ArticleInfection and immunity2006
IdeS, a highly specific immunoglobulin G (IgG)-cleaving enzyme from Streptococcus pyogenes, is inhibited by specific IgG antibodies generated during infection.
Article in Infection and immunity, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed.
- Safety, efficacy, and immunogenicity of a novel IgG degrading enzyme (KJ103): results from two randomised, blinded, phase 1 clinical trials.Gene therapy · 2025Trial
- Trial
- Novel assays to assess the prevalence and neutralizing potential of anti-IdeS antibodies in healthy humans.Frontiers in immunology · 2026Article
- Therapeutic IgG- and IgM-specific proteases disarm the acetylcholine receptor autoantibodies that drive myasthenia gravis pathology.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Neutralisation of the Immunoglobulin-Cleaving Activity ofVaccines · 2025Article
- Structural and functional characterization of IdeC, a novel IgG-specific protease ofInfection and immunity · 2025Article
- The intricate pathogenicity of Group AVirulence · 2024Review
- Non-Antibody-Based Binders for the Enrichment of Proteins for Analysis by Mass Spectrometry.Biomolecules · 2021Review
- Signature of Antibody Domain Exchange by Native Mass Spectrometry and Collision-Induced Unfolding.Analytical chemistry · 2018Article
- Article
- Monocyte recruitment by HLA IgG-activated endothelium: the relationship between IgG subclass and FcγRIIa polymorphisms.American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons · 2015Article
- Disease manifestations and pathogenic mechanisms of Group A Streptococcus.Clinical microbiology reviews · 2014Review
- Engineering and characterization of the chimeric antibody that targets the C-terminal telopeptide of the α2 chain of human collagen I: a next step in the quest to reduce localized fibrosis.Connective tissue research · 2013Article
- 3-aminopiperidine-based peptide analogues as the first selective noncovalent inhibitors of the bacterial cysteine protease IdeS.Journal of medicinal chemistry · 2012Article
- Microbial and fungal protease inhibitors--current and potential applications.Applied microbiology and biotechnology · 2012Review
- Streptococcal IdeS and its impact on immune response and inflammation.Journal of innate immunity · 2012Review
- Getting to grips with strangles: an effective multi-component recombinant vaccine for the protection of horses from Streptococcus equi infection.PLoS pathogens · 2009Article
- 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.Infection and immunity · 2008Article
- Article
- Phylogenomic analysis of natural selection pressure in Streptococcus genomes.BMC evolutionary biology · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
IdeS, a recently discovered cysteine proteinase secreted by the important human pathogen Streptococcus pyogenes, interferes with phagocytic killing by specifically cleaving the heavy chain of immunoglobulin G. The fact that the enzyme targets one of the key molecules of the adapted immune response raised the question of whether an antibody response against IdeS could inhibit, i.e., neutralize, enzyme activity. Paired acute- and convalescent-phase serum samples from patients with pharyngotonsillitis (n = 10), bacteremia (n = 7), and erysipelas (n = 4) were analyzed. Antibodies with the ability to neutralize IdeS enzymatic activity were already found in two-thirds of acute-phase sera. However, patients who seroconverted to IdeS, in particular patients with pharyngotonsillitis and erysipelas, developed specific antibodies during convalescence with an increased capability to efficiently neutralize the enzymatic activity of IdeS. Also, the presence of neutralizing antibodies decreased the ability of IdeS to mediate bacterial survival in human immune blood. In patients with bacteremia, several acute-phase sera contained neutralizing antibodies, but no correlation was found to severity or outcome of invasive infections. Still, the fact that the human immune response targets the enzymatic activity of IdeS supports the view that the enzyme plays an important role during streptococcal infection.
Indexed as
Identifiers
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.