Part:BBa_K380010

Immunoglobulin G protease (IdeS)

Immunoglobulin G protease (IdeS) is a proteolytic enzyme produced by Streptococcus pyogenes. The protein is designated to IdeS for Immunoglobulin G-degrading enzyme of S. pyogenes. This streptococcal cysteine proteinase, IdeS, is an immunoglobulin-degrading enzyme. It has a high specificity to cleave human IgG antibodies at the hinge region.

Reference:

• IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G. von Pawel-Rammingen U et al. EMBO J. 2002 Apr 2;21(7):1607-15.
• IdeS and SpeB: immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes. von Pawel-Rammingen U et al. Curr Opin Microbiol. 2003 Feb;6(1):50-5.

Immunoglobulin G protease (IdeS): Protein name: IgG-degrading protease.

Molecular function: Protease

Protein existence: Evidence at protein level. http://www.uniprot.org/uniprot/Q7DAM2. The identification, purification and characterization of IgG protease (IdeS) was first done by IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G. von Pawel-Rammingen U et al. EMBO J. 2002 Apr 2;21(7):1607-15.

Our iGEM group recived this gene from http://www.umu.se/sok/english/staff-directory/view-person?uid=ulvo0001.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  INCOMPATIBLE WITH RFC[1000]

  Illegal SapI.rc site found at 268
  

MIT MAHE 2020

Summary

Immunoglobulin G protease (IdeS) is a proteolytic enzyme produced by Streptococcus pyogenes. The protein is designated to IdeS for Immunoglobulin G-degrading enzyme of S. pyogenes. This streptococcal cysteine proteinase, IdeS, is an immunoglobulin-degrading enzyme. It has a high specificity to cleave human IgG antibodies at the hinge region.

References

1. Johansson, B. P., Shannon, O., & Björck, L. (2008). IdeS: a bacterial proteolytic enzyme with therapeutic potential. PloS one, 3(2), e1692. https://doi.org/10.1371/journal.pone.0001692

2. Woodle, E. S., Tremblay, S., & Driscoll, J. J. (2017). IgG Endopeptidase in Highly Sensitized Patients Undergoing Transplantation. The New England journal of medicine, 377(17), 1692–1693. https://doi.org/10.1056/NEJMc1711335

3. Nandakumar, K. S., Johansson, B. P., Björck, L., & Holmdahl, R. (2007). Blocking of experimental arthritis by cleavage of IgG antibodies in vivo. Arthritis and rheumatism, 56(10), 3253–3260. https://doi.org/10.1002/art.22930

4. Scully, M., Hunt, B. J., Benjamin, S., Liesner, R., Rose, P., Peyvandi, F., Cheung, B., Machin, S. J., & British Committee for Standards in Haematology (2012). Guidelines on the diagnosis and management of thrombotic thrombocytopenic purpura and other thrombotic microangiopathies. British journal of haematology, 158(3), 323–335. https://doi.org/10.1111/j.1365-2141.2012.09167.x