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Gastric interactions

Genome Biology20012:spotlight-20010117-01

  • Published:


  • Polypeptide
  • False Positive
  • False Negative
  • Background Noise
  • Biological Pathway

Large numbers of protein-protein interactions have been mapped for yeast and worms, and now in the January 11 Nature, Rain et al. present the first large set of interactions for a prokaryote (Nature 2001, 409:211-215). The two-hybrid screen of 261 proteins from the gastric pathogen Heliobacter pylori against a library of genome-encoded polypeptides revealed 1,200 putative interactions. Screening against a library allows the identification of interacting domains, and reduces the rate of false negatives encountered in classical pair-wise screens. A strong selection protocol reduces the number of false positives. Rain et al. also use a probability score to compute the likelihood that a given two-hybrid result is a consequence of background noise, and use some of the identified interactions to assign various proteins to particular biological pathways.


  1. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae.Google Scholar
  2. Protein interaction mapping in C. elegans using proteins involved in vulval development.Google Scholar
  3. Nature, []


© BioMed Central Ltd 2001