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Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP.

Upon infection of human cells, the herpes simplex virus protein VP16 associates with the endogenous cell-proliferation factor HCF. VP16 can also associate with HCFs from invertebrates, suggesting that VP16 mimics a cellular protein whose interaction with HCF has been conserved. Here, we show that VP16 mimics the human basic leucine-zipper protein LZIP, which, through association with HCF, may control cell-cycle progression. VP16 and LZIP share a tetrapeptide motif-D/EHXY-used to associate with human HCF. The LZIP-related Drosophila protein BBF-2/dCREB-A contains this HCF-binding motif, indicating that the LZIP-HCF interaction has been conserved during metazoan evolution.

Pubmed ID: 9389645


  • Freiman RN
  • Herr W


Genes & development

Publication Data

December 1, 1997

Associated Grants

  • Agency: NCI NIH HHS, Id: CA13106

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cell Division
  • Cell Line, Transformed
  • Cyclic AMP Response Element-Binding Protein A
  • DNA-Binding Proteins
  • Drosophila Proteins
  • Drosophila melanogaster
  • HeLa Cells
  • Herpes Simplex Virus Protein Vmw65
  • Herpesvirus 1, Human
  • Host Cell Factor C1
  • Humans
  • Leucine Zippers
  • Mice
  • Molecular Mimicry
  • Molecular Sequence Data
  • Proteins
  • Recombinant Fusion Proteins
  • Sequence Homology, Amino Acid
  • Transcription Factors