The role of SurA factor in outer membrane protein transport and virulence.

The Escherichia coli periplasmic chaperone and peptidyl-prolyl isomerase (PPIase) SurA is a major factor in the biogenesis of β-barrel outer membrane proteins (OMPs) and as such plays an integral role in cell envelope homeostasis and cell envelope functions. Recently, the biological importance of SurA was further substantiated by the finding that SurA also affects pathogenicity, being required for full virulence of uropathogenic Escherichia coli, Salmonella, and Shigella spp. Moreover, given the conservation of the protein, SurA likely plays similar roles in other Gram-negative bacteria and may hence prove a valuable drug target against Gram-negative pathogens. While our understanding on how SurA promotes transport and folding of β-barrel OMPs, how it provides support to virulence, and how it functions at a molecular level is still limited, major contributions have recently been made on our way to find answers to these questions. This review is a compilation of our current state of knowledge on E. coli SurA function and a discussion of recent findings with a particular emphasis on the pleiotropic contributions of SurA to pathogenicity.