Literature for peptidase C66.001: IdeS peptidase

Summary Alignment Sequences Sequence features Distribution Structure Literature Substrates

(Topics flags: S Structure, P Specificity, I Inhibitor, E Expression, U Therapeutic, V Review. To select only the references relevant to a single topic, click the link above. See explanation.)

    2025
  1. Beaudrey,T., Apithy,M.J., Olagne,J., Lemonnier,L., Perrin,P., Vargas,G.G., Jahn,I., Radosavljevic,M., Bahram,S., Carapito,R. and Caillard,S.
    Evolution of anti-MICA antibodies after imlifidase infusion for a high immunological risk kidney transplantation
    Hum Immunol (2025) 86, 111213-111213. PubMed  Europe PubMed DOI
  2. Cao,M., Katial,R., Liu,Y., Lu,X., Gu,Q., Chen,C., Liu,K., Zhu,Z., Marshall,M.R., Yu,Y. and Wang,Z.
    Safety, efficacy, and immunogenicity of a novel IgG degrading enzyme (KJ103): results from two randomised, blinded, phase 1 clinical trials
    Gene Ther (2025) PubMed  Europe PubMed DOI
  3. 2024
  4. Daventure,V., Bou-Jaoudeh,M., Hannachi,E., Reyes-Ruiz,A., Trecco,A., Delignat,S., Lacroix-Desmazes,S. and Deligne,C.
    Half-Life Extension of the IgG-Degrading Enzyme (IdeS) Using Fc-Fusion Technology
    Eur J Immunol (2024) , e202451264-e202451264. PubMed  Europe PubMed DOI
  5. Vo,A., Ammerman,N. and Jordan,S.C.
    New therapies for highly sensitized patients on the waiting list
    Kidney360 (2024) 5, 1207-1225. PubMed  Europe PubMed DOI
  6. 2023
  7. Boksha,I.S., Lunin,V.G., Danilova,T.A., Poponova,M.S., Polyakov,N.B., Lyashchuk,A.M., Konstantinova,S.V., Galushkina,Z.M. and Ustenko,E.V.
    Recombinant Endopeptidases IdeS and IdeZ and Their Potential Application
    Biochemistry (Mosc) (2023) 88, 731-740. PubMed  Europe PubMed DOI
  8. Frick,I.M., Happonen,L., Wrighton,S., Nordenfelt,P. and Bjorck,L.
    IdeS, a secreted proteinase of Streptococcus pyogenes, is bound to a nuclease at the bacterial surface where it inactivates opsonizing IgG antibodies
    J Biol Chem (2023) 299, 105345-105345. PubMed  Europe PubMed DOI  PMC  EPMC
  9. Lindh,T., Collin,M., Lood,R. and Carlquist,M.
    Expression of the Bacterial Enzyme IdeS Using a GFP Fusion in the Yeast Saccharomyces cerevisiae
    Methods Mol Biol (2023) 2674, 131-146. PubMed  Europe PubMed DOI
  10. Sethi,S. and Jordan,S.C.
    Novel therapies for treatment of antibody-mediated rejection of the kidney
    Curr Opin Organ Transplant (2023) 28, 29-35. PubMed  Europe PubMed DOI  V
  11. 2022
  12. Lynch,D.R., Stringham,E.N., Zhang,B., Balbin-Cuesta,G., Curtis,B.R., Palumbo,J.S., Greineder,C.F. and Tourdot,B.E.
    Anchoring IgG-degrading enzymes to the surface of platelets selectively neutralizes antiplatelet antibodies
    Blood Adv (2022) 6, 4645-4656. PubMed  Europe PubMed DOI
  13. McClain,A., Zhang,Y., Yin,Y., Wang,Q., Hwang,L.Y., Gu,Y., Beckman,J. and Ludwig,R.
    Using Digestion by IdeS Protease to Improve Quantification of Degradants in Monoclonal Antibodies by Non-Reducing Capillary Gel Electrophoresis
