Flagellin outer domain dimerization modulates motility in pathogenic and soil bacteria from viscous environments.

Mark A B Kreutzberger, Richard C Sobe, Amber B Sauder, Sharanya Chatterjee, Alejandro Peña, Fengbin Wang, Jorge A Giron, Volker Kiessling, Tiago R D Costa, Vincent P Conticello, Gad Frankel, Melissa M Kendall, Birgit E Scharf, Edward H Egelman


Flagellar filaments function as the propellers of the bacterial flagellum and their supercoiling is key to motility. The outer domains on the surface of the filament are non-critical for motility in many bacteria and their structures and functions are not conserved. Here, we show the atomic cryo-electron microscopy structures for flagellar filaments from enterohemorrhagic Escherichia coli O157:H7, enteropathogenic E. coli O127:H6, Achromobacter, and Sinorhizobium meliloti, where the outer domains dimerize or tetramerize to form either a sheath or a screw-like surface. These dimers are formed by 180° rotations of half of the outer domains. The outer domain sheath (ODS) plays a role in bacterial motility by stabilizing an intermediate waveform and prolonging the tumbling of E. coli cells. Bacteria with these ODS and screw-like flagellar filaments are commonly found in soil and human intestinal environments of relatively high viscosity suggesting a role for the dimerization in these environments.