The protein-protein interaction map of Helicobacter pylori

Nature. 2001 Jan 11;409(6817):211-5. doi: 10.1038/35051615.


With the availability of complete DNA sequences for many prokaryotic and eukaryotic genomes, and soon for the human genome itself, it is important to develop reliable proteome-wide approaches for a better understanding of protein function. As elementary constituents of cellular protein complexes and pathways, protein-protein interactions are key determinants of protein function. Here we have built a large-scale protein-protein interaction map of the human gastric pathogen Helicobacter pylori. We have used a high-throughput strategy of the yeast two-hybrid assay to screen 261 H. pylori proteins against a highly complex library of genome-encoded polypeptides. Over 1,200 interactions were identified between H. pylori proteins, connecting 46.6% of the proteome. The determination of a reliability score for every single protein-protein interaction and the identification of the actual interacting domains permitted the assignment of unannotated proteins to biological pathways.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Databases, Factual
  • Escherichia coli / genetics
  • Gene Library
  • Helicobacter pylori / metabolism*
  • Humans
  • Internet
  • Molecular Sequence Data
  • Protein Binding
  • Proteome
  • Sequence Alignment
  • Software
  • Urease / metabolism


  • Bacterial Proteins
  • Proteome
  • Urease