    Anal Chem (2022) 94, 17388-17395. PubMed  Europe PubMed DOI  PMC  EPMC
  14. 2020
  15. Al-Salama,Z.T.
    Imlifidase: First Approval
    Drugs (2020) 80, 1859-1864. PubMed  Europe PubMed DOI
  16. Rosenstein,S., Vaisman-Mentesh,A., Levy,L., Kigel,A., Dror,Y. and Wine,Y.
    Production of F(ab')2 from monoclonal and polyclonal antibodies
    Curr Protoc Mol Biol (2020) 131, e119-e119. PubMed  Europe PubMed DOI  E
  17. 2019
  18. Kizlik-Masson,C., Deveuve,Q., Zhou,Y., Vayne,C., Thibault,G., McKenzie,S.E., Pouplard,C., Loyau,S., Gruel,Y. and Rollin,J.
    Cleavage of anti-PF4/heparin IgG by a bacterial protease and potential benefit in heparin-induced thrombocytopenia
    Blood (2019) 133, 2427-2435. PubMed  Europe PubMed DOI
  19. Rafat,C. and Luque,Y.
    IdeS in anti-glomerular basement membrane disease: is this the new deal?
    Kidney Int (2019) 96, 1068-1070. PubMed  Europe PubMed DOI  U
  20. Soveri,I., Molne,J., Uhlin,F., Nilsson,T., Kjellman,C., Sonesson,E. and Segelmark,M.
    The IgG-degrading enzyme of Streptococcus pyogenes causes rapid clearance of anti-glomerular basement membrane antibodies in patients with refractory anti-glomerular basement membrane disease
    Kidney Int (2019) 96, 1234-1238. PubMed  Europe PubMed DOI  U
  21. Stubbs,M.J., Thomas,M., Vendramin,C., Sonesson,E., Kjellman,C., Jarnum,S., Stenberg,Y., Elfving,C. and Scully,M.
    Administration of immunoglobulin G-degrading enzyme of Streptococcus pyogenes (IdeS) for persistent anti-ADAMTS13 antibodies in patients with thrombotic thrombocytopenic purpura in clinical remission
    Br J Haematol (2019) 186, 137-140. PubMed  Europe PubMed DOI  U
  22. 2018
  23. Burner,J.D. and Goldfinger,D.
    Potential use of IgG endopeptidase in the management of platelet refractoriness due to HLA alloimmunization
    Transfus Apher Sci (2018) 57, 409-410. PubMed  Europe PubMed DOI
  24. Huang,E. and Jordan,S.C.
    Immunoglobulin G-degrading enzyme of Streptococcus pyogenes (IdeS), desensitization, and the kidney allocation system: complementary approaches to increase transplantation in highly HLA sensitized patients
    Clin J Am Soc Nephrol (2018) 13, 799-801. PubMed  Europe PubMed DOI  PMC  EPMC
  25. Karlsson,C.A.Q., Jarnum,S., Winstedt,L., Kjellman,C., Bjorck,L., Linder,A. and Malmstrom,J.A.
    Streptococcus pyogenes infection and the human proteome with a special focus on the immunoglobulin G-cleaving enzyme IdeS
    Mol Cell Proteomics (2018) 17, 1097-1111. PubMed  Europe PubMed DOI  PMC  EPMC
  26. Lonze,B.E., Tatapudi,V.S., Weldon,E.P., Min,E.S., Ali,N.M., Deterville,C.L., Gelb,B.E., Benstein,J.A., Dagher,N.N., Wu,M. and Montgomery,R.A.
    IdeS (Imlifidase): a novel agent that cleaves human IgG and permits successful kidney transplantation across high-strength donor-specific antibody
    Ann Surg (2018) 268, 488-496. PubMed  Europe PubMed DOI  U
  27. Montgomery,R.A., Lonze,B.E. and Tatapudi,V.S.
    IgG degrading enzyme of Streptococcus pyogenes: an exciting new development in desensitization therapy
    Transplantation (2018) 102, 2-4. PubMed  Europe PubMed DOI  U
  28. 2017
  29. Collin,M. and Bjorck,L.
    Toward clinical use of the IgG specific enzymes IdeS and EndoS against antibody-mediated diseases
    Methods Mol Biol (2017) 1535, 339-351. PubMed  Europe PubMed DOI  U
  30. Faid,V., Leblanc,Y., Bihoreau,N. and Chevreux,G.
    Middle-up analysis of monoclonal antibodies after combined IgdE and IdeS hinge proteolysis: investigation of free sulfhydryls
    J Pharm Biomed Anal (2017) 149, 541-546. PubMed  Europe PubMed DOI
  31. Falkenburg,W.J., van Schaardenburg,D., Ooijevaar-de Heer,P., Tsang-A-Sjoe,M.W., Bultink,I.E., Voskuyl,A.E., Bentlage,A.E., Vidarsson,G., Wolbink,G. and Rispens,T.
