Structural insights into ail-mediated adhesion in Yersinia pestis

Satoshi Yamashita, Petra Lukacik, Travis J. Barnard, Nicholas Noinaj, Suleyman Felek, Tiffany M. Tsang, Eric S. Krukonis, B. Joseph Hinnebusch, Susan K. Buchanan

Research output: Contribution to journalArticlepeer-review

52 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1672-1682
Number of pages11
JournalStructure
Volume19
Issue number11
DOIs
Publication statusPublished - 2011 Nov 9

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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