From the Department of Pathology, Case Western Reserve University School of Medicine, Cleveland, Ohio 44107.
From the Department of Pathology, Case Western Reserve University School of Medicine, Cleveland, Ohio 44107
J Biol Chem. 2018 Mar 9;293(10):3490-3491. doi: 10.1074/jbc.H118.001955.
Immunoglobulin G (IgG) antibodies function, in part, through ligation of cell-surface Fc receptors such as FcγRIIIA (also known as CD16A). IgG glycosylation is known to impact antibody function, but the role of FcγRIIIA glycans, if any, is unclear. Patel now reveal that these glycans do impact protein conformation and IgG affinity and display cell-specific glycosylation patterns, leading to a potential model in which the affinity and possibly function of Fc receptors is dictated by the cell type and its surface glycome.
免疫球蛋白 G（IgG）抗体的功能部分通过与细胞表面 Fc 受体（如 FcγRIIIA，也称为 CD16A）的结合来实现。已知 IgG 的糖基化会影响抗体的功能，但 FcγRIIIA 聚糖的作用（如果有的话）尚不清楚。现在，Patel 等人揭示了这些聚糖确实会影响蛋白质构象和 IgG 亲和力，并表现出细胞特异性的糖基化模式，从而提出了一个潜在的模型，即 Fc 受体的亲和力和功能可能取决于细胞类型及其表面糖组。
