{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T17:48:03Z","timestamp":1791308883260,"version":"4.3.1"},"reference-count":99,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,10,1]],"date-time":"2018-10-01T00:00:00Z","timestamp":1538352000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,12,24]],"date-time":"2018-12-24T00:00:00Z","timestamp":1545609600000},"content-version":"vor","delay-in-days":84,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"content-domain":{"domain":["clinicalkey.jp","clinicalkey.com","clinicalkey.es","clinicalkey.com.au","clinicalkey.fr","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Seminars in Immunology"],"published-print":{"date-parts":[[2018,10]]},"DOI":"10.1016\/j.smim.2018.05.003","type":"journal-article","created":{"date-parts":[[2018,6,11]],"date-time":"2018-06-11T15:43:31Z","timestamp":1528731811000},"page":"102-110","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":180,"special_numbering":"C","title":["Antibody glycosylation in inflammation, disease and vaccination"],"prefix":"10.1016","volume":"39","author":[{"given":"Galit","family":"Alter","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tom H.M.","family":"Ottenhoff","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Simone A.","family":"Joosten","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.smim.2018.05.003_bib0005","doi-asserted-by":"crossref","first-page":"33","DOI":"10.3389\/fimmu.2015.00033","article-title":"The evolution and development of the antibody repertoire","volume":"6","author":"Schroeder","year":"2015","journal-title":"Front. Immunol."},{"key":"10.1016\/j.smim.2018.05.003_bib0010","doi-asserted-by":"crossref","first-page":"E16","DOI":"10.1371\/journal.pbio.0000016","article-title":"V(D)J recombination and the evolution of the adaptive immune system","volume":"1","author":"Market","year":"2003","journal-title":"PLoS Biol."},{"key":"10.1016\/j.smim.2018.05.003_bib0015","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.immuni.2017.07.009","article-title":"Fcgamma receptor function and the design of vaccination strategies","volume":"47","author":"Bournazos","year":"2017","journal-title":"Immunity"},{"key":"10.1016\/j.smim.2018.05.003_bib0020","first-page":"2183","article-title":"On the development of immunity to diphtheria and tetanus in animals","volume":"90","author":"Behring","year":"1965","journal-title":"Dtsch. Med. Wochenschr."},{"key":"10.1016\/j.smim.2018.05.003_bib0025","doi-asserted-by":"crossref","first-page":"S41","DOI":"10.1016\/j.jaci.2009.09.046","article-title":"Structure and function of immunoglobulins","volume":"125","author":"Schroeder","year":"2010","journal-title":"J. Allergy Clin. Immunol."},{"key":"10.1016\/j.smim.2018.05.003_bib0030","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1126\/science.3317826","article-title":"Evolutionary and somatic selection of the antibody repertoire in the mouse","volume":"238","author":"Rajewsky","year":"1987","journal-title":"Science"},{"key":"10.1016\/j.smim.2018.05.003_bib0035","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/0092-8674(95)90227-9","article-title":"Somatic hypermutation: how many mechanisms diversify V region sequences?","volume":"83","author":"Maizels","year":"1995","journal-title":"Cell"},{"key":"10.1016\/j.smim.2018.05.003_bib0040","doi-asserted-by":"crossref","first-page":"5370","DOI":"10.4049\/jimmunol.1401849","article-title":"IgH chain class switch recombination: mechanism and regulation","volume":"193","author":"Stavnezer","year":"2014","journal-title":"J. Immunol."},{"key":"10.1016\/j.smim.2018.05.003_bib0045","doi-asserted-by":"crossref","first-page":"1510","DOI":"10.1126\/science.1118948","article-title":"Divergent immunoglobulin g subclass activity through selective Fc receptor binding","volume":"310","author":"Nimmerjahn","year":"2005","journal-title":"Science"},{"key":"10.1016\/j.smim.2018.05.003_bib0050","doi-asserted-by":"crossref","first-page":"520","DOI":"10.3389\/fimmu.2014.00520","article-title":"IgG subclasses and allotypes: from structure to effector functions","volume":"5","author":"Vidarsson","year":"2014","journal-title":"Front. Immunol."