{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T01:20:36Z","timestamp":1792200036101,"version":"4.4.0"},"reference-count":49,"publisher":"Oxford University Press (OUP)","issue":"5","license":[{"start":{"date-parts":[[2022,2,7]],"date-time":"2022-02-07T00:00:00Z","timestamp":1644192000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["289991887"],"award-info":[{"award-number":["289991887"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["2920\/2\u20132"],"award-info":[{"award-number":["2920\/2\u20132"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["2992\/2\u20132"],"award-info":[{"award-number":["2992\/2\u20132"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["432218849"],"award-info":[{"award-number":["432218849"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["2920\/4-1"],"award-info":[{"award-number":["2920\/4-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2022,4,21]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Rare genetic mutations of the mannosyl-oligosaccharide glucosidase (MOGS) gene affecting the function of the mannosyl-oligosaccharide glucosidase (glucosidase I) are the cause of the congenital disorder of glycosylation IIb (CDG-IIb). Glucosidase I specifically removes the distal \u03b11,2-linked glucose from the protein bound precursor N-glycan Glc3Man9GlcNAc2, which is the initial step of N-glycan maturation. Here, we comparatively analyzed N-glycosylation of the whole serum proteome, serum-derived immunoglobulin G (IgG), transferrin (TF), and \u03b1-1-antitrypsin (AAT) of a female patient who is compound heterozygous for 2 novel missense mutations in the MOGS gene, her heterozygous parents, and a sibling with wildtype genotype by multiplexed capillary gel electrophoresis coupled to laser induced fluorescence detection (xCGE-LIF) at unprecedented depth. Thereby, we detected the CDG-IIb-characteristic non-de-glucosylated N-glycans Glc3Man7-9GlcNAc2 as well as the free tetrasaccharide Glc3-Man in whole serum of the patient but not in the other family members. The N-glycan analysis of the serum proteome further revealed that relative intensities of IgG-specific complex type di-antennary N-glycans with core-fucosylation were considerably reduced in the patient\u2019s serum whereas TF- and AAT-characteristic sialylated di- and tri-antennary N-glycans were increased. This finding reflected the hypogammaglobulinemia diagnosed in the patient. We further detected aberrant oligo-mannose (Glc3Man7GlcNAc2) and hybrid type N-glycans on patient-derived IgGs and we attributed this defective glycosylation to be the reason for an increased IgG clearance. This mechanism can explain the hypogammaglobulinemia that is associated with CDG-IIb.<\/jats:p>","DOI":"10.1093\/glycob\/cwac003","type":"journal-article","created":{"date-parts":[[2022,2,4]],"date-time":"2022-02-04T20:11:20Z","timestamp":1644005480000},"page":"380-390","source":"Crossref","is-referenced-by-count":20,"title":["Serum <i>N<\/i>-glycomics of a novel CDG-IIb patient reveals aberrant IgG glycosylation"],"prefix":"10.1093","volume":"32","author":[{"given":"Julia","family":"Beimdiek","sequence":"first","affiliation":[{"name":"Institute of Clinical Biochemistry, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ren\u00e9","family":"Hennig","sequence":"additional","affiliation":[{"name":"glyXera GmbH, Brenneckestra\u00dfe 20, 39120 Magdeburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert","family":"Burock","sequence":"additional","affiliation":[{"name":"glyXera GmbH, Brenneckestra\u00dfe 20, 39120 Magdeburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Oliver","family":"Puk","sequence":"additional","affiliation":[{"name":"Praxis f\u00fcr Humangenetik, Paul-Ehrlich-Str. 23, 72076 Tuebingen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Saskia","family":"Biskup","sequence":"additional","affiliation":[{"name":"Praxis f\u00fcr Humangenetik, Paul-Ehrlich-Str. 23, 72076 Tuebingen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erdmann","family":"Rapp","sequence":"additional","affiliation":[{"name":"glyXera GmbH, Brenneckestra\u00dfe 20, 39120 Magdeburg, Germany"},{"name":"Max Planck Institute for Dynamics of Complex Technical Systems, Sandtorstra\u00dfe, 39106 Magdeburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anke","family":"Lesinski-Schiedat","sequence":"additional","affiliation":[{"name":"Otorhinolaryngology Department, Head and Neck Surgery, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8468-1223","authenticated-orcid":false,"given":"Falk F R","family":"Buettner","sequence":"additional","affiliation":[{"name":"Institute of Clinical Biochemistry, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anibh M","family":"Das","sequence":"additional","affiliation":[{"name":"Clinic for Pediatric Kidney-, Liver- and Metabolic Diseases, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2022,2,7]]},"reference":[{"key":"2022042117415932700_ref1","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/j.ymgme.2016.12.014","article-title":"Phenotypic and genotypic spectrum of congenital disorders of glycosylation type I and type II","volume":"120","author":"Al Teneiji","year":"2017","journal-title":"Mol Genet Metab"},{"key":"2022042117415932700_ref2","article-title":"Congenital disorders of glycosylation type IIb with MOGS mutations cause early infantile epileptic encephalopathy, dysmorphic features, and hepatic dysfunction","volume":"43","year":"2021","journal-title":"Brain Dev"},{"key":"2022042117415932700_ref3","volume-title":"Ganong's review of medical physiology","author":"Barrett","edition":"23rd"},{"key":"2022042117415932700_ref4","doi-asserted-by":"crossref","first-page":"3029","DOI":"10.1074\/mcp.M114.039537","article-title":"Immunoglobulin G (IgG) fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes","volume":"13","author":"Bondt","year":"2014","journal-title":"Mol Cell Proteomics: MCP"},{"key":"2022042117415932700_ref5","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1373\/clinchem.2003.021568","article-title":"Diagnosis of congenital disorders of glycosylation by capillary zone electrophoresis of serum transferrin","volume":"50","author":"Carchon","year":"2004","journal-title":"Clin Chem"},{"key":"2022042117415932700_ref6","doi-asserted-by":"crossref","first-page":"257","DOI":"10.3851\/IMP2907","article-title":"Viral resistance of MOGS-CDG patients implies a broad-spectrum strategy against acute virus infections","volume":"20","author":"Chang","year":"2015","journal-title":"Antivir Ther"},{"key":"2022042117415932700_ref7","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1007\/s10719-015-9626-2","article-title":"Human plasma protein N-glycosylation","volume":"33","author":"Clerc","year":"2016","journal-title":"Glycoconj 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