescue the E1a mutant's transformation deficiency.

Conclusions:

  • The E6-p300 interaction is not exclusive to high-risk HPV types.
  • The interaction between HPV E6 proteins and p300 plays a significant role in facilitating cell transformation by HPV E6.

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