},{"key":"10.1016\/j.smim.2018.05.003_bib0055","doi-asserted-by":"crossref","first-page":"1369","DOI":"10.1016\/0161-5890(91)90039-M","article-title":"Diversification of the IgG molecule by oligosaccharides","volume":"28","author":"Rudd","year":"1991","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.smim.2018.05.003_bib0060","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1038\/nrd2804","article-title":"Glycosylation as a strategy to improve antibody-based therapeutics","volume":"8","author":"Jefferis","year":"2009","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.smim.2018.05.003_bib0065","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.abb.2012.03.021","article-title":"Isotype and glycoform selection for antibody therapeutics","volume":"526","author":"Jefferis","year":"2012","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.smim.2018.05.003_bib0070","first-page":"43","article-title":"Biological importance of glycosylation","volume":"96","author":"Dwek","year":"1998","journal-title":"Dev. Biol. Stand."},{"key":"10.1016\/j.smim.2018.05.003_bib0075","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1038\/nrrheum.2017.146","article-title":"Differential antibody glycosylation in autoimmunity: sweet biomarker or modulator of disease activity?","volume":"13","author":"Seeling","year":"2017","journal-title":"Nat. Rev. Rheumatol."},{"key":"10.1016\/j.smim.2018.05.003_bib0080","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1038\/nri3401","article-title":"Intravenous immunoglobulin therapy: how does IgG modulate the immune system?","volume":"13","author":"Schwab","year":"2013","journal-title":"Nat. Rev. Immunol."},{"issue":"M111","key":"10.1016\/j.smim.2018.05.003_bib0085","first-page":"010090","article-title":"High throughput isolation and glycosylation analysis of IgG-variability and heritability of the IgG glycome in three isolated human populations","volume":"10","author":"Pucic","year":"2011","journal-title":"Mol. Cell Proteom."},{"key":"10.1016\/j.smim.2018.05.003_bib0090","article-title":"Antigen-specific antibody glycosylation is regulated via vaccination","volume":"12","author":"Mahan","year":"2016","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.smim.2018.05.003_bib0095","doi-asserted-by":"crossref","first-page":"4522","DOI":"10.1021\/pr400589m","article-title":"Association between galactosylation of immunoglobulin G and improvement of rheumatoid arthritis during pregnancy is independent of sialylation","volume":"12","author":"Bondt","year":"2013","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.smim.2018.05.003_bib0100","doi-asserted-by":"crossref","first-page":"1853","DOI":"10.1021\/acs.jproteome.6b00038","article-title":"Changes in healthy human IgG Fc-glycosylation after birth and during early childhood","volume":"15","author":"de Haan","year":"2016","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.smim.2018.05.003_bib0105","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1016\/j.arr.2012.02.002","article-title":"N-glycomic biomarkers of biological aging and longevity: a link with inflammaging","volume":"12","author":"Dall","year":"2013","journal-title":"Ageing Res. Rev."},{"key":"10.1016\/j.smim.2018.05.003_bib0110","doi-asserted-by":"crossref","first-page":"25957","DOI":"10.1038\/srep25957","article-title":"Disease-specific IgG Fc N-glycosylation as personalized biomarkers to differentiate gastric cancer from benign gastric diseases","volume":"6","author":"Zhang","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.smim.2018.05.003_bib0115","doi-asserted-by":"crossref","first-page":"4070","DOI":"10.1002\/pmic.200700289","article-title":"Glycosylation profiling of immunoglobulin G (IgG) subclasses from human serum","volume":"7","author":"Wuhrer","year":"2007","journal-title":"Proteomics"},{"key":"10.1016\/j.smim.2018.05.003_bib0120","doi-asserted-by":"crossref","first-page":"12325","DOI":"10.1038\/s41598-017-12495-0","article-title":"Subclass-specific IgG glycosylation is associated with markers of inflammation and metabolic health","volume":"7","author":"Plomp","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.smim.2018.05.003_bib0125","doi-asserted-by":"crossref","first-page":"742","DOI":"10.1016\/j.autrev.2014.02.005","article-title":"Impact of autoantibody glycosylation in autoimmune diseases","volume":"13","author":"Goulabchand","year":"2014","journal-title":"Autoimmun. Rev."