Structural Insights into Ail-Mediated Adhesion in Yersinia pestis

Journal Article · Mon Jan 30 04:00:00 EST 2012 · Structure

DOI:https://doi.org/10.1016/j.str.2011.08.010· OSTI ID:1034189

Yamashita, Satoshi; Lukacik, Petra; Barnard, Travis J; Noinaj, Nicholas; Felek, Suleyman; Tsang, Tiffany M; Krukonis, Eric S; Hinnebusch, B Joseph; Buchanan, Susan K ^[1]

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1. Michigan

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.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: NIH
• OSTI ID: 1034189
• Journal Information: Structure, Journal Name: Structure Journal Issue: 11 Vol. 19
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
ADHESION
CRYSTAL STRUCTURE
HEPARIN
MEMBRANE PROTEINS
PROTEINS
RODENTS
SACCHAROSE
TARGETS
VACCINES