Complex formation of the nonstructural protein 3 of hepatitis C virus with the p53 tumor suppressor

FEBS Lett. 1998 Nov 6;438(3):258-62. doi: 10.1016/s0014-5793(98)01312-x.

Abstract

By co-immunoprecipitation analysis, we demonstrated that wt-p53 formed a complex with non-structural protein (NS) 3 of hepatitis C virus, both in the absence and the presence of NS4A, a viral cofactor that strongly associates with NS3. Deletional analysis revealed that a portion near the N-terminus of NS3 (amino acids (aa) 1055 and 1200), which is different from the NS4A binding site, was necessary for the complex formation with wt-p53. On the other hand, a portion near the C-terminus of wt-p53 (aa 301-360), which has been reported to contain the oligomerization domain, was important for the complex formation with NS3.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • DNA Primers
  • HeLa Cells
  • Hepacivirus / metabolism*
  • Humans
  • Molecular Sequence Data
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Sequence Deletion
  • Transfection
  • Tumor Suppressor Protein p53 / chemistry
  • Tumor Suppressor Protein p53 / isolation & purification
  • Tumor Suppressor Protein p53 / metabolism*
  • Viral Nonstructural Proteins / chemistry
  • Viral Nonstructural Proteins / genetics
  • Viral Nonstructural Proteins / metabolism*

Substances

  • DNA Primers
  • NS3 protein, hepatitis C virus
  • NS4 protein, hepatitis C virus
  • Recombinant Proteins
  • Tumor Suppressor Protein p53
  • Viral Nonstructural Proteins