},{"key":"10.1016\/j.smim.2018.05.003_bib0130","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1016\/j.it.2017.02.004","article-title":"The immunoregulatory roles of antibody glycosylation","volume":"38","author":"Jennewein","year":"2017","journal-title":"Trends Immunol."},{"key":"10.1016\/j.smim.2018.05.003_bib0135","doi-asserted-by":"crossref","DOI":"10.3390\/ijms18122632","article-title":"Aberrant N-glycosylation profile of serum immunoglobulins is a diagnostic biomarker of Urothelial Carcinomas","volume":"18","author":"Tanaka","year":"2017","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.smim.2018.05.003_bib0140","doi-asserted-by":"crossref","first-page":"28098","DOI":"10.1038\/srep28098","article-title":"Glycosylation of plasma IgG in colorectal cancer prognosis","volume":"6","author":"Theodoratou","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.smim.2018.05.003_bib0145","first-page":"1237","article-title":"Inflammatory bowel disease associates with proinflammatory potential of the immunoglobulin G glycome","volume":"21","author":"Trbojevic Akmacic","year":"2015","journal-title":"Inflamm. Bowel Dis."},{"key":"10.1016\/j.smim.2018.05.003_bib0150","unstructured":"C. R. Varki A, Esko JD, Essentials of Glycobiology., (Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2015-2017., 2015-2017), vol. 3rd Edition."},{"key":"10.1016\/j.smim.2018.05.003_bib0155","article-title":"Correction: antigen-specific antibody glycosylation Is regulated via vaccination","volume":"12","author":"Mahan","year":"2016","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.smim.2018.05.003_bib0160","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.M110.004655","article-title":"Fc-glycosylation of IgG1 is modulated by B-cell stimuli","volume":"10","author":"Wang","year":"2011","journal-title":"Mol. Cell Proteom."},{"key":"10.1016\/j.smim.2018.05.003_bib0165","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.M111.014563","article-title":"Changes in antigen-specific IgG1 Fc N-glycosylation upon influenza and tetanus vaccination","volume":"11","author":"Selman","year":"2012","journal-title":"Mol. Cell Proteom."},{"key":"10.1016\/j.smim.2018.05.003_bib0170","doi-asserted-by":"crossref","first-page":"2070","DOI":"10.1002\/eji.201747208","article-title":"IgG subclass and vaccination stimulus determine changes in antigen specific antibody glycosylation in mice","volume":"47","author":"Kao","year":"2017","journal-title":"Eur. J. Immunol."},{"key":"10.1016\/j.smim.2018.05.003_bib0175","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.4049\/jimmunol.1502136","article-title":"The emerging importance of IgG fab glycosylation in immunity","volume":"196","author":"van de Bovenkamp","year":"2016","journal-title":"J. Immunol."},{"key":"10.1016\/j.smim.2018.05.003_bib0180","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.jaut.2013.09.001","article-title":"Galactosylation of IgG1 modulates FcgammaRIIB-mediated inhibition of murine autoimmune hemolytic anemia","volume":"47","author":"Yamada","year":"2013","journal-title":"J. Autoimmun."},{"issue":"April","key":"10.1016\/j.smim.2018.05.003_bib0185","article-title":"ACPA IgG galactosylation associates with disease activity in pregnant patients with rheumatoid arthritis","author":"Bondt","year":"2018","journal-title":"Ann. Rheum. Dis."},{"key":"10.1016\/j.smim.2018.05.003_bib0190","doi-asserted-by":"crossref","first-page":"R193","DOI":"10.1186\/ar2892","article-title":"Immunoglobulin G galactosylation and sialylation are associated with pregnancy-induced improvement of rheumatoid arthritis and the postpartum flare: results from a large prospective cohort study","volume":"11","author":"van de Geijn","year":"2009","journal-title":"Arthritis Res. Ther."