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Papillomavirus polypeptides E6 and E7 are zinc-binding proteins.

M S Barbosa1, D R Lowy, J T Schiller

  • 1Laboratory of Cellular Oncology, National Cancer Institute, Bethesda, Maryland 20892.

Journal of Virology
|March 1, 1989
PubMed
Summary

Papillomavirus E6 and E7 proteins bind zinc, suggesting they are metalloproteins. This study confirms their cysteine-mediated zinc coordination using a modified filter assay.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Virology

Background:

  • Human papillomavirus (HPV) E6 and E7 oncoproteins are key viral factors.
  • These proteins possess Cys-X-X-Cys motifs, implicated in zinc binding.
  • The role of zinc in E6 and E7 function requires direct experimental validation.

Purpose of the Study:

  • To investigate the zinc-binding capabilities of papillomavirus E6 and E7 proteins.
  • To determine if zinc coordination involves cysteine residues within these proteins.
  • To characterize E6 and E7 as potential metalloproteins.

Main Methods:

  • Development of a modified filter assay for detecting protein-bound zinc.
  • Utilizing well-characterized metalloproteins as controls.
  • Assessing zinc binding to E6 and E7 polypeptides under reducing conditions.

Main Results:

  • The modified assay successfully distinguished cysteine-mediated zinc binding.
  • E6 and E7 polypeptides from human papillomavirus type 18 and bovine papillomavirus type 1 demonstrated high-affinity zinc binding.
  • Zinc coordination by E6 and E7 appears to involve cysteine residues.

Conclusions:

  • Papillomavirus E6 and E7 proteins are likely metalloproteins.
  • Cysteine residues play a crucial role in the coordination of zinc by E6 and E7.
  • These findings provide direct evidence for the metalloprotein nature of E6 and E7.

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