{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dixon EV"],"funding":["Medical Research Council"],"pagination":["13876-89"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4022860"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["289(20)"],"pubmed_abstract":["Endoglycosidase S (EndoS) is a glycoside-hydrolase secreted by the bacterium Streptococcus pyogenes. EndoS preferentially hydrolyzes the N-linked glycans from the Fc region of IgG during infection. This hydrolysis impedes Fc functionality and contributes to the immune evasion strategy of S. pyogenes. Here, we investigate the mechanism of human serum IgG deactivation by EndoS. We expressed fragments of IgG1 and demonstrated that EndoS was catalytically active against all of them including the isolated CH2 domain of the Fc domain. Similarly, we sought to investigate which domains within EndoS could contribute to activity. Bioinformatics analysis of the domain organization of EndoS confirmed the previous predictions of a chitinase domain and leucine-rich repeat but also revealed a putative ca"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Fragments of bacterial endoglycosidase s and immunoglobulin g reveal subdomains of each that contribute to deglycosylation."],"pmcid":["PMC4022860"],"funding_grant_id":["MC_PC_12020"],"pubmed_authors":["Baruah K","Krishna B","Dixon EV","Pritchard LK","Harvey DJ","Mattick S","Schnell JR","Higgins MK","Vesiljevic S","Scanlan CN","Claridge JK","Zitzmann N","Yu X","Crispin M"],"additional_accession":[]},"is_claimable":false,"name":"Fragments of bacterial endoglycosidase s and immunoglobulin g reveal subdomains of each that contribute to deglycosylation.","description":"Endoglycosidase S (EndoS) is a glycoside-hydrolase secreted by the bacterium Streptococcus pyogenes. EndoS preferentially hydrolyzes the N-linked glycans from the Fc region of IgG during infection. This hydrolysis impedes Fc functionality and contributes to the immune evasion strategy of S. pyogenes. Here, we investigate the mechanism of human serum IgG deactivation by EndoS. We expressed fragments of IgG1 and demonstrated that EndoS was catalytically active against all of them including the isolated CH2 domain of the Fc domain. Similarly, we sought to investigate which domains within EndoS could contribute to activity. Bioinformatics analysis of the domain organization of EndoS confirmed the previous predictions of a chitinase domain and leucine-rich repeat but also revealed a putative ca","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 May","modification":"2025-04-18T17:57:36.432Z","creation":"2019-03-27T01:28:20Z"},"accession":"S-EPMC4022860","cross_references":{"pubmed":["24668806"],"doi":["10.1074/jbc.M113.532812"]}}