K. Qin et al resolve Vibrio alginolyticus sheathed flagella structure and rotation mechanism
Updated
Updated · Nature.com · Apr 23
K. Qin et al resolve Vibrio alginolyticus sheathed flagella structure and rotation mechanism
6 articles · Updated · Nature.com · Apr 23
Using cryo-EM and genetic analyses, the team identified FlaD2 as the main flagellin and revealed a highly electronegative filament surface enveloped by a bilayered sheath.
Electrostatic repulsion between the filament and sheath likely reduces friction, enabling high-speed flagellar rotation, while a unique FliD cap domain may coordinate sheath assembly with filament growth.
These findings provide molecular insight into bacterial motility and virulence, building on recent atomic mapping advances and offering new targets for therapies against antibiotic-resistant Vibrio infections.
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Structural Insights into Vibrio’s Sheathed Flagellum: A Blueprint to Combat Rising Antibiotic Resistance
Overview
In April 2026, researchers at King's College London revealed the atomic structure of the sheathed flagellum in Vibrio alginolyticus using advanced cryo-EM techniques. They identified FlaD2 as the main building block and discovered that electrostatic repulsion between the filament and its sheath reduces friction, enabling high-speed rotation. An additional domain in the FliD protein anchors the filament tip to the sheath, ensuring synchronized movement. This sheath not only helps the bacterium evade the immune system by shielding flagellins but also promotes the release of outer membrane vesicles carrying virulence factors. These insights open new paths for antivirulence therapies targeting the flagellum, crucial as climate change and antibiotic resistance increase Vibrio infections worldwide.