Effect of chaperone-adhesin complex on plug release by the PapC usher.

The P pilus of uropathogenic Escherichia coli is a multisubunit fiber assembled at the outer membrane in a defined sequence by a chaperone/usher secretion system, comprising a periplasmic chaperone and a beta-barrel outer membrane protein, the PapC usher. To gain insight into the pilus biogenesis mechanism, we used patch clamp electrophysiology to investigate the effect of the initiating adhesin subunit, as it is delivered to PapC in a complex with the chaperone. We show that the chaperone-adhesin complex facilitates opening of the PapC pore and appears to engage within the PapC lumen, in agreement with prior biochemical and structural data.