| Autor: |
Abdoollah Z; Translational Glycobiology Institute, Department of Cellular and Molecular Medicine, Herbert Wertheim College of Medicine, Florida International University, Miami, Florida 33199, United States., Marrero Roche DE; Translational Glycobiology Institute, Department of Cellular and Molecular Medicine, Herbert Wertheim College of Medicine, Florida International University, Miami, Florida 33199, United States., Pavan CH; Translational Glycobiology Institute, Department of Cellular and Molecular Medicine, Herbert Wertheim College of Medicine, Florida International University, Miami, Florida 33199, United States., Moore E; Fischell Department of Bioengineering, University of Maryland, College Park, College Park, Maryland 20742, United States., Chandler KB; Translational Glycobiology Institute, Department of Cellular and Molecular Medicine, Herbert Wertheim College of Medicine, Florida International University, Miami, Florida 33199, United States.; Biomolecular Sciences Institute, Florida International University, 11200 SW Eighth St., Miami, Florida 33199, United States. |
| Abstrakt: |
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. |