    Anti-hinge antibodies recognize IgG subclass- and protease-restricted neoepitopes
    J Immunol (2017) 198, 82-93. PubMed  Europe PubMed DOI
  32. Ingelfinger,J.R.
    A bacterial IgG-degrading enzyme to unhinge antibodies
    N Engl J Med (2017) 377, 487-489. PubMed  Europe PubMed DOI
  33. Jarnum,S., Runstrom,A., Bockermann,R., Winstedt,L., Crispin,M. and Kjellman,C.
    Enzymatic inactivation of endogenous IgG by IdeS enhances therapeutic antibody efficacy
    Mol Cancer Ther (2017) 16, 1887-1897. PubMed  Europe PubMed DOI  U
  34. Jordan,S.C., Lorant,T., Choi,J., Kjellman,C., Winstedt,L., Bengtsson,M., Zhang,X., Eich,T., Toyoda,M., Eriksson,B.M., Ge,S., Peng,A., Jarnum,S., Wood,K.J., Lundgren,T., Wennberg,L., Backman,L., Larsson,E., Villicana,R., Kahwaji,J., Louie,S., Kang,A., Haas,M., Nast,C., Vo,A. and Tufveson,G.
    IgG endopeptidase in highly sensitized patients undergoing transplantation
    N Engl J Med (2017) 377, 442-453. PubMed  Europe PubMed DOI  U
  35. Rungelrath,V., Wohlsein,J.C., Siebert,U., Stott,J., Prenger-Berninghoff,E., VonPawel-Rammingen,U., Valentin-Weigand,P., Baums,C.G. and Seele,J.
    Identification of a novel host-specific IgG protease in Streptococcus phocae subsp. phocae
    Vet Microbiol (2017) 201, 42-48. PubMed  Europe PubMed DOI  I
  36. Sjogren,J., Andersson,L., Mejare,M. and Olsson,F.
    Generating and purifying Fab fragments from human and mouse IgG using the bacterial enzymes IdeS, SpeB and Kgp
    Methods Mol Biol (2017) 1535, 319-329. PubMed  Europe PubMed DOI
  37. Wang,Y., Shi,Q., Lv,H., Hu,M., Wang,W., Wang,Q., Qiao,B., Zhang,G., Lv,Z., Kjellman,C., Jarnum,S., Winstedt,L., Zhang,Y., Wen,J., Hao,Y. and Yuki,N.
    IgG-degrading enzyme of Streptococcus pyogenes (IdeS) prevents disease progression and facilitates improvement in a rabbit model of Guillain-Barre syndrome
    Exp Neurol (2017) 291, 134-140. PubMed  Europe PubMed DOI  U
  38. 2016
  39. Kirley,T.L., Greis,K.D. and Norman,A.B.
    Structural characterization of expressed monoclonal antibodies by single sample mass spectral analysis after IdeS proteolysis
    Biochem Biophys Res Commun (2016) 477, 363-368. PubMed  Europe PubMed DOI
  40. Novarra,S., Grinberg,L., Rickert,K.W., Barnes,A., Wilson,S. and Baca,M.
    A hingeless Fc fusion system for site-specific cleavage by IdeS
    MAbs (2016) 8, 1118-1125. PubMed  Europe PubMed DOI
  41. 2015
  42. Jarnum,S., Bockermann,R., Runstrom,A., Winstedt,L. and Kjellman,C.
    The bacterial enzyme IdeS cleaves the IgG-type of B cell receptor (BCR), abolishes BCR-mediated cell signaling, and inhibits memory B cell activation
