The molecular dissection of the chaperone-usher pathway

Biochim Biophys Acta. 2014 Aug;1843(8):1559-67. doi: 10.1016/j.bbamcr.2013.09.023. Epub 2013 Oct 16.


Secretion systems are specialized in transport of proteins, DNA or nutrients across the cell envelope of bacteria and enable them to communicate with their environment. The chaperone-usher (CU) pathway is used for assembly and secretion of a large family of long adhesive protein polymers, termed pili, and is widespread among Gram-negative pathogens [1]. Moreover, recent evidence has indicated that CU secretion systems are also involved in sporulation [2,3]. In this review we focus on the structural biology of the paradigmatic type 1 and P pili CU systems encoded by uropathogenic Escherichia coli (UPEC), where recent progress has provided unprecedented insights into pilus assembly and secretion mechanism. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey.

Keywords: Chaperone–usher pathway; Donor strand complementation; Donor strand exchange; P pilus; Type 1 pilus; Urinary tract infection.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adhesins, Escherichia coli / chemistry
  • Adhesins, Escherichia coli / metabolism
  • Cell Membrane / chemistry
  • Cell Membrane / genetics
  • Cell Membrane / metabolism*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli / pathogenicity
  • Fimbriae Proteins / chemistry
  • Fimbriae Proteins / metabolism
  • Fimbriae, Bacterial / metabolism
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / metabolism
  • Protein Binding
  • Protein Conformation
  • Protein Transport*
  • Receptors, Immunologic / genetics
  • Receptors, Immunologic / metabolism
  • Urinary Tract Infections / genetics
  • Urinary Tract Infections / metabolism
  • Urinary Tract Infections / microbiology*


  • Adhesins, Escherichia coli
  • Molecular Chaperones
  • Receptors, Immunologic
  • fimH protein, E coli
  • fimbriae receptor, type 1
  • Fimbriae Proteins