Fiber assembly by the chaperone-usher pathway

Frederic G. Sauer, Han Remaut, Scott J. Hultgren, Gabriel Waksman

Research output: Contribution to journalReview articlepeer-review

157 Scopus citations

Abstract

Bacterial pathogens utilize the chaperone-usher pathway to assemble extracellular multi-subunit fibers essential for virulence. The periplasmic chaperone facilitates the initial folding of fiber subunits but then traps them in activated folding transition states. Chaperone dissociation releases the folding energy that drives subunit incorporation into the fiber, which grows through a pore formed by the outer-membrane usher.

Original languageEnglish
Pages (from-to)259-267
Number of pages9
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Volume1694
Issue number1-3 SPEC.ISS.
DOIs
StatePublished - Nov 11 2004

Keywords

  • Bacterial pathogenesis
  • Chaperone-usher pathway
  • Pilus assembly
  • Protein folding
  • Structural basis of fiber formation

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