Multiple driving forces required for efficient secretion of autotransporter virulence proteins.

ABSTRACT: Autotransporter (AT) proteins are a broad class of virulence proteins from Gram-negative bacterial pathogens that require their own C-terminal transmembrane domain to translocate their N-terminal passenger across the bacterial outer membrane (OM). But given the unavailability of ATP or a proton gradient across the OM, it is unknown what energy source(s) drives this process. Here we used a combination of computational and experimental approaches to quantitatively compare proposed AT OM translocation mechanisms. We show directly for the first time that when translocation was blocked an AT passenger remained unfolded in the periplasm. We demonstrate that AT secretion is a kinetically controlled, non-equilibrium process coupled to folding of the passenger and propose a model connecting passeng

SUBMITTER: Drobnak I 

PROVIDER: S-EPMC4400326 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature