ArticleThe Biochemical journal2013
EndoS2 is a unique and conserved enzyme of serotype M49 group A Streptococcus that hydrolyses N-linked glycans on IgG and α1-acid glycoprotein.
Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 106 citations in OpenAlex.
- Article
- Glycoengineering of Monoclonal Antibodies with Homogeneous Glycan Isomers with Asymmetric Antennae.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Site-specific antibody labeling via endo-S2 mediated Fc glycan remodeling.Methods in enzymology · 2026Article
- BisectingACS chemical biology · 2025Article
- Technical, preclinical, and clinical developments of Fc-glycan-specific antibody-drug conjugates.RSC medicinal chemistry · 2025Review
- First site-specific conjugation method for native goat IgG antibodies via glycan remodeling at the conserved Fc region.Antibody therapeutics · 2024Article
- Article
- Site-Specific Conjugation of Native Antibody: Transglutaminase-Mediated Modification of a Conserved Glutamine While Maintaining the Primary Sequence and Core Fc Glycan via Trimming with an Endoglycosidase.Bioconjugate chemistry · 2024Article
- Immunomodulating Enzymes fromMicroorganisms · 2024Review
- Simple Routes to Stable Isotope-Coded Native Glycans.Analytical chemistry · 2024Article
- Pathogen-driven degradation of endogenous and therapeutic antibodies during streptococcal infections.Nature communications · 2023Article
- Modulating antibody effector functions by Fc glycoengineering.Biotechnology advances · 2023Review
- Functional assays to screen and select monoclonal antibodies that targetHuman vaccines & immunotherapeutics · 2023Article
- LC-MS/MS-PRM Quantification of IgG Glycoforms Using Stable Isotope Labeled IgG1 Fc Glycopeptide Standard.Journal of proteome research · 2023Article
- Mechanism of antibody-specific deglycosylation and immune evasion by Streptococcal IgG-specific endoglycosidases.Nature communications · 2023Article
- Mass Spectrometry-Based Methods to Determine the Substrate Specificities and Kinetics of N-Linked Glycan Hydrolysis by Endo-β-N-Acetylglucosaminidases.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Extensive substrate recognition by the streptococcal antibody-degrading enzymes IdeS and EndoS.Nature communications · 2022Article
- Site-Specific Chemoenzymatic Conjugation of High-Affinity M6P Glycan Ligands to Antibodies for Targeted Protein Degradation.ACS chemical biology · 2022Article
- Glycoconjugates: Synthesis, Functional Studies, and Therapeutic Developments.Chemical reviews · 2022Review
- Endoglycosidase assay using enzymatically synthesized fluorophore-labeled glycans as substrates to uncover enzyme substrate specificities.Communications biology · 2022Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
Many bacteria have evolved ways to interact with glycosylation functions of the immune system of their hosts. Streptococcus pyogenes [GAS (group A Streptococcus)] secretes the enzyme EndoS that cleaves glycans on human IgG and impairs the effector functions of the antibody. The ndoS gene, encoding EndoS, has, until now, been thought to be conserved throughout the serotypes. However, in the present study, we identify EndoS2, an endoglycosidase in serotype M49 GAS strains. We characterized EndoS2 and the corresponding ndoS2 gene using sequencing, bioinformatics, phylogenetic analysis, recombinant expression and LC-MS analysis of glycosidic activity. This revealed that EndoS2 is present exclusively, and highly conserved, in serotype M49 of GAS and is only 37% identical with EndoS. EndoS2 showed endo-β-N-acetylglucosaminidase activity on all N-linked glycans of IgG and on biantennary and sialylated glycans of AGP (α1-acid glycoprotein). The enzyme was found to act only on native IgG and AGP and to be specific for free biantennary glycans with or without terminal sialylation. GAS M49 expression of EndoS2 was monitored in relation to carbohydrates present in the culture medium and was linked to the presence of sucrose. We conclude that EndoS2 is a unique endoglycosidase in serotype M49 and differs from EndoS of other GAS strains by targeting both IgG and AGP. EndoS2 expands the repertoire of GAS effectors that modify key glycosylated molecules of host defence.
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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.