ArticleThe EMBO journal2002
IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 223 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
223 citing papers in PubMed, 475 citations in OpenAlex.
- Endopeptidase Cleavage of Anti-Glomerular Basement Membrane AntibodiesJournal of the American Society of Nephrology : JASN · 2022Trial
- Pre-existing antibody-mediated adverse effects prevent the clinical development of a bacterial anti-inflammatory protein.Disease models & mechanisms · 2020Trial
- Safety, immunogenicity, pharmacokinetics, and efficacy of degradation of anti-HLA antibodies by IdeS (imlifidase) in chronic kidney disease patients.American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons · 2018Trial
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- Group A Streptococcus secreted esterase hydrolyzes platelet-activating factor to impede neutrophil recruitment and facilitate innate immune evasion.PLoS pathogens · 2012Trial
- Article
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- Molecular mechanism of complement interference by Streptococcus pyogenes nuclease A.Communications biology · 2026Article
- Bacterial targeting of the neutrophil inhibitory receptor LILRB3 to evade antibody immunity.Nature communications · 2026Article
- Advancements in Dual-Load Antibody-Drug Conjugates and Challenges with Quality Analysis.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Emerging Role of Gut Microbiota in Modulating Response to Therapies in IBD.Microorganisms · 2026Review
- Identification and Characterization of Novel Human IgG-Degrading Enzymes.Biochemistry · 2026Article
- The Role of the RGD Motif of the IdeC Protein inMicroorganisms · 2026Article
- Polypharmacology of S-1117, an Fc-fused IgG-selective degrading enzyme, for chronic treatment of autoantibody-mediated diseases.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Group A Streptococcal Virulence Factors and Vaccine Development-An Update.Microorganisms · 2026Review
- Depletion and recovery of IgG following treatment with an anti-FcRn antibody and IdeS in pigtail macaques.Clinical and experimental immunology · 2026Article
- Novel assays to assess the prevalence and neutralizing potential of anti-IdeS antibodies in healthy humans.Frontiers in immunology · 2026Article
- Revisiting the streptococcal M protein: modern perspectives on antibody function, host interactions, and therapeutic targeting.Frontiers in immunology · 2026Review
- Integrating natural language processing and genome analysis enables accurate bacterial phenotype prediction.NAR genomics and bioinformatics · 2025Article
163 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Recent work from several laboratories has demonstrated that proteolytic mechanisms significantly contribute to the molecular interplay between Streptococcus pyogenes, an important human pathogen, and its host. Here we describe the identification, purification and characterization of a novel extracellular cysteine proteinase produced by S.pyogenes. This enzyme, designated IdeS for Immunoglobulin G-degrading enzyme of S.pyogenes, is distinct from the well-characterized streptococcal cysteine proteinase, SpeB, and cleaves human IgG in the hinge region with a high degree of specificity. Thus, other human proteins, including immunoglobulins M, A, D and E, are not degraded by IdeS. The enzyme efficiently cleaves IgG antibodies bound to streptococcal surface structures, thereby inhibiting the killing of S.pyogenes by phagocytic cells. This and additional observations on the distribution and expression of the ideS gene indicate that IdeS represents a novel and significant bacterial virulence determinant, and a potential therapeutic target.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.