Glycerol-induced unraveling of the tight helical conformation of Escherichia coli type 1 fimbriae.
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.
Department of Pathology, Washington University School of Medicine, St. Louis, Missouri.
S N
SN
Abraham
M
M
Land
S
S
Ponniah
R
R
Endres
D L
DL
Hasty
J P
JP
Babu
D004926:Escherichia coli / Q000648:ultrastructure*; D010861:Fimbriae, Bacterial / Q000187:drug effects / Q000648:ultrastructure*; D005990:Glycerol / Q000494:pharmacology*; D011487:Protein Conformation; D014357:Trypsin / Q000494:pharmacology
D014357:Trypsin; D005990:Glycerol