T-cell surface glycoprotein CD3 epsilon chain–B-lymphocyte antigen CD20 complex (CD3ε–CD20)

The T-cell surface glycoprotein CD3 epsilon chain–B-lymphocyte antigen CD20 complex (CD3ε–CD20) is a therapeutic target formed by bispecific antibodies to treat B-cell malignancies (Nature Reviews Drug Discovery, 2019). CD3ε is a critical component of the T-cell receptor complex involved in signal transduction (UniProt P07766), while CD20 is a surface protein expressed on mature B cells (UniProt P11836). Bispecific antibodies targeting this interface bind both proteins simultaneously, creating an artificial immunological synapse between a cytotoxic T cell and a malignant B cell (PubMed: 33033267). This interaction triggers T-cell activation and the subsequent release of perforin and granzymes, leading to the lysis of the target B cell. Unlike traditional T-cell activation, this process does not require MHC-mediated antigen presentation, allowing for a broad and potent anti-tumor response. Clinically, drugs like Mosunetuzumab and Glofitamab target this interface to treat relapsed or refractory follicular lymphoma and diffuse large B-cell lymphoma (FDA.gov). However, the resulting systemic immune activation can lead to significant safety concerns, including cytokine release syndrome and neurotoxicity (ASCO Guidelines). Monitoring B-cell depletion and cytokine levels is essential for managing patients undergoing these therapies.

Other names

CD20xCD3CD3xCD20CD3e-CD20T-cell engager interfaceCD20-CD3 complex

Bispecific antibodies simultaneously bind to CD20 on B cells and CD3ε on T cells, facilitating the formation of an artificial immunological synapse. This interaction triggers T-cell activation and the release of cytotoxic granules (perforin and granzymes), leading to the targeted lysis of CD20-positive B cells (Nature Reviews Clinical Oncology, 2023).