The PapC usher forms an oligomeric channel: implications for pilus biogenesis across the outer membrane.

Article Details

Citation

Thanassi DG, Saulino ET, Lombardo MJ, Roth R, Heuser J, Hultgren SJ

The PapC usher forms an oligomeric channel: implications for pilus biogenesis across the outer membrane.

Proc Natl Acad Sci U S A. 1998 Mar 17;95(6):3146-51.

PubMed ID
9501230 [ View in PubMed
]
Abstract

Bacterial virulence factors are typically surface-associated or secreted molecules that in Gram-negative bacteria must cross the outer membrane (OM). Protein translocation across the bacterial OM is not well understood. To elucidate this process we studied P pilus biogenesis in Escherichia coli. We present high-resolution electron micrographs of the OM usher PapC and show that it forms an oligomeric complex containing a channel approximately 2 nm in diameter. This is large enough to accommodate pilus subunits or the linear tip fibrillum of the pilus but not large enough to accommodate the final 6.8-nm-wide helical pilus rod. We show that P pilus rods can be unraveled into linear fibers by incubation in 50% glycerol. Thus, they are likely to pass through the usher in this unwound form. Packaging of these fibers into their final helical structure would only occur outside the cell, a process that may drive outward growth of the pilus organelles. The usher complex appears to be similar to complexes formed by members of the PulD/pIV family of OM proteins, and thus these two protein families, previously thought to be unrelated, may share structural and functional homologies.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Outer membrane usher protein PapCP07110Details