Characterization and purification of the F17 adhesin on the surface of bovine enteropathogenic and septicemic Escherichia coli.

@article{Lintermans1988CharacterizationAP,
  title={Characterization and purification of the F17 adhesin on the surface of bovine enteropathogenic and septicemic Escherichia coli.},
  author={P F Lintermans and Pierre Pohl and A Bertels and Gerard Charlier and Jo{\"e}l Vandekerckhove and Jozef Van Damme and J Schoup and C Schlicker and Taina K. Korhonen and Henri De Greve},
  journal={American journal of veterinary research},
  year={1988},
  volume={49 11},
  pages={1794-9}
}
The F17 antigen from bovine enterotoxigenic Escherichia coli strain (E coli 25KHO9), which adhered to calf intestinal villi, was isolated. An enterotoxin-negative derivative (25KHO9st) was used for further studies. Using an immunogold-labeling technique, the F17 antigen was characterized as a fimbrial protein. Pure fimbriae with a subunit molecular weight of 20,000 were obtained by homogenization and use of a sucrose gradient. The adhesion of E coli 25KHO9st was mediated by the F17 fimbriae, as… CONTINUE READING

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