Structural insights into Ail-mediated adhesion in Yersinia pestis

Structure. 2011 Nov 9;19(11):1672-82. doi: 10.1016/j.str.2011.08.010.


Ail is an outer membrane protein from Yersinia pestis that is highly expressed in a rodent model of bubonic plague, making it a good candidate for vaccine development. Ail is important for attaching to host cells and evading host immune responses, facilitating rapid progression of a plague infection. Binding to host cells is important for injection of cytotoxic Yersinia outer proteins. To learn more about how Ail mediates adhesion, we solved two high-resolution crystal structures of Ail, with no ligand bound and in complex with a heparin analog called sucrose octasulfate. We identified multiple adhesion targets, including laminin and heparin, and showed that a 40 kDa domain of laminin called LG4-5 specifically binds to Ail. We also evaluated the contribution of laminin to delivery of Yops to HEp-2 cells. This work constitutes a structural description of how a bacterial outer membrane protein uses a multivalent approach to bind host cells.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Bacterial Adhesion*
  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Outer Membrane Proteins / metabolism
  • Bacterial Outer Membrane Proteins / physiology
  • Bacterial Proteins / metabolism
  • Cell Line
  • Crystallography, X-Ray
  • Extracellular Matrix / metabolism
  • Extracellular Matrix Proteins / metabolism
  • Host-Pathogen Interactions
  • Humans
  • Laminin / metabolism
  • Membrane Proteins / metabolism
  • Molecular Chaperones / metabolism
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Sucrose / analogs & derivatives*
  • Sucrose / chemistry
  • Surface Properties
  • Virulence Factors / chemistry*
  • Virulence Factors / metabolism
  • Virulence Factors / physiology
  • Yersinia pestis*


  • Ail protein, Yersinia pestis
  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Extracellular Matrix Proteins
  • Laminin
  • Membrane Proteins
  • Molecular Chaperones
  • Virulence Factors
  • YscG protein, Yersinia
  • Sucrose
  • sucrose octasulfate

Associated data

  • PDB/3QRA
  • PDB/3QRC