},{"key":"10.1016\/j.smim.2018.05.003_bib0195","doi-asserted-by":"crossref","first-page":"3466","DOI":"10.1074\/jbc.M210665200","article-title":"The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity","volume":"278","author":"Shinkawa","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.smim.2018.05.003_bib0200","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1007\/s13238-017-0433-3","article-title":"Glycosylation engineering of therapeutic IgG antibodies: challenges for the safety, functionality and efficacy","volume":"9","author":"Mimura","year":"2018","journal-title":"Protein Cell"},{"key":"10.1016\/j.smim.2018.05.003_bib0205","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/j.coi.2008.06.007","article-title":"Terminal sugars of Fc glycans influence antibody effector functions of IgGs","volume":"20","author":"Raju","year":"2008","journal-title":"Curr. Opin. Immunol."},{"key":"10.1016\/j.smim.2018.05.003_bib0210","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1007\/s12325-016-0451-1","article-title":"A review of obinutuzumab (GA101), a novel type II anti-CD20 monoclonal antibody, for the treatment of patients with B-cell malignancies","volume":"34","author":"Tobinai","year":"2017","journal-title":"Adv. Ther."},{"key":"10.1016\/j.smim.2018.05.003_bib0215","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1097\/MOT.0b013e328342538f","article-title":"The role of differential IgG glycosylation in the interaction of antibodies with FcgammaRs in vivo","volume":"16","author":"Anthony","year":"2011","journal-title":"Curr. Opin. Organ Transpl."},{"key":"10.1016\/j.smim.2018.05.003_bib0220","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.immuni.2005.11.010","article-title":"Fcgamma receptors: old friends and new family members","volume":"24","author":"Nimmerjahn","year":"2006","journal-title":"Immunity"},{"key":"10.1016\/j.smim.2018.05.003_bib0225","doi-asserted-by":"crossref","first-page":"3716","DOI":"10.1182\/blood-2008-09-179754","article-title":"Specificity and affinity of human fcgamma receptors and their polymorphic variants for human IgG subclasses","volume":"113","author":"Bruhns","year":"2009","journal-title":"Blood"},{"key":"10.1016\/j.smim.2018.05.003_bib0230","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.molimm.2014.06.010","article-title":"How antibodies use complement to regulate antibody responses","volume":"61","author":"Sorman","year":"2014","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.smim.2018.05.003_bib0235","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1093\/intimm\/dxx053","article-title":"Sweet SIGNs: IgG glycosylation leads the way in IVIG-mediated resolution of inflammation","volume":"29","author":"Bruckner","year":"2017","journal-title":"Int. Immunol."},{"key":"10.1016\/j.smim.2018.05.003_bib0240","doi-asserted-by":"crossref","first-page":"1698","DOI":"10.1182\/blood-2009-12-261461","article-title":"IVIg modulates BCR signaling through CD22 and promotes apoptosis in mature human B lymphocytes","volume":"116","author":"Seite","year":"2010","journal-title":"Blood"},{"key":"10.1016\/j.smim.2018.05.003_bib0245","doi-asserted-by":"crossref","first-page":"4793","DOI":"10.4049\/jimmunol.152.10.4793","article-title":"CD23\/IgE-mediated regulation of the specific antibody response in vivo","volume":"152","author":"Gustavsson","year":"1994","journal-title":"J. Immunol."