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Bacterial flagella hijack type IV pili proteins to control motility.

ABSTRACT: 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.

SUBMITTER: Liu X

PROVIDER: S-EPMC10823254 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature

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Bacterial flagella hijack type IV pili proteins to control motility.

Liu Xiaolin X Tachiyama Shoichi S Zhou Xiaotian X Mathias Rommel A RA Bonny Sharmin Q SQ Khan Mohammad F MF Xin Yue Y Roujeinikova Anna A Liu Jun J Ottemann Karen M KM

Proceedings of the National Academy of Sciences of the United States of America 20240118 4

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 ...[more]

PMID: 38236729

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