    J Immunol (2015) 195, 5592-5601. PubMed  Europe PubMed DOI  PMC  EPMC
  43. Persson,H., Soderberg,J.J., Vindebro,R., Johansson,B.P. and von Pawel-Rammingen,U.
    Proteolytic processing of the streptococcal IgG endopeptidase IdeS modulates the functional properties of the enzyme and results in reduced immunorecognition
    Mol Immunol (2015) 68, 176-184. PubMed  Europe PubMed DOI
  44. Postnikov,P., Krotov,G., Mesonzhnik,N., Efimova,Y. and Rodchenkov,G.
    Fc-fragment removal allows the EPO-Fc fusion protein to be detected in blood samples by IEF-PAGE
    Drug Test Anal (2015) 7, 999-1008. PubMed  Europe PubMed DOI
  45. Winstedt,L., Jarnum,S., Nordahl,E.A., Olsson,A., Runstrom,A., Bockermann,R., Karlsson,C., Malmstrom,J., Palmgren,G.S., Malmqvist,U., Bjorck,L. and Kjellman,C.
    Complete removal of extracellular IgG antibodies in a randomized dose-escalation phase I Study with the bacterial enzyme IdeS - a novel therapeutic opportunity
    PLoS ONE (2015) 10, e0132011-e0132011. PubMed  Europe PubMed DOI  PMC  EPMC  U
  46. 2014
  47. An,Y., Zhang,Y., Mueller,H.M., Shameem,M. and Chen,X.
    A new tool for monoclonal antibody analysis: application of IdeS proteolysis in IgG domain-specific characterization
    MAbs (2014) 6, 879-893. PubMed  Europe PubMed DOI
  48. Brezski,R.J., Kinder,M., Grugan,K.D., Soring,K.L., Carton,J., Greenplate,A.R., Petley,T., Capaldi,D., Brosnan,K., Emmell,E., Watson,S. and Jordan,R.E.
    A monoclonal antibody against hinge-cleaved IgG restores effector function to proteolytically-inactivated IgGs in vitro and in vivo
    MAbs (2014) 6, 1265-1273. PubMed  Europe PubMed DOI
  49. Leblanc,Y., Romanin,M., Bihoreau,N. and Chevreux,G.
    LC-MS analysis of polyclonal IgGs using IdeS enzymatic proteolysis for oxidation monitoring
    J Chromatogr B Analyt Technol Biomed Life Sci (2014) 961, 1-4. PubMed  Europe PubMed DOI
  50. Wagner-Rousset,E., Janin-Bussat,M.-C., Colas,O., Excoffier,M., Ayoub,D., Haeuw,J.-F., Rilatt,I., Perez,M., Corvaia,N. and Beck,A.
    Antibody-drug conjugate model fast characterization by LC-MS following IdeS proteolytic digestion
    MAbs (2014) 6, 273-285. PubMed  Europe PubMed DOI
  51. 2013
  52. Janin-Bussat,M.C., Tonini,L., Huillet,C., Colas,O., Klinguer-Hamour,C., Corvaia,N. and Beck,A.
    Cetuximab Fab and Fc N-glycan fast characterization using IdeS digestion and liquid chromatography coupled to electrospray ionization mass spectrometry
    Methods Mol Biol (2013) 988, 93-113. PubMed  Europe PubMed DOI
  53. Okumura,C.Y., Anderson,E.L., Dohrmann,S., Tran,D.N., Olson,J., von Pawel-Rammingen,U. and Nizet,V.
    IgG protease Mac/IdeS is not essential for phagocyte resistance or mouse virulence of M1T1 group A Streptococcus
    MBio (2013) 4, e00499-13. PubMed  Europe PubMed DOI  PMC  EPMC
  54. Vindebro,R., Spoerry,C. and von Pawel-Rammingen,U.
    Rapid IgG heavy chain cleavage by the streptococcal IgG endopeptidase IdeS is mediated by IdeS monomers and is not due to enzyme dimerization
    FEBS Lett (2013) 587, 1818-1822. PubMed  Europe PubMed DOI
  55. 2012
  56. Berggren,K., Vindebro,R., Bergstrom,C., Spoerry,C., Persson,H., Fex,T., Kihlberg,J., von Pawel-Rammingen,U. and Luthman,K.