},{"key":"10.1016\/j.smim.2018.05.003_bib0250","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.cell.2015.06.026","article-title":"Anti-HA glycoforms Drive B cell affinity selection and determine influenza vaccine efficacy","volume":"162","author":"Wang","year":"2015","journal-title":"Cell"},{"key":"10.1016\/j.smim.2018.05.003_bib0255","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1038\/35018508","article-title":"The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex","volume":"406","author":"Sondermann","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.smim.2018.05.003_bib0260","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1016\/S0022-2836(02)01250-0","article-title":"Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity","volume":"325","author":"Krapp","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.smim.2018.05.003_bib0265","doi-asserted-by":"crossref","first-page":"12669","DOI":"10.1073\/pnas.1108455108","article-title":"Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcgammaRIII and antibodies lacking core fucose","volume":"108","author":"Ferrara","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.smim.2018.05.003_bib0270","doi-asserted-by":"crossref","first-page":"1644","DOI":"10.1021\/bp050228w","article-title":"Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro","volume":"21","author":"Hodoniczky","year":"2005","journal-title":"Biotechnol. Prog."},{"key":"10.1016\/j.smim.2018.05.003_bib0275","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1038\/nm0395-237","article-title":"Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein","volume":"1","author":"Malhotra","year":"1995","journal-title":"Nat. Med."},{"key":"10.1016\/j.smim.2018.05.003_bib0280","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1016\/S0009-9120(99)00060-0","article-title":"Fucosylation of IgG heavy chains is increased in rheumatoid arthritis","volume":"32","author":"Gornik","year":"1999","journal-title":"Clin. Biochem."},{"key":"10.1016\/j.smim.2018.05.003_bib0285","doi-asserted-by":"crossref","first-page":"2034","DOI":"10.1016\/j.bbadis.2018.03.018","article-title":"Low galactosylation of IgG associates with higher risk for future diagnosis of rheumatoid arthritis during 10years of follow-up","volume":"1864","author":"Gudelj","year":"2018","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.smim.2018.05.003_bib0290","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1136\/annrheumdis-2014-206598","article-title":"Extensive glycosylation of ACPA-IgG variable domains modulates binding to citrullinated antigens in rheumatoid arthritis","volume":"75","author":"Rombouts","year":"2016","journal-title":"Ann. Rheum. Dis."},{"key":"10.1016\/j.smim.2018.05.003_bib0295","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1136\/annrheumdis-2013-203565","article-title":"Anti-citrullinated protein antibodies acquire a pro-inflammatory Fc glycosylation phenotype prior to the onset of rheumatoid arthritis","volume":"74","author":"Rombouts","year":"2015","journal-title":"Ann. Rheum. Dis."},{"key":"10.1016\/j.smim.2018.05.003_bib0300","doi-asserted-by":"crossref","first-page":"1620","DOI":"10.1002\/art.27414","article-title":"Glycan profiling of anti-citrullinated protein antibodies isolated from human serum and synovial fluid","volume":"62","author":"Scherer","year":"2010","journal-title":"Arthritis Rheum."},{"key":"10.1016\/j.smim.2018.05.003_bib0305","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1002\/prca.200800098","article-title":"Immunoglobulin 1 (IgG1) Fc-glycosylation profiling of anti-citrullinated peptide antibodies from human serum","volume":"3","author":"Scherer","year":"2009","journal-title":"Proteom. Clin. Appl."},{"key":"10.1016\/j.smim.2018.05.003_bib0310","doi-asserted-by":"crossref","first-page":"2978","DOI":"10.1002\/art.39273","article-title":"Association of systemic lupus erythematosus with decreased immunosuppressive potential of the IgG glycome","volume":"67","author":"Vuckovic","year":"2015","journal-title":"Arthritis Rheumatol"},{"key":"10.1016\/j.smim.2018.05.003_bib0315","doi-asserted-by":"crossref","first-page":"1794","DOI":"10.1177\/1352458516631036","article-title":"Abnormal galactosylation of immunoglobulin G in cerebrospinal fluid of multiple sclerosis patients","volume":"22","author":"Decker","year":"2016","journal-title":"Mult. Scler."