Site-Specific Glycosylation Analysis of Human and Murine Fcγ Receptor II Family Members Reveals Variant-Specific N-Glycosylation.

{"sci_version": "1.2", "schema": "https://corpus.bntrg.co.uk/sci/1.0/sci.schema.json", "id": "pmid:39007905", "kind": "science-record", "revision": 2, "content_hash": "sha256:5a6abd9d3b66e4df9597e54ffa76c88ee64f989a332755daa6d0275c1dd8e0db", "created_at": "2026-11-01T20:29:05Z", "updated_at": "2026-11-01T21:33:28Z", "generator": {"name": "corpus-assay-engine", "run_id": "reading-sci-2026-11-01"}, "paper": {"state": "complete", "title": "Site-Specific Glycosylation Analysis of Human and Murine Fcγ Receptor II Family Members Reveals Variant-Specific N-Glycosylation.", "doi": "10.1021/acs.jproteome.4c00141", "pmid": "39007905", "authors": ["Zaraah Abdoollah", "Daniel E Marrero Roche", "Carlos H Pavan", "Erika Moore", "Kevin Brown Chandler"], "journal": "Journal of proteome research", "year": 2024, "abstract": "Fcγ-receptors (FcγRs) including FcγRII (CD32) gene family members are expressed on leukocytes, bind the crystallizable fragment (Fc) region of immunoglobulin G (IgG), and bridge humoral and cellular immunity. FcγRIIA and FcγRIIB have opposing roles, with the former responsible for activation and the latter for inhibition of immune cell signaling and effector functions. The extracellular domains of human and murine FcγRIIs share multiple conserved N-glycosylation sites. Understanding the role(s) of FcγRIIA and FcγRIIB glycosylation in autoimmune diseases is precluded by a lack of effective methods to study disease-associated changes in glycosylation. To address this barrier, we developed a method to assess site-specific glycosylation of human FcγRIIA and FcγRIIB, and the mouse ortholog of human FcγRIIB. Among the receptors, conserved glycosylation sites are compared, with the N144/145 site displaying predominantly complex glycans in recombinant FcγRIIs. Differences in sialylation between recombinant human FcγRIIA H/R134 (H/R131) variants at a nearby N145 N-glycosylation site are reported. Further, a potential human FcγRIIA O-glycosylation site, S179 (S212), is reported in recombinant FcγRIIA. The robust method to assess site-specific glycosylation of FcγRIIs reported here, can be utilized to study the potential role of FcγRII family glycosylation in disease. Data are available via ProteomeXchange with identifier PXD049429.", "claims": [{"id": "claim-method", "statement": "Finally, the relative abundances of glycoforms sharing a common N-glycosylation site were determined by summing all glycoform AUCs and dividing individual glycoform AUCs by the summed value. Student’s paired t tests were calculated in Microsoft Excel when suitable.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:39007905", "locator": "sections[6] \"Data Analysis\" paragraph 4", "quote": "Finally, the relative abundances of glycoforms sharing a common N-glycosylation site were determined by summing all glycoform AUCs and dividing individual glycoform AUCs by the summed value. Student’s paired t tests were calculated in Microsoft Excel when suitable."}], "state": "complete"}, {"id": "claim-data-access", "statement": "Data are available via ProteomeXchange with identifier PXD049429.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:39007905", "locator": "sections[0] \"Abstract\" paragraph 1", "quote": "Data are available via ProteomeXchange with identifier PXD049429."}], "state": "complete"}, {"id": "claim-target-result", "statement": "At site N145, hFcγRIIA H134 N-glycan compositions with sialic acid account for 11.3 ± 0.3% of the relative abundance, while hFcγRIIA R134 N-glycan compositions with sialic acid account for 39.3 ± 1.2% of the relative abundance (3.5-fold change, p = 5.5 × 10–5).", "kind": "quantitative", "target": {"value": 3.5, "unit": "fold change", "tolerance": null, "source": "At site N145, the two variants display quite distinct levels of sialic acid (Figure 6D). hFcγRIIA H134 site N145 N-glycan compositions with sialic acid account for 11.3 ± 0.3% of the relative abundance, while hFcγRIIA R134 site N145 N-glycan compositions with sialic acid account for 39.3 ± 1.2% of the relative abundance (3.5-fold change, p = 5.5 × 10–5)."}, "evidence": [{"asset": "source:pmid:39007905", "locator": "sections[13] \"Comparison of Human FcγRIIA H/R134 (H/R167) Variant Specific N- and O-Glycopeptide Relative Abundances\" paragraph 5", "quote": "At site N145, the two variants display quite distinct levels of sialic acid (Figure 6D). hFcγRIIA H134 site N145 N-glycan compositions with sialic acid account for 11.3 ± 0.3% of the relative abundance, while hFcγRIIA R134 site N145 N-glycan compositions with sialic acid account for 39.3 ± 1.2% of the relative abundance (3.5-fold change, p = 5.5 × 10–5)."}], "state": "complete"}], "gaps": []}, "experiment": {"state": "complete", "objective": "At site N145, hFcγRIIA H134 N-glycan compositions with sialic acid account for 11.3 ± 0.3% of the relative abundance, while hFcγRIIA R134 N-glycan compositions with sialic acid account for 39.3 ± 1.2% of the relative abundance (3.5-fold change, p = 5.5 × 10–5).", "steps": [{"id": "read_published_estimate", "order": 1, "name": "Read the published estimate from the source", "kind": "other", "state": "complete", "blocked_on": null, "description": "The claim, method and evidence span published with the source article.", "duration_hours": null, "parameters": {}, "inputs": ["source:pmid:39007905"], "outputs": ["the published estimate and its evidence"], "instruments": [], "reagents": []}, {"id": "obtain_source_data", "order": 2, "name": "Obtain the source data from the named repository", "kind": "data-preparation", "state": "complete", "blocked_on": null, "description": "The GEO series accession resolves and its sample accessions are listed. 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