{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T07:32:12Z","timestamp":1790235132035,"version":"4.1.0"},"reference-count":53,"publisher":"Oxford University Press (OUP)","issue":"8","license":[{"start":{"date-parts":[[2019,4,1]],"date-time":"2019-04-01T00:00:00Z","timestamp":1554076800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2019,4,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Abs can acquire N-linked glycans in their V regions during Ag-specific B cell responses. Among others, these N-linked glycans can affect Ag binding and Ab stability. Elevated N-linked glycosylation has furthermore been associated with several B cell\u2013associated pathologies. Basic knowledge about patterns of V region glycosylation at different stages of B cell development is scarce. The aim of the current study is to establish patterns of N-glycosylation sites in Ab V regions of naive and memory B cell subsets. We analyzed the distribution and acquisition of N-glycosylation sites within Ab V regions of peripheral blood and bone marrow B cells of 12 healthy individuals, eight myasthenia gravis patients, and six systemic lupus erythematosus patients, obtained by next-generation sequencing. N-glycosylation sites are clustered around CDRs and the DE loop for both H and L chains, with similar frequencies for healthy donors and patients. No evidence was found for an overall selection bias against acquiring an N-glycosylation site, except for the CDR3 of the H chain. Interestingly, both IgE and IgG4 subsets have a 2-fold higher propensity to acquire Fab glycans compared with IgG1 or IgA. When expressed as rmAb, 35 out of 38 (92%) nongermline N-glycosylation sites became occupied. These results point toward a differential selection pressure of N-glycosylation site acquisition during affinity maturation of B cells, which depends on the location within the V region and is isotype and subclass dependent. Elevated Fab glycosylation represents an additional hallmark of TH2-like IgG4\/IgE responses.<\/jats:p>","DOI":"10.4049\/jimmunol.1801622","type":"journal-article","created":{"date-parts":[[2019,3,8]],"date-time":"2019-03-08T21:05:46Z","timestamp":1552079146000},"page":"2220-2228","source":"Crossref","is-referenced-by-count":34,"title":["Biased <i>N<\/i>-Glycosylation Site Distribution and Acquisition across the Antibody V Region during B Cell Maturation"],"prefix":"10.1093","volume":"202","author":[{"given":"Jana","family":"Koers","sequence":"first","affiliation":[{"name":"Department of Immunopathology, Sanquin Research and Landsteiner Laboratory, Amsterdam University Medical Center, University of Amsterdam , 1066 CX Amsterdam ,","place":["the Netherlands"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ninotska I L","family":"Derksen","sequence":"additional","affiliation":[{"name":"Department of Immunopathology, Sanquin Research and Landsteiner Laboratory, Amsterdam University Medical Center, University of Amsterdam , 1066 CX Amsterdam ,","place":["the Netherlands"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pleuni","family":"Ooijevaar-de Heer","sequence":"additional","affiliation":[{"name":"Department of Immunopathology, Sanquin Research and Landsteiner Laboratory, Amsterdam University Medical Center, University of Amsterdam , 1066 CX Amsterdam ,","place":["the Netherlands"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7500-5760","authenticated-orcid":false,"given":"Benjamin","family":"Nota","sequence":"additional","affiliation":[{"name":"Department of Research Facilities, Sanquin Research and Landsteiner Laboratory, Amsterdam University Medical Center, University of Amsterdam , 1066 CX Amsterdam ,","place":["the Netherlands"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fleur S","family":"van de Bovenkamp","sequence":"additional","affiliation":[{"name":"Department of Immunopathology, Sanquin Research and Landsteiner Laboratory, Amsterdam University Medical Center, University of Amsterdam , 1066 CX Amsterdam ,","place":["the Netherlands"]},{"name":"Department of Immunohematology and Blood Transfusion, Leiden University Medical Center , 2333 ZA Leiden ,","place":["the Netherlands"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5621-003X","authenticated-orcid":false,"given":"Gestur","family":"Vidarsson","sequence":"additional","affiliation":[{"name":"Department of Experimental Immunohematology, Sanquin Research and Landsteiner Laboratory, Amsterdam University Medical Center, University of Amsterdam , 1066 CX Amsterdam ,","place":["the Netherlands"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Theo","family":"Rispens","sequence":"additional","affiliation":[{"name":"Department of Immunopathology, Sanquin Research and Landsteiner Laboratory, Amsterdam University Medical Center, University of Amsterdam , 1066 CX Amsterdam ,","place":["the Netherlands"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2019,4,15]]},"reference":[{"key":"2025030417561508400_r1","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. 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