},{"key":"10.1016\/j.smim.2018.05.003_bib0320","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1186\/s12974-015-0450-1","article-title":"Pro-inflammatory pattern of IgG1 Fc glycosylation in multiple sclerosis cerebrospinal fluid","volume":"12","author":"Wuhrer","year":"2015","journal-title":"J. Neuroinflammation"},{"key":"10.1016\/j.smim.2018.05.003_bib0325","doi-asserted-by":"crossref","first-page":"79","DOI":"10.2337\/dc17-1042","article-title":"N-glycan profile and kidney disease in type 1 diabetes","volume":"41","author":"Bermingham","year":"2018","journal-title":"Diabetes Care"},{"key":"10.1016\/j.smim.2018.05.003_bib0330","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1016\/0896-8411(92)90151-F","article-title":"Galactose terminating oligosaccharides of IgG in patients with primary Sjogren\u2019s syndrome","volume":"5","author":"Youinou","year":"1992","journal-title":"J. Autoimmun."},{"key":"10.1016\/j.smim.2018.05.003_bib0335","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1002\/prca.201500089","article-title":"Role of aberrant IgG glycosylation in the pathogenesis of inflammatory bowel disease","volume":"10","author":"Miyoshi","year":"2016","journal-title":"Proteom. Clin. Appl."},{"key":"10.1016\/j.smim.2018.05.003_bib0340","doi-asserted-by":"crossref","first-page":"1330","DOI":"10.1002\/elps.201400575","article-title":"Combination of IgG N-glycomics and corresponding transcriptomics data to identify anti-TNF-alpha treatment responders in inflammatory diseases","volume":"36","author":"Varadi","year":"2015","journal-title":"Electrophoresis"},{"key":"10.1016\/j.smim.2018.05.003_bib0345","doi-asserted-by":"crossref","first-page":"567","DOI":"10.3233\/JAD-131088","article-title":"Blood plasma IgG Fc glycans are significantly altered in Alzheimer\u2019s disease and progressive mild cognitive impairment","volume":"38","author":"Lundstrom","year":"2014","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.smim.2018.05.003_bib0350","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1021\/pr1004373","article-title":"IgG fc N-glycosylation changes in Lambert-Eaton myasthenic syndrome and myasthenia gravis","volume":"10","author":"Selman","year":"2011","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.smim.2018.05.003_bib0355","doi-asserted-by":"crossref","first-page":"1722","DOI":"10.1021\/pr401213z","article-title":"IgG Fc N-glycosylation in Guillain-Barre syndrome treated with immunoglobulins","volume":"13","author":"Fokkink","year":"2014","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.smim.2018.05.003_bib0360","doi-asserted-by":"crossref","first-page":"28207","DOI":"10.1038\/srep28207","article-title":"IgG1 Fc N-glycan galactosylation as a biomarker for immune activation","volume":"6","author":"de Jong","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.smim.2018.05.003_bib0365","doi-asserted-by":"crossref","first-page":"7455","DOI":"10.18632\/oncotarget.7059","article-title":"Identification of novel plasma glycosylation-associated markers of aging","volume":"7","author":"Catera","year":"2016","journal-title":"Oncotarget"},{"key":"10.1016\/j.smim.2018.05.003_bib0370","doi-asserted-by":"crossref","first-page":"2183","DOI":"10.1172\/JCI65708","article-title":"Natural variation in Fc glycosylation of HIV-specific antibodies impacts antiviral activity","volume":"123","author":"Ackerman","year":"2013","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.smim.2018.05.003_bib0375","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1002\/bit.10022","article-title":"Metabolic control of recombinant monoclonal antibody N-glycosylation in GS-NS0 cells","volume":"75","author":"Hills","year":"2001","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.smim.2018.05.003_bib0380","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1186\/s13075-016-1172-1","article-title":"Fab glycosylation of immunoglobulin G does not associate with improvement of rheumatoid arthritis during pregnancy","volume":"18","author":"Bondt","year":"2016","journal-title":"Arthritis Res. Ther."