Acquisition of omptin reveals cryptic virulence function of autotransporter YapE in Yersinia pestis

Mol Microbiol. 2013 Jul;89(2):276-87. doi: 10.1111/mmi.12273. Epub 2013 Jun 10.


Autotransporters, the largest family of secreted proteins in Gram-negative bacteria, perform a variety of functions, including adherence, cytotoxicity and immune evasion. In Yersinia pestis the autotransporter YapE has adhesive properties and contributes to disease in the mouse model of bubonic plague. Here, we demonstrate that omptin cleavage of Y. pestis YapE is required to mediate bacterial aggregation and adherence to eukaryotic cells. We demonstrate that omptin cleavage is specific for the Y. pestis and Y. pseudotuberculosis YapE orthologues but is not conserved in the Yersinia enterocolitica protein. We also show that cleavage of YapE occurs in Y. pestis but not in the enteric Yersinia species, and requires the omptin Pla (plasminogen activator protease), which is encoded on the Y. pestis-specific plasmid pPCP1. Together, these data show that post-translation modification of YapE appears to be specific to Y. pestis, was acquired along with the acquisition of pPCP1 during the divergence of Y. pestis from Y. pseudotuberculosis, and are the first evidence of a novel mechanism to regulate bacterial adherence.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Adhesion*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Cell Line
  • Humans
  • Macrophages
  • Mice
  • Plague / microbiology
  • Plague / pathology
  • Protein Processing, Post-Translational*
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / metabolism*
  • Virulence
  • Yersinia pestis / genetics
  • Yersinia pestis / metabolism
  • Yersinia pestis / pathogenicity*
  • Yersinia pseudotuberculosis / genetics
  • Yersinia pseudotuberculosis / metabolism
  • Yersinia pseudotuberculosis / pathogenicity


  • Bacterial Proteins
  • Serine Endopeptidases
  • omptin outer membrane protease