    3-Aminopiperidine-based peptide analogues as the first selective noncovalent inhibitors of the bacterial cysteine protease IdeS
    J Med Chem (2012) 55, 2549-2560. PubMed  Europe PubMed DOI  I
  57. Pawel-Rammingen,U.
    IdeS peptidase
    [ISSN:978-0-12-407743-0] (2012) 3, 2175-2178. DOI
  58. 2011
  59. Chevreux,G., Tilly,N. and Bihoreau,N.
    Fast analysis of recombinant monoclonal antibodies using IdeS proteolytic digestion and electrospray mass spectrometry
    Anal Biochem (2011) 415, 212-214. PubMed  Europe PubMed DOI
  60. Su,Y.F., Chuang,W.J., Wang,S.M., Chen,W.Y., Chiang-Ni,C., Lin,Y.S., Wu,J.J. and Liu,C.C.
    The deficient cleavage of M protein-bound IgG by IdeS: insight into the escape of Streptococcus pyogenes from antibody-mediated immunity
    Mol Immunol (2011) 49, 134-142. PubMed  Europe PubMed DOI
  61. 2010
  62. Yang,R., Otten,M.A., Hellmark,T., Collin,M., Bjorck,L., Zhao,M.H., Daha,M.R. and Segelmark,M.
    Successful treatment of experimental glomerulonephritis with IdeS and EndoS, IgG-degrading streptococcal enzymes
    Nephrol Dial Transplant (2010) 25, 2479-2486. PubMed  Europe PubMed DOI  U
  63. 2009
  64. Berggren,K., Johansson,B., Fex,T., Kihlberg,J., Bjorck,L. and Luthman,K.
    Synthesis and biological evaluation of reversible inhibitors of IdeS, a bacterial cysteine protease and virulence determinant
    Bioorg Med Chem (2009) 17, 3463-3470. PubMed  Europe PubMed DOI  I
  65. Radaev,S., Agniswamy,J. and Sun,P.D.
    A case of structure determination using pseudosymmetry
    Acta Crystallogr D Biol Crystallogr (2009) 65, 1334-1340. PubMed  Europe PubMed DOI  PMC  EPMC  S
  66. 2008
  67. Johansson,B.P., Shannon,O. and Bjorck,L.
    IdeS: a bacterial proteolytic enzyme with therapeutic potential
    PLoS ONE (2008) 3, e1692-e1692. PubMed  Europe PubMed DOI  PMC  EPMC  U
  68. Nandakumar,K.S. and Holmdahl,R.
    Therapeutic cleavage of IgG: new avenues for treating inflammation
    Trends Immunol (2008) 29, 173-178. PubMed  Europe PubMed DOI  U
  69. Shen,A. and Bogyo,M.
    Friend or foe? Turning a host defense protein into a pathogen's accomplice
    Chem Biol (2008) 15, 879-880. PubMed  Europe PubMed DOI
  70. Soderberg,J.J. and von Pawel-Rammingen,U.
    The streptococcal protease IdeS modulates bacterial IgGFc binding and generates 1/2Fc fragments with the ability to prime polymorphonuclear leucocytes
    Mol Immunol (2008) 45, 3347-3353. PubMed  Europe PubMed DOI
  71. Soderberg,J.J., Engstrom,P. and von Pawel-Rammingen,U.
    The intrinsic immunoglobulin G endopeptidase activity of streptococcal Mac-2 proteins implies a unique role for the enzymatically impaired Mac-2 protein of M28 serotype strains
    Infect Immun (2008) 76, 2183-2188. PubMed  Europe PubMed DOI  PMC  EPMC
  72. Vincents,B., Vindebro,R., Abrahamson,M. and von Pawel-Rammingen,U.
    The human protease inhibitor cystatin C is an activating cofactor for the streptococcal cysteine protease IdeS