},{"key":"10.1016\/j.smim.2018.05.003_bib0385","doi-asserted-by":"crossref","first-page":"15005","DOI":"10.1073\/pnas.0808248105","article-title":"In vivo enzymatic modulation of IgG glycosylation inhibits autoimmune disease in an IgG subclass-dependent manner","volume":"105","author":"Albert","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.smim.2018.05.003_bib0390","doi-asserted-by":"crossref","first-page":"2352","DOI":"10.1007\/s00125-017-4426-9","article-title":"Increased plasma N-glycome complexity is associated with higher risk of type 2 diabetes","volume":"60","author":"Keser","year":"2017","journal-title":"Diabetologia"},{"key":"10.1016\/j.smim.2018.05.003_bib0395","doi-asserted-by":"crossref","first-page":"2240","DOI":"10.1016\/j.bbagen.2017.06.020","article-title":"IgG glycan patterns are associated with type 2 diabetes in independent European populations","volume":"1861","author":"Lemmers","year":"2017","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.smim.2018.05.003_bib0400","doi-asserted-by":"crossref","first-page":"1401","DOI":"10.1038\/nm.2862","article-title":"Anti-inflammatory activity of IgG1 mediated by Fc galactosylation and association of FcgammaRIIB and dectin-1","volume":"18","author":"Karsten","year":"2012","journal-title":"Nat. Med."},{"key":"10.1016\/j.smim.2018.05.003_bib0405","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1126\/science.1129594","article-title":"Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation","volume":"313","author":"Kaneko","year":"2006","journal-title":"Science"},{"key":"10.1016\/j.smim.2018.05.003_bib0410","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0134949","article-title":"In vitro glycoengineering of IgG1 and its effect on Fc receptor binding and ADCC activity","volume":"10","author":"Thomann","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.smim.2018.05.003_bib0415","doi-asserted-by":"crossref","first-page":"1524","DOI":"10.1016\/j.molimm.2006.09.005","article-title":"Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality","volume":"44","author":"Scallon","year":"2007","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.smim.2018.05.003_bib0420","doi-asserted-by":"crossref","first-page":"4160","DOI":"10.1172\/JCI82695","article-title":"Sialylation of IgG Fc domain impairs complement-dependent cytotoxicity","volume":"125","author":"Quast","year":"2015","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.smim.2018.05.003_bib0425","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1126\/science.1154315","article-title":"Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc","volume":"320","author":"Anthony","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.smim.2018.05.003_bib0430","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1038\/nature10134","article-title":"Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway","volume":"475","author":"Anthony","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.smim.2018.05.003_bib0435","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1097\/01.aids.0000161767.21405.68","article-title":"Increased levels of galactose-deficient IgG in sera of HIV-1-infected individuals","volume":"19","author":"Moore","year":"2005","journal-title":"AIDS"},{"issue":"433-443","key":"10.1016\/j.smim.2018.05.003_bib0440","first-page":"e414","article-title":"A functional role for antibodies in tuberculosis","volume":"167","author":"Lu","year":"2016","journal-title":"Cell"},{"key":"10.1016\/j.smim.2018.05.003_bib0445","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1097\/QAD.0b013e32835bd1f0","article-title":"Decoupling activation and exhaustion of B cells in spontaneous controllers of HIV infection","volume":"27","author":"Sciaranghella","year":"2013","journal-title":"AIDS"},{"key":"10.1016\/j.smim.2018.05.003_bib0450","doi-asserted-by":"crossref","first-page":"62","DOI":"10.3389\/fpubh.2018.00062","article-title":"Vaccines meet Big data: State-of-the-art and future prospects. From the classical 3Is (\"isolate-inactivate-inject\") vaccinology 1.0 to vaccinology 3.0, vaccinomics, and beyond: a historical overview","volume":"6","author":"Bragazzi","year":"2018","journal-title":"Front. Public