Structural and topographical studies of the type IV bundle-forming pilus assembly complex of enteropathogenic Escherichia coli.

@article{Hwang2003StructuralAT,
  title={Structural and topographical studies of the type IV bundle-forming pilus assembly complex of enteropathogenic Escherichia coli.},
  author={Jaiweon Hwang and David W. Bieber and Sandra W. Ramer and Cheng-Yen Wu and Gary K. Schoolnik},
  journal={Journal of bacteriology},
  year={2003},
  volume={185 22},
  pages={
          6695-701
        }
}
The type IV bundle-forming pili (BFP) of enteropathogenic Escherichia coli (EPEC) are required for virulence in orally challenged human volunteers and for the localized adherence and autoaggregation in vitro phenotypes. BFP filament biogenesis and function are encoded by the 14-gene bfp operon. The BFP assembly complex, containing a BfpB-His6 fusion protein, was chemically cross-linked in situ, and the complex was then purified from BFP-expressing EPEC by a combination of nickel- and BfpB… CONTINUE READING

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  • Proceedings of the National Academy of Sciences of the United States of America
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