A Novel Protein to Bind RCV Core Protein: The Carboxyl Terminus-Truncated Core$_{120}$ Protein of HCV Interacts with E7 Antigen of Human Papilloma Virus Type 18

  • So, Kwan Young (Department of Biochemistry, Chungnam National University) ;
  • Lee, Hyang Ju (Department of Biochemistry, Chungnam National University) ;
  • Kang, Kwang Il (Institute of Biotechnology, Chungnam National University) ;
  • Lee, Hay Young (Institute of Biotechnology, Chungnam National University) ;
  • Lim, Kyu (Biochemistry, College of Medicine, Chungnam National University) ;
  • Park, Sang Gi (Biology, Chungnam National University) ;
  • Ahn, Jeong Keun (Microbiology, College of Natural Sciences, Chungnam National University) ;
  • Kim, Chul Joong (Veterinary Medicine, College of Veterinary Medicine, Chungnam National University) ;
  • Lee, Chong Kil (Department of Pharmacy, College of Pharmacy, Chungbuk National University) ;
  • Kim, Young Sang (Department of Biochemistry, Chungnam National University)
  • Published : 2002.10.01

Abstract

In order to analyze the cellular proteins which interact with core protein of hepatitis C virus (HCV), a yeast two-hybrid screening technique was employed. A carboxyl terminus truncated core protein, which contained amino acid residues from the 1st to 120th, was used as a bait to screen cellular proteins. The expression library prepared from HeLa cell was screened and 400 positive clones were selected. The 75 clones from the positive clones were sequenced and analyzed by undergoing the Blast search. Interestingly, 7 out of the 75 clones encoded E7 antigen of human papilloma virus (HPV). We studied in detail the Interaction between the truncated version of HCV core and E7 antigen in vitro. The core$_{120}$ protein expressed in chimeric form with G57 was able to bring down the E7 protein of HPV type 18 expressed in bacteria. It is therefore suggested that the core of HCV might affect the interaction between E7 and a normal cellular tumor suppressor, known as Rb protein.

Keywords

References

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