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SurA is a periplasmic protein folding factor involved in chaperoning and trafficking of outer membrane proteins across the Gram-negative bacterial periplasm. In addition, SurA also possesses peptidyl-prolylcis/trans isomerase activity. We have previously reported that in enteropathogenicYersinia pseudotuberculosis , SurA is needed for bacterial virulence and envelope integrity. In this study, we investigated the role of SurA in the assembly of importantYersinia adhesins. Using genetic mutation, biochemical characterization, and anin vitro -based bacterial host cell association assay, we confirmed that surface localization of the invasin adhesin is dependent on SurA. As asurA deletion also has some impact on the levels of individual components of the BAM complex in theYersinia outer membrane, abolished invasin surface assembly could reflect both a direct loss of SurA-dependent periplasmic targeting and a potentially compromised BAM complex assembly platform in the outer membrane. To various degrees, the assembly of two other adhesins, Ail and the pH 6 antigen fibrillum PsaA, also depends on SurA. Consequently, loss of SurA leads to a dramatic reduction inYersinia attachment to eukaryotic host cells. Genetic complementation ofsurA deletion mutants indicated a prominent role for SurA chaperone function in outer membrane protein assembly. Significantly, the N terminus of SurA contributed most of this SurA chaperone function. Despite a dominant chaperoning role, it was also evident that SurA isomerization activity did make a modest contribution to this assembly process.

Demarcating SurA Activities Required for Outer Membrane Targeting of Yersinia pseudotuberculosis Adhesins