B-cell surface glycans

B-cell surface glycans are a complex array of carbohydrate structures, predominantly sialic acids, that form the glycocalyx of B-lymphocytes and play a pivotal role in immune regulation. These glycans serve as the primary ligands for Siglecs (Sialic acid-binding immunoglobulin-type lectins), particularly CD22 (Siglec-2), which is a B-cell-restricted inhibitory receptor that modulates the B-cell receptor (BCR) signaling threshold (Nitschke, 2014). By interacting with these glycans, CD22 maintains B cells in a quiescent state, preventing inappropriate activation and autoimmunity. In B-cell malignancies and certain autoimmune disorders, altered glycosylation patterns—such as increased sialylation—contribute to immune evasion by hyper-activating inhibitory Siglec pathways (Smith et al., 2023). Therapeutic approaches targeting B-cell surface glycans include the use of sialidase fusion proteins (e.g., E-602) to strip immunosuppressive sialic acids, as well as monoclonal antibodies and antibody-drug conjugates (e.g., inotuzumab ozogamicin) that target the glycan-binding receptor CD22 (Macauley et al., 2014). These strategies aim to either deplete malignant B cells or restore normal immune signaling by disrupting the sialic acid-Siglec axis.

Other names

B-cell glycocalyxB-lymphocyte surface carbohydratesSialic acid-containing glycansCD22 ligandsSiglec-2 ligandsB-cell sialosides

Modulation of B-cell receptor (BCR) signaling through the Siglec-sialic acid axis and targeted delivery of cytotoxic agents to B-cells via glycan-binding receptors.