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Bacterial flagella hijack type IV pili proteins to control motility.

Xiaolin LiuShoichi TachiyamaXiaotian ZhouRommel A MathiasSharmin Q BonnyMohammad F KhanYue XinAnna RoujeinikovaJun LiuKaren M Ottemann
Published in: Proceedings of the National Academy of Sciences of the United States of America (2024)
Bacterial flagella and type IV pili (TFP) are surface appendages that enable motility and mechanosensing through distinct mechanisms. These structures were previously thought to have no components in common. Here, we report that TFP and some flagella share proteins PilO, PilN, and PilM, which we identified as part of the Helicobacter pylori flagellar motor. H. pylori mutants lacking PilO or PilN migrated better than wild type in semisolid agar because they continued swimming rather than aggregated into microcolonies, mimicking the TFP-regulated surface response. Like their TFP homologs, flagellar PilO/PilN heterodimers formed a peripheral cage that encircled the flagellar motor. These results indicate that PilO and PilN act similarly in flagella and TFP by differentially regulating motility and microcolony formation when bacteria encounter surfaces.
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