ArticleNature communications2022
Extensive substrate recognition by the streptococcal antibody-degrading enzymes IdeS and EndoS.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 23 citations in OpenAlex.
- Article
- IgA autoantibodies demonstrate a novel mechanism of MuSK myasthenia gravis pathology.Brain : a journal of neurology · 2026Article
- Development and Immunogenicity of a Five-Antigen Strangles Vaccine Based on Equine Ferritin Nanoparticles in Mice.Veterinary sciences · 2026Article
- Identification and Characterization of Novel Human IgG-Degrading Enzymes.Biochemistry · 2026Article
- An atypical F-type ATPase is necessary for the function of the antibody cleavage system MIB-MIP in mycoplasmas.PLoS pathogens · 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
- Depletion and recovery of IgG following treatment with Rozanoliximab and Imlifidase in pigtail macaques.bioRxiv : the preprint server for biology · 2025Article
- Structural and functional characterization of IdeC, a novel IgG-specific protease ofInfection and immunity · 2025Article
- Molecular basis of Fab-dependent IgA antibody recognition by gut-bacterial metallopeptidases.The EMBO journal · 2025Article
- The mechanistic basis for interprotomer deglycosylation of antibodies by corynebacterial IgG-specific endoglycosidases.Nature communications · 2025Article
- Structural insights into the role of the prosegment binding loop in a papain-superfamily cysteine protease from Treponema denticola.Acta crystallographica. Section F, Structural biology communications · 2025Article
- A bipartite bacterial virulence factor targets the complement system and neutrophil activation.The EMBO journal · 2025Article
- The intricate pathogenicity of Group AVirulence · 2024Review
- Article
- Engineered IgM and IgG cleaving enzymes for mitigating antibody neutralization and complement activation in AAV gene transfer.Molecular therapy : the journal of the American Society of Gene Therapy · 2024Article
- Review
- Immunomodulating Enzymes fromMicroorganisms · 2024Review
- Serum immunoglobulin and the threshold of Fc receptor-mediated immune activation.Biochimica et biophysica acta. General subjects · 2023Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymatic cleavage of IgG antibodies is a common strategy used by pathogenic bacteria to ablate immune effector function. The Streptococcus pyogenes bacterium secretes the protease IdeS and the glycosidase EndoS, which specifically catalyse cleavage and deglycosylation of human IgG, respectively. IdeS has received clinical approval for kidney transplantation in hypersensitised individuals, while EndoS has found application in engineering antibody glycosylation. We present crystal structures of both enzymes in complex with their IgG1 Fc substrate, which was achieved using Fc engineering to disfavour preferential Fc crystallisation. The IdeS protease displays extensive Fc recognition and encases the antibody hinge. Conversely, the glycan hydrolase domain in EndoS traps the Fc glycan in a "flipped-out" conformation, while additional recognition of the Fc peptide is driven by the so-called carbohydrate binding module. In this work, we reveal the molecular basis of antibody recognition by bacterial enzymes, providing a template for the development of next-generation enzymes.
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