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Significance Flagella are used by many pathogenic bacteria not only for motility but also for adhesion to host cells and to other bacteria in biofilm formation. Since thousands of copies of flagellin, the protein that forms the flagellar filament, are exposed on the surface of bacteria, they are a target for immune surveillance by hosts. Some bacteria important to human health, such asCampylobacter jejuni andHelicobacter pylori , have managed to evade the innate immune recognition of their flagellin. We show, with an atomic structure of theCampylobacter jejuni flagellar filament, how mutations that destabilize the filament in one region recognized by vertebrates have been compensated for by new contacts not seen in other flagellar filaments that would stabilize these filaments.

Atomic structure of the Campylobacter jejuni flagellar filament reveals how ε Proteobacteria escaped Toll-like receptor 5 surveillance