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I24-Microfocus Macromolecular Crystallography	Structural insight into host recognition by aggregative adherence fimbriae of enteroaggregative Escherichia coli Andrea A. Berry , Yi Yang , Natalia Pakharukova , James Garnett , Wei-Chao Lee , Ernesto Cota , Jan Marchant , Saumendra Roy , Minna Tuittila , Bing Liu , Keith G. Inman , Fernando Ruiz-Perez , Inacio Mandomando , James P. Nataro , Anton V. Zavialov , Steve Matthews Plos Pathogens 10 (9) DOI: 10.1371/journal.ppat.1004404 PMID: 25232738 Diamond Proposal Number(s): [9424] Open Access Show Abstract ▼ Abstract: Enteroaggregative Escherichia coli (EAEC) is a leading cause of acute and persistent diarrhea worldwide. A recently emerged Shiga-toxin-producing strain of EAEC resulted in significant mortality and morbidity due to progressive development of hemolytic-uremic syndrome. The attachment of EAEC to the human intestinal mucosa is mediated by aggregative adherence fimbria (AAF). Using X-ray crystallography and NMR structures, we present new atomic resolution insight into the structure of AAF variant I from the strain that caused the deadly outbreak in Germany in 2011, and AAF variant II from archetype strain 042, and propose a mechanism for AAF-mediated adhesion and biofilm formation. Our work shows that major subunits of AAF assemble into linear polymers by donor strand complementation where a single minor subunit is inserted at the tip of the polymer by accepting the donor strand from the terminal major subunit. Whereas the minor subunits of AAF have a distinct conserved structure, AAF major subunits display large structural differences, affecting the overall pilus architecture. These structures suggest a mechanism for AAF-mediated adhesion and biofilm formation. Binding experiments using wild type and mutant subunits (NMR and SPR) and bacteria (ELISA) revealed that despite the structural differences AAF recognize a common receptor, fibronectin, by employing clusters of basic residues at the junction between subunits in the pilus. We show that AAF-fibronectin attachment is based primarily on electrostatic interactions, a mechanism not reported previously for bacterial adhesion to biotic surfaces.	Sep 2014

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I24-Microfocus Macromolecular Crystallography

Structural insight into host recognition by aggregative adherence fimbriae of enteroaggregative Escherichia coli