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Chem Biol. 2012 Feb 24;19(2):287-96. doi: 10.1016/j.chembiol.2011.11.009. Epub 2011 Dec 29.

ATP-independent control of autotransporter virulence protein transport via the folding properties of the secreted protein.

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  • 1Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556-5670, USA.


Autotransporter (AT) proteins are the largest class of extracellular virulence proteins secreted from Gram-negative bacteria. The mechanism by which AT proteins cross the bacterial outer membrane (OM), in the absence of ATP or another external energy source, is unknown. Here we demonstrate a linear correlation between localized regions of stability (ΔG(folding)) in the mature virulence protein (the AT "passenger") and OM secretion efficiency. Destabilizing the C-terminal β-helical domain of a passenger reduced secretion efficiency. In contrast, destabilizing the globular N-terminal domain of a passenger produced a linearly correlated increase in secretion efficiency. Thus, C-terminal passenger stability facilitates OM secretion, whereas N-terminal stability hinders it. The contributions of regional passenger stability to OM secretion demonstrate a crucial role for the passenger itself in directing its secretion, suggesting a novel type of ATP-independent, folding-driven transporter.

Copyright © 2012 Elsevier Ltd. All rights reserved.

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