Structure and function of enterotoxigenic Escherichia coli fimbriae from differing assembly pathways

Mol Microbiol. 2015 Jan;95(1):116-26. doi: 10.1111/mmi.12847. Epub 2014 Nov 27.

Abstract

Pathogenic enterotoxigenic Escherichia coli (ETEC) are the major bacterial cause of diarrhea in young children in developing countries and in travelers, causing significant mortality in children. Adhesive fimbriae are a prime virulence factor for ETEC, initiating colonization of the small intestinal epithelium. Similar to other Gram-negative bacteria, ETEC express one or more diverse fimbriae, some assembled by the chaperone-usher pathway and others by the alternate chaperone pathway. Here, we elucidate structural and biophysical aspects and adaptations of each fimbrial type to its respective host niche. CS20 fimbriae are compared with colonization factor antigen I (CFA/I) fimbriae, which are two ETEC fimbriae assembled via different pathways, and with P-fimbriae from uropathogenic E. coli. Many fimbriae unwind from their native helical filament to an extended linear conformation under force, thereby sustaining adhesion by reducing load at the point of contact between the bacterium and the target cell. CFA/I fimbriae require the least force to unwind, followed by CS20 fimbriae and then P-fimbriae, which require the highest unwinding force. We conclude from our electron microscopy reconstructions, modeling and force spectroscopy data that the target niche plays a central role in the biophysical properties of fimbriae that are critical for bacterial pathophysiology.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Enterotoxigenic Escherichia coli / chemistry
  • Enterotoxigenic Escherichia coli / genetics
  • Enterotoxigenic Escherichia coli / metabolism*
  • Fimbriae Proteins / chemistry*
  • Fimbriae Proteins / genetics*
  • Fimbriae, Bacterial / chemistry*
  • Fimbriae, Bacterial / metabolism
  • Microscopy, Electron
  • Models, Molecular
  • Protein Structure, Secondary
  • Structural Homology, Protein

Substances

  • colonization factor antigens
  • Fimbriae Proteins