Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite binding.

@article{Vincents2004EnzymaticCO,
  title={Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite binding.},
  author={Bjarne Vincents and Ulrich von Pawel-Rammingen and Lars Bj{\"o}rck and Magnus Abrahamson},
  journal={Biochemistry},
  year={2004},
  volume={43 49},
  pages={
          15540-9
        }
}
  • Bjarne Vincents, Ulrich von Pawel-Rammingen, +1 author Magnus Abrahamson
  • Published in Biochemistry 2004
  • Chemistry, Medicine
  • Streptococcus pyogenes, an important pathogen in humans, secretes an IgG specific endopeptidase named IdeS. To elucidate the mechanism that is responsible for this specificity, we have here characterized the activity of IdeS in detail. Both gamma chains of human IgG or its Fc fragment were cleaved in the hinge region after Gly236 by IdeS, but other proteins or synthetic peptides containing sequences such as the P(4)-P(1) segment in the IgG cleavage site, or long peptides resembling the IgG… CONTINUE READING

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