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Showing papers by "Scott J. Hultgren published in 1997"


Journal ArticleDOI
25 Apr 1997-Science
TL;DR: Virtually all uropathogenic strains of Escherichia coli, the primary cause of cystitis, assemble adhesive surface organelles called type 1 pili that contain the FimH adhesin that reduce in vivo colonization of the bladder mucosa by more than 99 percent.
Abstract: Virtually all uropathogenic strains of Escherichia coli, the primary cause of cystitis, assemble adhesive surface organelles called type 1 pili that contain the FimH adhesin. Sera from animals vaccinated with candidate FimH vaccines inhibited uropathogenic E. coli from binding to human bladder cells in vitro. Immunization with FimH reduced in vivo colonization of the bladder mucosa by more than 99 percent in a murine cystitis model, and immunoglobulin G to FimH was detected in urinary samples from protected mice. Furthermore, passive systemic administration of immune sera to FimH also resulted in reduced bladder colonization by uropathogenic E. coli. This approach may represent a means of preventing recurrent and acute infections of the urogenital mucosa.

578 citations


Journal ArticleDOI
TL;DR: In the absence of the chaperone, subunits remained tethered to the membrane and were driven off‐pathway via non‐productive interactions, which were detrimental to cell growth and restored by co‐expression of PapD.
Abstract: The assembly of interactive protein subunits into extracellular structures, such as pilus fibers in the Enterobacteriaceae, is dependent on the activity of PapD-like periplasmic chaperones. The ability of PapD to undergo a beta zippering interaction with the hydrophobic C-terminus of pilus subunits facilitates their folding and release from the cytoplasmic membrane into the periplasm. In the absence of the chaperone, subunits remained tethered to the membrane and were driven off-pathway via non-productive interactions. These off-pathway reactions were detrimental to cell growth; wild-type growth was restored by co-expression of PapD. Subunit misfolding in the absence of PapD was sensed by two parallel pathways: the Cpx two-component signaling system and the sigma E modulatory pathway.

254 citations


Journal ArticleDOI
TL;DR: Observations of the interaction of the Escherichia coli PapD chaperone with the synthetic peptide PapG308‐314 indicate that the peptide binds to PapD in an extended conformation and are in excellent agreement with a recent crystal structure of a PapG peptide complexed with PapD.

10 citations