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Related Experiment Videos

The HPV16 E7 viral oncoprotein self-assembles into defined spherical oligomers.

Leonardo G Alonso1, Maria M García-Alai, Clara Smal

  • 1Instituto Leloir, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Patricias Argentinas 435, (1405) Buenos Aires, Argentina.

Biochemistry
|March 24, 2004
PubMed
Summary

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Human papillomavirus (HPV) oncoprotein E7 undergoes pH-dependent conformational changes. Treatment reveals its ability to self-assemble into stable, amyloid-like particles, offering new insights into viral oncogenesis.

Area of Science:

  • Oncology
  • Virology
  • Structural Biology

Background:

  • Human papillomavirus (HPV) E7 oncoprotein is crucial for viral transformation.
  • The precise structure and mechanism of E7 remain largely unknown.
  • E7 shares similarities with other DNA tumor virus oncoproteins like adenovirus E1A and SV40 T antigen.

Purpose of the Study:

  • To elucidate the structural properties and assembly mechanism of HPV16 E7.
  • To investigate the conformational transitions and particle formation of E7.
  • To characterize the nature of the assembled E7 structures.

Main Methods:

  • Dynamic light scattering and electron microscopy were used to determine particle size and mass.
  • Circular dichroism and fluorescence spectroscopy analyzed conformational changes.

Related Experiment Videos

  • Binding assays with Congo Red and thioflavin T assessed beta-sheet structures.

    • Main Results:

    • HPV16 E7, a nonglobular dimer, exhibits pH-dependent conformational changes.
    • Chelator treatment induced slow self-assembly into homogeneous spherical particles (790 kDa, 50 nm diameter).
    • Assembled particles showed a transition to beta-sheet structure, stability, and amyloid-binding dye interactions.

    Conclusions:

    • HPV E7 can transition from a disordered state to form stable, amyloid-like particles.
    • These conformational changes and assembly properties are key to understanding E7's oncogenic function.
    • The findings provide novel insights into the structural plasticity and aggregation behavior of viral oncoproteins.