    Chem Biol (2008) 15, 960-968. PubMed  Europe PubMed DOI
  73. 2007
  74. Hess,J.L., Porsch,E.A., Shertz,C.A. and Boyle,M.D.
    Immunoglobulin cleavage by the streptococcal cysteine protease IdeS can be detected using protein G capture and mass spectrometry
    J Microbiol Methods (2007) 70, 284-291. PubMed  Europe PubMed DOI  PMC  EPMC
  75. Nandakumar,K.S., Johansson,B.P., Bjorck,L. and Holmdahl,R.
    Blocking of experimental arthritis by cleavage of IgG antibodies in vivo
    Arthritis Rheum (2007) 56, 3253-3260. PubMed  Europe PubMed DOI
  76. 2006
  77. Agniswamy,J., Nagiec,M.J., Liu,M., Schuck,P., Musser,J.M. and Sun,P.D.
    Crystal structure of group A Streptococcus Mac-1: insight into dimer-mediated specificity for recognition of human IgG
    Structure (2006) 14, 225-235. PubMed  Europe PubMed DOI  S
  78. Akesson,P., Moritz,L., Truedsson,M., Christensson,B. and von Pawel-Rammingen,U.
    IdeS, a highly specific immunoglobulin G (IgG)-cleaving enzyme from Streptococcus pyogenes, is inhibited by specific IgG antibodies generated during infection
    Infect Immun (2006) 74, 497-503. PubMed  Europe PubMed DOI  PMC  EPMC
  79. 2004
  80. Agniswamy,J., Lei,B., Musser,J.M. and Sun,P.D.
    Insight of host immune evasion mediated by two variants of group a Streptococcus Mac protein
    J Biol Chem (2004) 279, 52789-52796. PubMed  Europe PubMed DOI
  81. [YEAR:14-12-2004]Vincents,B., von Pawel-Rammingen,U., Bjorck,L. and Abrahamson,M.
    Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite binding
    Biochemistry (14-12-2004) 43, 15540-15549. PubMed  Europe PubMed DOI  P
  82. [YEAR:14-12-2004]Wenig,K., Chatwell,L., von Pawel-Rammingen,U., Bjorck,L., Huber,R. and Sondermann,P.
    Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG
    Proc Natl Acad Sci U S A (14-12-2004) 101, 17371-17376. PubMed  Europe PubMed DOI  PMC  EPMC  S
  83. 2003
  84. Lei,B., Liu,M., Meyers,E.G., Manning,H.M., Nagiec,M.J. and Musser,J.M.
    Histidine and aspartic acid residues important for immunoglobulin G endopeptidase activity of the group A Streptococcus opsonophagocytosis-inhibiting Mac protein
    Infect Immun (2003) 71, 2881-2884. PubMed  Europe PubMed DOI  PMC  EPMC
  85. von Pawel-Rammingen,U. and Bjorck,L.
    IdeS and SpeB: immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes
    Curr Opin Microbiol (2003) 6, 50-55. PubMed  Europe PubMed DOI
  86. 2002
  87. Lei,B., DeLeo,F.R., Reid,S.D., Voyich,J.M., Magoun,L., Liu,M., Braughton,K.R., Ricklefs,S., Hoe,N.P., Cole,R.L., Leong,J.M. and Musser,J.M.
    Opsonophagocytosis-inhibiting Mac protein of Group A Streptococcus: identification and characteristics of two genetic complexes
    Infect Immun (2002) 70, 6880-6890. PubMed  Europe PubMed DOI  PMC  EPMC
  88. [YEAR:1-4-2002]von Pawel-Rammingen,U., Johansson,B.P. and Bjorck,L.
    IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G
    EMBO J (1-4-2002) 21, 1607-1615. PubMed  Europe PubMed DOI  PMC  EPMC
  89. 2001
  90. Lei,B., DeLeo,F.R., Hoe,N.P., Graham,M.R., Mackie,S.M., Cole,R.L., Liu,M., Hill,H.R., Low,D.E., Federle,M.J., Scott,J.R. and Musser,J.M.
    Evasion of human innate and acquired immunity by a bacterial homolog of CD11b that inhibits opsonophagocytosis
    Nat Med (2001) 7, 1298-1305. PubMed  Europe PubMed DOI
  91. 2000
  92. Lei,B., Mackie,S., Lukomski,S. and Musser,J.M.
    Identification and immunogenicity of group A Streptococcus culture supernatant proteins
    Infect Immun (2000) 68, 6807-6818. PubMed  Europe PubMed DOI  PMC  EPMC