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Correlating the Structure and Activity of Y. pestis Ail in a Bacterial Cell Envelope. Biophys J 2021 Feb 02;120(3):453-462



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Pubmed Central ID




Scopus ID

2-s2.0-85099124668 (requires institutional sign-in at Scopus site)   3 Citations


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.

Author List

Kent JE, Fujimoto LM, Shin K, Singh C, Yao Y, Park SH, Opella SJ, Plano GV, Marassi FM


Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of Wisconsin
Kyungsoo Shin PhD Assistant Professor in the Biophysics department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Bacterial Outer Membrane Proteins
Escherichia coli
Virulence Factors
Yersinia pestis