Correlating the Structure and Activity of Y. pestis Ail in a Bacterial Cell Envelope |
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Authors: | James E. Kent Lynn M. Fujimoto Kyungsoo Shin Chandan Singh Yong Yao Sang Ho Park Stanley J. Opella Gregory V. Plano Francesca M. Marassi |
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Affiliation: | 1. Cancer Center, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, California;2. Department Chemistry and Biochemistry, University of California, San Diego, La Jolla, California;3. Department of Microbiology and Immunology, University of Miami Miller School of Medicine, Miami, Florida |
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Abstract: | Understanding microbe-host interactions at the molecular level is a major goal of fundamental biology and therapeutic drug development. Structural biology strives to capture biomolecular structures in action, but the samples are often highly simplified versions of the complex native environment. Here, we present an Escherichia coli model system that allows us to probe the structure and function of Ail, the major surface protein of the deadly pathogen Yersinia pestis. We show that cell surface expression of Ail produces Y. pestis virulence phenotypes in E. coli, including resistance to human serum, cosedimentation of human vitronectin, and pellicle formation. Moreover, isolated bacterial cell envelopes, encompassing inner and outer membranes, yield high-resolution solid-state NMR spectra that reflect the structure of Ail and reveal Ail sites that are sensitive to the bacterial membrane environment and involved in the interactions with human serum components. The data capture the structure and function of Ail in a bacterial outer membrane and set the stage for probing its interactions with the complex milieu of immune response proteins present in human serum. |
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