Glycerol-induced unraveling of the tight helical conformation of Escherichia coli type 1 fimbriae

J Bacteriol. 1992 Aug;174(15):5145-8. doi: 10.1128/jb.174.15.5145-5148.1992.

Abstract

Glycerol was found to unravel the helical conformation of Escherichia coli type 1 fimbriae without appreciable depolymerization. The linearized fimbrial polymers have a diameter of 2 nm, react strongly with a monoclonal antibody directed at an inaccessible epitope on native fimbriae, and display greater mannose-binding activity and trypsin sensitivity than native fimbriae. Removal of glycerol by dialysis results in spontaneous reassembly of the linear polymers into structures morphologically, antigenically, and functionally indistinguishable from native fimbriae.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Escherichia coli / ultrastructure*
  • Fimbriae, Bacterial / drug effects
  • Fimbriae, Bacterial / ultrastructure*
  • Glycerol / pharmacology*
  • Protein Conformation
  • Trypsin / pharmacology

Substances

  • Trypsin
  • Glycerol