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Specifically, some O-glycans are missing galactose that is normally \u03b21,3-linked to N-acetylgalactosamine of the core 1 glycans. These galactose-deficient IgA1 glycoforms are produced by IgA1-secreting cells due to a dysregulated expression and activity of several glycosyltransferases. Galactose-deficient IgA1 in the circulation of patients with IgA nephropathy is bound by IgG autoantibodies and the resultant immune complexes can contain additional proteins, such as complement C3. These complexes, if not removed from the circulation, can enter the glomerular mesangium, activate the resident mesangial cells, and induce glomerular injury. In this review, we briefly summarize clinical and pathological features of IgA nephropathy, review normal and aberrant IgA1 O-glycosylation pathways, and discuss the origins and potential significance of natural anti-glycan antibodies, namely those recognizing N-acetylgalactosamine. We also discuss the features of autoantibodies specific for galactose-deficient IgA1 and the characteristics of pathogenic immune complexes containing IgA1 and IgG. In IgA nephropathy, kidneys are injured by IgA1-containing immune complexes as innocent bystanders. Most patients with IgA nephropathy progress to kidney failure and require dialysis or transplantation. Moreover, most patients after transplantation experience a recurrent disease. Thus, a better understanding of the pathogenetic mechanisms is needed to develop new disease-specific treatments.<\/jats:p>","DOI":"10.1093\/glycob\/cwae060","type":"journal-article","created":{"date-parts":[[2024,8,3]],"date-time":"2024-08-03T00:19:41Z","timestamp":1722644381000},"source":"Crossref","is-referenced-by-count":16,"title":["<i>O<\/i>-glycosylation of IgA1 and the pathogenesis of an autoimmune disease IgA nephropathy"],"prefix":"10.1093","volume":"34","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9211-6670","authenticated-orcid":false,"given":"Jan","family":"Novak","sequence":"first","affiliation":[{"name":"University of Alabama at Birmingham Department of Microbiology, , 845 19th Street South, Birmingham, AL 35294,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6522-0053","authenticated-orcid":false,"given":"R Glenn","family":"King","sequence":"additional","affiliation":[{"name":"University of Alabama at Birmingham Department of Microbiology, , 845 19th Street South, Birmingham, AL 35294,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4854-2752","authenticated-orcid":false,"given":"Janet","family":"Yother","sequence":"additional","affiliation":[{"name":"University of Alabama at Birmingham Department of Microbiology, , 845 19th Street South, Birmingham, AL 35294,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4193-7305","authenticated-orcid":false,"given":"Matthew B","family":"Renfrow","sequence":"additional","affiliation":[{"name":"University of Alabama at Birmingham Department of Biochemistry and Molecular Genetics, , 720 20th Street South, Birmingham, AL 35294,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1158-4710","authenticated-orcid":false,"given":"Todd J","family":"Green","sequence":"additional","affiliation":[{"name":"University of Alabama at Birmingham Department of Microbiology, , 845 19th Street South, Birmingham, AL 35294,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2024,8,2]]},"reference":[{"issue":"35","key":"2024093023311799400_ref1","doi-asserted-by":"crossref","first-page":"8568","DOI":"10.1021\/bi00099a012","article-title":"Complete structure of the cell surface polysaccharide of Streptococcus oralis C104: a 600-MHz NMR study","volume":"30","author":"Abeygunawardana","year":"1991","journal-title":"Biochemistry"},{"issue":"7","key":"2024093023311799400_ref2","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1093\/ndt\/10.7.1121","article-title":"Abnormal glycosylation of IgA: is it related to the pathogenesis of IgA nephropathy?","volume":"10","author":"Allen","year":"1995","journal-title":"Nephrol Dial Transplant"},{"issue":"2","key":"2024093023311799400_ref3","first-page":"76","article-title":"Methodological approaches to the analysis of IgA1 O-glycosylation in IgA nephropathy","volume":"12","author":"Allen","year":"1999","journal-title":"J Nephrol"},{"issue":"3","key":"2024093023311799400_ref4","doi-asserted-by":"crossref","first-page":"470","DOI":"10.1111\/j.1365-2249.1995.tb03724.x","article-title":"Galactosylation of N- and O-linked carbohydrate moieties of IgA1 and IgG in IgA nephropathy","volume":"100","author":"Allen","year":"1995","journal-title":"Clin Exp Immunol"},{"issue":"3","key":"2024093023311799400_ref5","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1046\/j.1523-1755.2001.060003969.x","article-title":"Mesangial IgA1 in IgA nephropathy exhibits aberrant O-glycosylation: observations in three patients","volume":"60","author":"Allen","year":"2001","journal-title":"Kidney Int"},{"issue":"2","key":"2024093023311799400_ref6","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1002\/jcla.1860040208","article-title":"Impairment of jacalin binding to serum IgA in IgA nephropathy","volume":"4","author":"Andre","year":"1990","journal-title":"J Clin Lab Anal"},{"issue":"22","key":"2024093023311799400_ref7","doi-asserted-by":"crossref","first-page":"7270","DOI":"10.1016\/S0021-9258(19)42101-7","article-title":"Structure of the carbohydrate units of IgA1 immunoglobulin II. 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