Gram-negative bacteria use an array of tripartite efflux pumps to defend against toxic metals and organic chemicals. How these multicomponent efflux complexes maintain and adjust the assembly of their constituents to function effectively in the cell remains poorly defined. Using single-molecule imaging and tracking approaches, we recently discovered that CusCBA, a Cu+/Ag+ efflux pump of the resistance-nodulation-division family, undergoes metal-responsive dynamic assembly-disassembly in the cell for effective efflux without compromising the periplasmic plasticity of the Gram-negative bacterium E. coli. We further identified that surprisingly, the periplasmic adaptor protein CusB acts the sensor for the metal substrate and triggers the assembly of the complex for efflux. Depending on available time, I will also describe our recent collaborative efforts in mechanically manipulating individual E. coli cells to alter CusCBA assembly in the cell and consequently the bacteria's ability to extrude toxins.

Understanding and manipulating bacterial toxin efflux at single-molecule single-cell level

2019 Spring National Meeting

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