Health"},{"key":"10.1016\/j.smim.2018.05.003_bib0455","doi-asserted-by":"crossref","first-page":"3788","DOI":"10.1172\/JCI65938","article-title":"T cell-independent B cell activation induces immunosuppressive sialylated IgG antibodies","volume":"123","author":"Hess","year":"2013","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.smim.2018.05.003_bib0460","doi-asserted-by":"crossref","first-page":"1647","DOI":"10.1016\/j.jaci.2012.02.037","article-title":"Tolerance induction with T cell-dependent protein antigens induces regulatory sialylated IgGs","volume":"129","author":"Oefner","year":"2012","journal-title":"J. Allergy Clin. Immunol. Pract."},{"key":"10.1016\/j.smim.2018.05.003_bib0465","doi-asserted-by":"crossref","first-page":"25","DOI":"10.3109\/08916939808993842","article-title":"Changes in the galactose content of IgG during humoral immune responses","volume":"28","author":"Lastra","year":"1998","journal-title":"Autoimmunity"},{"key":"10.1016\/j.smim.2018.05.003_bib0470","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.clinbiochem.2004.10.002","article-title":"Repeated immunization induces the increase in fucose content on antigen-specific IgG N-linked oligosaccharides","volume":"38","author":"Guo","year":"2005","journal-title":"Clin. Biochem."},{"key":"10.1016\/j.smim.2018.05.003_bib0475","doi-asserted-by":"crossref","first-page":"2329","DOI":"10.1182\/bloodadvances.2017011411","article-title":"Innate transcriptional effects by adjuvants on the magnitude, quality, and durability of HIV envelope responses in NHPs","volume":"1","author":"Francica","year":"2017","journal-title":"Blood Adv."},{"key":"10.1016\/j.smim.2018.05.003_bib0480","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1002\/iid3.22","article-title":"A pilot study showing differences in glycosylation patterns of IgG subclasses induced by pneumococcal, meningococcal, and two types of influenza vaccines","volume":"2","author":"Vestrheim","year":"2014","journal-title":"Immun., Inflamm. Dis."},{"key":"10.1016\/j.smim.2018.05.003_bib0485","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.M111.014563","article-title":"Changes in antigen-specific IgG1 Fc N-glycosylation upon influenza and tetanus vaccination","volume":"11","author":"Selman","year":"2012","journal-title":"Mol. Cell. Proteom. MCP"},{"key":"10.1016\/j.smim.2018.05.003_bib0490","doi-asserted-by":"crossref","first-page":"7648","DOI":"10.1038\/srep07648","article-title":"Glycomic signatures on serum IgGs for prediction of postvaccination response","volume":"5","author":"Wang","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.smim.2018.05.003_bib0495","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1002\/bit.1119","article-title":"Expression of GnTIII in a recombinant anti-CD20 CHO production cell line: expression of antibodies with altered glycoforms leads to an increase in ADCC through higher affinity for FC gamma RIII","volume":"74","author":"Davies","year":"2001","journal-title":"Biotechnol. Bioeng."}],"container-title":["Seminars in Immunology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S104453231830006X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S104453231830006X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,9,3]],"date-time":"2023-09-03T00:01:24Z","timestamp":1693699284000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S104453231830006X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,10]]},"references-count":99,"alternative-id":["S104453231830006X"],"URL":"https:\/\/doi.org\/10.1016\/j.smim.2018.05.003","relation":{},"ISSN":["1044-5323"],"issn-type":[{"value":"1044-5323","type":"print"}],"subject":[],"published":{"date-parts":[[2018,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Antibody glycosylation in inflammation, disease and vaccination","name":"articletitle","label":"Article Title"},{"value":"Seminars in Immunology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.smim.2018.05.003","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 The Authors. Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}]}}