Satoshi Yamashita

National Institutes of Health, Bethesda, MD, United States

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Publications (2)11.99 Total impact

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    ABSTRACT: Graphical Abstract Figure optionsView in workspaceDownload full-size imageDownload high-quality image (313 K)Download as PowerPoint slide Highlights ► Ail is an 8-stranded β-barrel having 4 extracellular loops that function in adhesion ► Ail-laminin and Ail-fibronectin interactions mediate delivery of Yops to host cells ► Ail has two binding sites for heparin that also confer adhesion to host cells
    Structure 11/2011; 19(11):1672–1682. · 5.99 Impact Factor
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    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.
    Structure 11/2011; 19(11):1672-82. · 5.99 Impact Factor

Publication Stats

14 Citations
11.99 Total Impact Points

Top Journals


  • 2011
    • National Institutes of Health
      • Laboratory of Molecular Biology
      Bethesda, MD, United States
    • The National Institute of Diabetes and Digestive and Kidney Diseases
      Maryland, United States