Molecular and Structural Aspects of Fimbriae Biosynthesis and Assembly in Escherichia Coli

FEMS Microbiol Rev. 1996 Oct;19(1):25-52. doi: 10.1111/j.1574-6976.1996.tb00252.x.

Abstract

Fimbriae are long filamentous polymeric protein structures located at the surface of bacterial cells. They enable the bacteria to bind to specific receptor structures and thereby to colonise specific surfaces. Fimbriae consist of so-called major and minor subunits, which form, in a specific order, the fimbrial structure. In this review emphasis is put on the genetic organisation, regulation and especially on the biosynthesis of fimbriae of enterotoxigenic Escherichia coli strains, and more in particular on K88 and related fimbriae, with ample reference to well-studied P and type 1 fimbriae. The biosynthesis of these fimbriae requires two specific and unique proteins, a periplasmic chaperone and an outer membrane located molecular usher ('doorkeeper'). Molecular and structural aspects of the secretion of fimbrial subunits across the cytoplasmic membrane, the interaction of these subunits with periplasmic molecular chaperone, their translocation to the inner site of the outer membrane and their interaction with the usher protein, as well as the (ordered) translocation of the subunits across the outer membrane and their assembly into a growing fimbrial structure will be described. A model for K88 fimbriae is presented.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Bacterial Outer Membrane Proteins / biosynthesis
  • Bacterial Outer Membrane Proteins / chemistry
  • Bacterial Outer Membrane Proteins / genetics
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli / pathogenicity
  • Fimbriae, Bacterial / metabolism*
  • Gene Expression Regulation, Bacterial
  • Genes, Bacterial
  • Humans
  • Models, Molecular
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism
  • Molecular Sequence Data
  • Molecular Structure
  • Sequence Homology, Amino Acid

Substances

  • Bacterial Outer Membrane Proteins
  • Molecular Chaperones