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Molecular mimicry between IL-33 and KSHV for attachment to chromatin through the H2A-H2B acidic pocket.

Interleukin-33 (IL-33) is an IL-1-like ligand for the ST2 receptor that stimulates the production of Th2-associated cytokines. Recently, we showed that IL-33 is a chromatin-associated factor in the nucleus of endothelial cells in vivo. Here, we report the identification of a short IL-33 chromatin-binding peptide that shares striking similarities with a motif found in Kaposi sarcoma herpesvirus LANA (latency-associated nuclear antigen), which is responsible for the attachment of viral genomes to mitotic chromosomes. Similar to LANA, the IL-33 peptide docks into the acidic pocket formed by the H2A-H2B dimer at the nucleosomal surface and regulates chromatin compaction by promoting nucleosome-nucleosome interactions. Taken together, our data provide important new insights into the nuclear roles of IL-33, and show a unique example of molecular mimicry of a chromatin-associated cytokine by a DNA tumour virus. In addition, the data provide, to the best of our knowledge, the first demonstration of the existence of non-histone cellular factors that bind to the acidic pocket of the nucleosome.

Pubmed ID: 18688256

Authors

  • Roussel L
  • Erard M
  • Cayrol C
  • Girard JP

Journal

EMBO reports

Publication Data

October 2, 2008

Associated Grants

None

Mesh Terms

  • 3T3 Cells
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Antigens, Viral
  • Cell Line
  • Chromatin
  • Chromosomes, Human
  • Dimerization
  • Dogs
  • Herpesvirus 8, Human
  • Histones
  • Humans
  • Interleukins
  • Mice
  • Mitosis
  • Molecular Mimicry
  • Molecular Sequence Data
  • Nuclear Proteins
  • Nucleosomes
  • Protein Binding
  • Protein Structure, Tertiary