Recombinant fragilysin isoforms cause E-cadherin cleavage of intact cells and do not cleave isolated E-cadherin.

@article{Kharlampieva2015RecombinantFI,
  title={Recombinant fragilysin isoforms cause E-cadherin cleavage of intact cells and do not cleave isolated E-cadherin.},
  author={Daria D. Kharlampieva and Valentin A. Manuvera and Oleg V Podgorny and Ekaterina N. Grafskaia and Sergey Kovalchuk and Olga Pobeguts and Ilya A. Altukhov and Vadim M. Govorun and Vassili N. Lazarev},
  journal={Microbial pathogenesis},
  year={2015},
  volume={83-84},
  pages={47-56}
}
The fragilysin (BFT) is a protein secreted by enterotoxigenic Bacteroides fragilis strains. BFT contains zinc-binding motif which was found in the metzincins family of metalloproteinases. In this study, we generated three known recombinant isoforms of BFT using Escherichia coli, tested their activity and examined whether E-cadherin is a substrate for BFTs. BFT treatment of HT-29 cells induced endogenous E-cadherin cleavage, and this BFT activity requires the native structure of zinc-binding… CONTINUE READING

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